G alpha (12/13) signaling events (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="G alpha (12/13) signalling events" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">The G12/13 family is probably the least well characterized subtype, partly because G12/13 coupling is difficult to determine when compared with the other subtypes which predominantly rely on assay technologies that measure intracellular calcium. The G12/13 family are best known for their involvement in the processes of cell proliferation and morphology, such as stress fiber and focal adhesion formation. Interactions with Rho guanine nucleotide exchange factors (RhoGEFs) are thought to mediate many of these processes. (Buhl et al.1995, Sugimoto et al. 2003). Activation of Rho or the regulation of events through Rho is often taken as evidence of G12/13 signaling. Receptors that are coupled with G12/13 invariably couple with one or more other G protein subtypes, usually Gq. View original pathway at:[http://www.reactome.org/PathwayBrowser/#DIAGRAM=416482 Reactome].</Comment> <Comment Source="Reactome-Converter">Pathway is converted from Reactome ID: 416482</Comment> <Comment Source="Reactome-version">Reactome version: 66</Comment> <Comment Source="Reactome Author">Reactome Author: Jupe, Steve</Comment> <BiopaxRef>f30</BiopaxRef> <BiopaxRef>b7d</BiopaxRef> <Attribute Key="reactome_id" Value="416482"/> <Graphics BoardWidth="2079.0" BoardHeight="2439.0"/> <DataNode TextLabel="RHOA " GraphId="a1072" Type="Protein" GroupRef="cb777"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-422483"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="240.0" CenterY="879.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P61586"/> </DataNode> <DataNode TextLabel="SOS2 " GraphId="a10cf" Type="Protein" GroupRef="f1bcb"> <Attribute 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Type="Protein" GroupRef="e84cf"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-751003"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="380.0" CenterY="839.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P35348"/> </DataNode> <DataNode TextLabel="GNB2 " GraphId="c86f8" Type="Protein" GroupRef="d639e"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-398082"/> <Attribute Key="copies_num" Value="1202"/> <Graphics CenterX="240.0" CenterY="1599.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P62879"/> </DataNode> <DataNode TextLabel="TXA2 " GraphId="c8750" Type="Metabolite" GroupRef="e3f5a"> <Attribute Key="cellular_location" Value="extracellular region"/> <Attribute Key="complex_id" Value="R-ALL-791498"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="660.0" CenterY="879.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:15627"/> </DataNode> <DataNode TextLabel="GNA13 " GraphId="c8a8c" Type="Protein" GroupRef="abb4e"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-398056"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="959.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q14344"/> </DataNode> <DataNode TextLabel="RHOA " GraphId="ca897" Type="Protein" GroupRef="a1da2"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-5665993"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="800.0" CenterY="879.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P61586"/> </DataNode> <DataNode TextLabel="ABR " GraphId="cabbf" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="1659.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q12979"/> </DataNode> <DataNode TextLabel="ARHGEF10 " GraphId="caf87" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="2239.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O15013"/> </DataNode> <DataNode TextLabel="GNA12 " GraphId="cb7a1" Type="Protein" GroupRef="a726b"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-398145"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="240.0" CenterY="1039.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q03113"/> </DataNode> <DataNode TextLabel="GNG5 " GraphId="cb8b6" Type="Protein" GroupRef="cffb7"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-167434"/> <Attribute Key="copies_num" Value="166"/> <Graphics CenterX="660.0" CenterY="1019.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P63218"/> </DataNode> <DataNode TextLabel="GNG7 " GraphId="cc000" Type="Protein" GroupRef="b4913"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-750994"/> <Attribute Key="copies_num" Value="419"/> <Graphics CenterX="380.0" CenterY="1099.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O60262"/> </DataNode> <DataNode TextLabel="GTP " GraphId="cd88b" Type="Metabolite" GroupRef="f8fb0"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-751015"/> <Attribute Key="copies_num" Value="2"/> <Graphics CenterX="520.0" CenterY="959.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:15996"/> </DataNode> <DataNode TextLabel="ADRA1B " GraphId="cd9ec" Type="Protein" GroupRef="e84cf"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-751003"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="380.0" CenterY="859.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P35368"/> </DataNode> <DataNode TextLabel="GDP " GraphId="cdc31" Type="Metabolite" GroupRef="f6761"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-418570"/> <Attribute Key="copies_num" Value="2"/> <Graphics CenterX="100.0" CenterY="859.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:17552"/> </DataNode> <DataNode TextLabel="GNGT1 " GraphId="ce643" Type="Protein" GroupRef="cffb7"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-167434"/> <Attribute Key="copies_num" Value="606"/> <Graphics CenterX="660.0" CenterY="1179.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P63211"/> </DataNode> <DataNode TextLabel="TXA2 " GraphId="cf317" Type="Metabolite" GroupRef="e84cf"> <Attribute Key="cellular_location" Value="extracellular region"/> <Attribute Key="complex_id" Value="R-HSA-751003"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="380.0" CenterY="799.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:15627"/> </DataNode> <DataNode TextLabel="PREX1 " GraphId="cfffd" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="2159.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q8TCU6"/> </DataNode> <DataNode TextLabel="TIAM1 " GraphId="d04fe" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="1479.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q13009"/> </DataNode> <DataNode TextLabel="GTP " GraphId="d06bb" Type="Metabolite" GroupRef="abb4e"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-398056"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="979.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:15996"/> </DataNode> <DataNode TextLabel="NAd " GraphId="d06f2" Type="Metabolite" GroupRef="b4913"> <Attribute Key="cellular_location" Value="extracellular region"/> <Attribute Key="complex_id" Value="R-HSA-750994"/> <Attribute Key="copies_num" Value="1556"/> <Graphics CenterX="380.0" CenterY="1499.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:18357"/> </DataNode> <DataNode TextLabel="G-protein alpha&#10;(12/13):LARG" GraphId="d0b84" Type="Complex"> <Comment Source="Reactome">Phospholipase C activation is the classical signalling route for G alpha (q) but an additional mechanism is an inhibitory interaction between G alpha (q) and phosphatidylinositol 3-kinase alpha (PI3K alpha). There are several PI3K subtypes but only the p85 alpha/p110 alpha subtype (PI3K alpha) is a G alpha (q) effector (PMID: 18515384). Activated G alpha (q) inhibits PI3K alpha directly, in a GTP-dependent manner. G alpha(q) binding of PI3K competes with Ras, a PI3K activator (PMID: 16268778).</Comment> <Attribute Key="cellular_location" Value="plasma membrane"/> <Graphics CenterX="960.5" CenterY="82.5" Width="91.0" Height="49.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-398145"/> </DataNode> <DataNode TextLabel="GNB2 " GraphId="d0cb3" Type="Protein" GroupRef="b4913"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-750994"/> <Attribute Key="copies_num" Value="1250"/> <Graphics CenterX="380.0" CenterY="1279.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P62879"/> </DataNode> <DataNode TextLabel="ARHGEF17 " GraphId="d0e2e" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="1899.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q96PE2"/> </DataNode> <DataNode TextLabel="Ligands of GPCRs&#10;that activate&#10;G12/13" GraphId="d15b3" Type="Complex"> <Attribute Key="cellular_location" Value="extracellular region"/> <Graphics CenterX="279.5" CenterY="707.0" Width="111.0" Height="48.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a"/> <Xref Database="Reactome" ID="R-ALL-791498"/> </DataNode> <DataNode TextLabel="ARHGEF15 " GraphId="d193d" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="2279.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O94989"/> </DataNode> <DataNode TextLabel="ADRA1A " GraphId="d4431" Type="Protein" GroupRef="f8fb0"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-751015"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="520.0" CenterY="839.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P35348"/> </DataNode> <DataNode TextLabel="ROCK1,ROCK2" GraphId="d4863" Type="Complex"> <Comment Source="Reactome">ROCK I (alternatively called ROK ?) and ROCK II (also known as Rho kinase or ROK ?) were originally isolated as RhoA-GTP interacting proteins. The kinase domains of ROCK I and ROCK II are 92% identical, and so far there is no evidence that they phosphorylate different substrates. RhoA, RhoB, and RhoC associate with and activate ROCK but other GTP-binding proteins can be inhibitors, e.g. RhoE, Rad and Gem. PDK1 kinase promotes ROCK I activity not through phosphorylation but by blocking RhoE association. PLK1 can phosphorylate ROCK II and this enhances the effect of RhoA. Arachidonic acid can activate ROCK independently of Rho.</Comment> <Attribute Key="cellular_location" Value="cytosol"/> <Graphics CenterX="1892.5" CenterY="212.0" Width="57.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-419057"/> </DataNode> <DataNode TextLabel="ARHGEF38 " GraphId="d52ab" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="2359.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q9NXL2"/> </DataNode> <DataNode TextLabel="PLXNB1" GraphId="d56a0" Type="Protein"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Graphics CenterX="1062.0" CenterY="87.0" Width="54.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O43157"/> </DataNode> <DataNode TextLabel="ADR " GraphId="d5a81" Type="Metabolite" GroupRef="f8fb0"> <Attribute Key="cellular_location" Value="extracellular region"/> <Attribute Key="complex_id" Value="R-HSA-751015"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="520.0" CenterY="899.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:28918"/> </DataNode> <DataNode TextLabel="ARHGEF12 " GraphId="d6907" Type="Protein" GroupRef="a726b"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-398145"/> <Attribute Key="copies_num" Value="2"/> <Graphics CenterX="240.0" CenterY="1099.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q9NZN5"/> </DataNode> <DataNode TextLabel="ARHGEF18 " GraphId="d69cc" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="1919.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q6ZSZ5"/> </DataNode> <DataNode TextLabel="ARHGEF37 " GraphId="d6b64" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="2339.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="A1IGU5"/> </DataNode> <DataNode TextLabel="GDP" GraphId="d8541" Type="Metabolite"> <Attribute Key="cellular_location" Value="cytosol"/> <Graphics CenterX="1658.5" CenterY="220.5" Width="39.0" Height="31.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:17552"/> </DataNode> <DataNode TextLabel="GNB5 " GraphId="d9158" Type="Protein" GroupRef="cffb7"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-167434"/> <Attribute Key="copies_num" Value="822"/> <Graphics CenterX="660.0" CenterY="1279.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O14775"/> </DataNode> <DataNode TextLabel="ARHGEF5 " GraphId="d9587" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="1759.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q12774"/> </DataNode> <DataNode TextLabel="RHOC " GraphId="d9674" Type="Protein" GroupRef="cb777"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-422483"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="240.0" CenterY="919.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P08134"/> </DataNode> <DataNode TextLabel="GNG13 " GraphId="d983f" Type="Protein" GroupRef="f8fb0"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-751015"/> <Attribute Key="copies_num" Value="1083"/> <Graphics CenterX="520.0" CenterY="1179.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q9P2W3"/> </DataNode> <DataNode TextLabel="PLEKHG5 " GraphId="d9a37" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="1599.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O94827"/> </DataNode> <DataNode TextLabel="GNG11 " GraphId="d9f0d" Type="Protein" GroupRef="f8fb0"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-751015"/> <Attribute Key="copies_num" Value="867"/> <Graphics CenterX="520.0" CenterY="1139.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P61952"/> </DataNode> <DataNode TextLabel="GDP " GraphId="da1e4" Type="Metabolite" GroupRef="d639e"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-398082"/> <Attribute Key="copies_num" Value="2"/> <Graphics CenterX="240.0" CenterY="1299.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:17552"/> </DataNode> <DataNode TextLabel="GNB2 " GraphId="daa9b" Type="Protein" GroupRef="cffb7"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-167434"/> <Attribute Key="copies_num" Value="660"/> <Graphics CenterX="660.0" CenterY="1219.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P62879"/> </DataNode> <DataNode TextLabel="GTP " GraphId="db0b5" Type="Metabolite" GroupRef="d3fc5"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-114527"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="1059.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:15996"/> </DataNode> <DataNode TextLabel="G-protein alpha&#10;(13):GTP" GraphId="db3f8" Type="Complex"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Graphics CenterX="1341.5" CenterY="85.0" Width="119.0" Height="38.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-398056"/> </DataNode> <DataNode TextLabel="GNB3 " GraphId="db667" Type="Protein" GroupRef="d639e"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-398082"/> <Attribute Key="copies_num" Value="1300"/> <Graphics CenterX="240.0" CenterY="1619.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P16520"/> </DataNode> <DataNode TextLabel="GNGT1 " GraphId="db795" Type="Protein" GroupRef="d639e"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-398082"/> <Attribute Key="copies_num" Value="1103"/> <Graphics CenterX="240.0" CenterY="1559.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P63211"/> </DataNode> <DataNode TextLabel="RHOA:GTP" GraphId="ddf42" Type="Complex"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Graphics CenterX="1614.5" CenterY="150.0" Width="71.0" Height="22.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-5665993"/> </DataNode> <DataNode TextLabel="GNGT2 " GraphId="de216" Type="Protein" GroupRef="d639e"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-398082"/> <Attribute Key="copies_num" Value="603"/> <Graphics CenterX="240.0" CenterY="1459.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O14610"/> </DataNode> <DataNode TextLabel="GNG12 " GraphId="de231" Type="Protein" GroupRef="cffb7"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-167434"/> <Attribute Key="copies_num" Value="496"/> <Graphics CenterX="660.0" CenterY="1139.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q9UBI6"/> </DataNode> <DataNode TextLabel="SOS1 " GraphId="de34b" Type="Protein" GroupRef="f1bcb"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-194849"/> <Attribute Key="copies_num" Value="1"/> <Graphics CenterX="100.0" CenterY="1619.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q07889"/> </DataNode> <DataNode TextLabel="GNG7 " GraphId="de558" Type="Protein" GroupRef="f8fb0"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-751015"/> <Attribute Key="copies_num" Value="435"/> <Graphics CenterX="520.0" CenterY="1059.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O60262"/> </DataNode> <DataNode TextLabel="Ligand:GPCR&#10;complexes that&#10;activate G12/13" GraphId="de6bd" Type="Complex"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Graphics CenterX="121.5" CenterY="92.5" Width="139.0" Height="51.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="RoundedRectangle" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-751003"/> </DataNode> <DataNode TextLabel="GNG11 " GraphId="dec7d" Type="Protein" GroupRef="cffb7"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-167434"/> <Attribute Key="copies_num" Value="441"/> <Graphics CenterX="660.0" CenterY="1119.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P61952"/> </DataNode> <DataNode TextLabel="GNG10 " GraphId="def0f" Type="Protein" GroupRef="f8fb0"> <Attribute Key="cellular_location" Value="plasma membrane"/> <Attribute Key="complex_id" Value="R-HSA-751015"/> <Attribute Key="copies_num" Value="759"/> <Graphics CenterX="520.0" CenterY="1119.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P50151"/> </DataNode> <DataNode 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G alpha 12 activity appears to depend on LARG tyrosine phosphorylation by Tec-family kinases (Suzuki et al. 2003) or FAK (Chikumi et al. 2002). The involvement of LARG may be specific to particular receptor signalling pathways; RNAi-mediated knockdown of LARG specifically inhibited thrombin signaling via PAR1 but not LPA receptors (Wang et al 2004).</Comment> <BiopaxRef>e78</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="814.0" Y="137.0"/> <Point X="920.0" Y="110.0"/> <Anchor Position="0.0" Shape="None" GraphId="a2b43"/> <Anchor Position="0.99" Shape="None" GraphId="b64a7"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-398184"/> </Interaction> <Interaction GraphId="b588f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="167.0" Y="214.0" GraphRef="dd732" RelX="-0.4200000000000159" RelY="0.6700000000000159"/> <Point X="163.0" Y="257.0" GraphRef="c5f53" RelX="0.9834710743801653" RelY="0.0" ArrowHead="Arrow"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-751027"/> </Interaction> <Interaction GraphId="b71ca"> <Comment Source="Reactome">When a ligand activates a G protein-coupled receptor, it induces a conformational change in the receptor (a change in shape) that allows the receptor to function as a guanine nucleotide exchange factor (GEF), stimulating the exchange of GDP for GTP on the G alpha subunit. In the traditional view of heterotrimeric protein activation, this exchange triggers the dissociation of the now active G alpha subunit from the beta:gamma dimer, initiating downstream signalling events. The G alpha subunit has intrinsic GTPase activity and will eventually hydrolyze the attached GTP to GDP, allowing reassociation with G beta:gamma. Additional GTPase-activating proteins (GAPs) stimulate the GTPase activity of G alpha, leading to more rapid termination of the transduced signal. In some cases the downstream effector may have GAP activity, helping to deactivate the pathway. This is the case for phospholipase C beta, which possesses GAP activity within its C-terminal region (Kleuss et al. 1994).</Comment> <BiopaxRef>c81</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="730.0" Y="83.0"/> <Point X="638.0" Y="83.0"/> <Anchor Position="0.0" Shape="None" GraphId="fb349"/> <Anchor Position="0.99" Shape="None" GraphId="c8cb2"/> <Anchor Position="0.5" Shape="None" GraphId="fd472"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-418574"/> </Interaction> <Interaction GraphId="ba8d4"> <Comment Source="Reactome">LARG binds plexin-B1, a transmembrane receptor for the semaphorin Sema4D. Binding of Sema4D to plexin-B1 stimulates RhoA activation.</Comment> <BiopaxRef>dfe</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1060.0" Y="132.0"/> <Point X="1144.0" Y="114.0"/> <Anchor Position="0.0" Shape="None" GraphId="eadd7"/> <Anchor Position="0.99" Shape="None" GraphId="afbc5"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-398185"/> </Interaction> <Interaction GraphId="bc7c8"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1512.0" Y="108.0" GraphRef="eeebe" RelX="-0.008547008547008548" RelY="1.0"/> <Point X="1516.0" Y="157.0" GraphRef="e224b" RelX="-0.5" RelY="8.5" ArrowHead="mim-catalysis"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-114544"/> </Interaction> <Interaction GraphId="be545"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="177.0" Y="410.0" GraphRef="c75e2" RelX="0.0" RelY="0.6700000000000159"/> <Point X="219.0" Y="460.0" GraphRef="f0380" RelX="-1.0" RelY="-0.03225806451612903" ArrowHead="Arrow"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-751029"/> </Interaction> <Interaction GraphId="bf8ff"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="316.0" Y="540.0" GraphRef="dcfe1" RelX="1.5" RelY="0.34000000000003183"/> <Point X="387.0" Y="708.0" GraphRef="df19b" RelX="-1.0" RelY="0.0" ArrowHead="Arrow"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-751019"/> </Interaction> <Interaction GraphId="c16f6"> <Comment Source="Reactome">The liganded receptor undergoes a conformational change, generating a signal that is propagated in a manner that is not completely understood to the the G-protein. This stimulates the exchange of GDP for GTP in the G-protein alpha subunit, activating the G-protein. This event is negatively regulated by some Activators of G protein signaling (AGS) proteins, a class of proteins identified in yeast functional screens for proteins able to activate G protein signaling in the absence of a G protein–coupled receptor (GPCR) (Cismowski et al. 1999, Takesono et al. 1999). AGS proteins contain G protein regulatory (GPR) motifs (also referred to as the GoLoco motif) that bind and stabilize the Galpha subunit in its GDP-bound conformation (Mochizuki et al. 1996, Peterson et al. 2000, Cao et al. 2004, Blumer &amp; Lanier 2014). Some RGS proteins similarly bind to Galpha preventing the exchange of GDP for GTP (Soundararajan et al. 2008).</Comment> <BiopaxRef>b7d</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="177.0" Y="343.0"/> <Point X="177.0" Y="410.0"/> <Anchor Position="0.0" Shape="None" GraphId="d02a6"/> <Anchor Position="0.99" Shape="None" GraphId="c75e2"/> <Anchor Position="0.5" Shape="None" GraphId="caf73"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-751029"/> </Interaction> <Interaction GraphId="c18e8"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1700.0" Y="166.0" GraphRef="a9af9" RelX="-0.7200000000000273" RelY="0.0"/> <Point X="1658.0" Y="205.0" GraphRef="d8541" RelX="-0.02564102564102564" RelY="-1.0" ArrowHead="Arrow"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-419166"/> </Interaction> <Interaction GraphId="c3149"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="502.0" Y="88.0" GraphRef="a2a79" RelX="1.0" RelY="0.0"/> <Point X="497.0" Y="34.0" GraphRef="fb8dd" RelX="0.0" RelY="0.0"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-751039"/> </Interaction> <Interaction GraphId="c867d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="1864.0" Y="212.0" GraphRef="d4863" RelX="-1.0" RelY="0.0"/> <Point X="1817.0" Y="136.0" GraphRef="dd555" RelX="0.0" RelY="0.0"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-419049"/> </Interaction> <Interaction GraphId="c9f9c"> <Comment Source="Reactome">Guanine nucleotide exchange factors (GEFs) activate GTPases by enhancing the exchange of bound GDP for GTP. Much evidence points to GEFs being critical mediators of Rho GTPase activation (Schmidt and Hall, 2002). Many GEFs are known to be highly specific for a particular GTPase, e.g. Fgd1/Cdc42 and p115RhoGEF/Rho (Hart et al., 1996, Zheng et al., 1996). 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The active alpha subunit then participates in signaling, until its intrinsic GTPase activity degrades the bound GTP to GDP. 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Proteolytic cleavage at the C-terminus by caspase-3 and granzyme B also activates ROCK1 and ROCK2, causing plasma membrane blebbing during apoptosis (Coleman et al. 2001, Sebbagh et al. 2005). 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More importantly, the interaction between activated G alpha 13 (but not G alpha 12) triggers p115-RhoGEF activity. 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xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="f74"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">9308960</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Rho GTPases and signaling networks.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Van Aelst L, D'Souza-Schorey C.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="c12"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">11313914</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho?</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Fukuhara S, Chikumi H, Gutkind JS.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="e51"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">12101119</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Guanine nucleotide exchange factors for Rho GTPases: turning on the switch.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Schmidt A, Hall A.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="dfe"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">12123608</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Plexin-B1 directly interacts with PDZ-RhoGEF/LARG to regulate RhoA and growth cone morphology.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Swiercz JM, Kuner R, Behrens J, Offermanns S.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="c81"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">7937899</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Mechanism of GTP hydrolysis by G-protein alpha subunits.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Kleuss C, Raw AS, Lee E, Sprang SR, Gilman AG.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="b42"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">11283606</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Coleman ML, Sahai EA, Yeo M, Bosch M, Dewar A, Olson MF.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="f35"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">18577758</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Dissociation of 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Bertoglio J, Solary E, Bréard J.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="da2"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">12433842</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Galpha(12/13) mediates alpha(1)-adrenergic receptor-induced cardiac hypertrophy.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Maruyama Y, Nishida M, Sugimoto Y, Tanabe S, Turner JH, Kozasa T, Wada T, Nagao T, Kurose H.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="b7d"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">19212140</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Regulation and physiological functions of G12/13-mediated signaling pathways.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Suzuki N, Hajicek N, Kozasa T.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="f96"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">8617235</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita 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xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="e8d"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">15951850</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Siderovski DP, Willard FS.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="d96"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">8816443</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Leung T, Chen XQ, Manser E, Lim L.</bp:AUTHORS> </bp:PublicationXref> <bp:openControlledVocabulary xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#"><bp:TERM>G protein mediated signaling pathway via Galpha12/Galpha13 family</bp:TERM><bp:ID>PW:0000230</bp:ID><bp:Ontology>Pathway Ontology</bp:Ontology></bp:openControlledVocabulary></Biopax> </Pathway>

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