Regulation of cholesterol biosynthesis by SREBP (SREBF) (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="Regulation of cholesterol biosynthesis by SREBP (SREBF)" Data-Source="Reactome - http://www.reactome.org" Version="56" Author="May, Bruce" Maintainer="May, Bruce" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">Sterol regulatory element binding proteins (SREBPs, SREBFs) respond to low cholesterol concentrations by transiting to the nucleus and activating genes involved in cholesterol and lipid biosynthesis (reviewed in Brown and Goldstein 2009, Osborne and Espenshade 2009, Weber et al. 2004).&lt;br&gt; Newly synthesized SREBPs are transmembrane proteins that bind SCAP in the endoplasmic reticulum (ER) membrane. SCAP binds cholesterol which causes a conformational change that allows SCAP to interact with INSIG, retaining the SCAP:SREBP complex in the ER. INSIG binds oxysterols, which cause INSIG to bind SCAP and retain SCAP:SREBP in the endoplasmic reticulum.&lt;br&gt;In low cholesterol (below about 5 mol%) SCAP no longer interacts with cholesterol or INSIG and binds Sec24 of the CopII coat complex instead. Thus SCAP:SREBP transits with the CopII complex from the ER to the Golgi. In the Golgi SREBP is cleaved by S1P and then by S2P, releasing the N-terminal fragment of SREBP into the cytosol. The N-terminal fragment is imported to the nucleus by importin-beta and then acts with other factors, such as SP1 and NF-Y, to activate transcription of target genes. Targets of SREBP include the genes encoding all enzymes of cholesterol biosynthesis and several genes involved in lipogenesis. SREBP2 most strongly activates cholesterol biosynthesis while SREBP1C most strongly activates lipogenesis. View original pathway at:[http://www.reactome.org/PathwayBrowser/#DIAGRAM=1655829 Reactome].</Comment> <Comment Source="Reactome Converter">Pathway is converted from Reactome id: </Comment> <BiopaxRef>f76</BiopaxRef> <BiopaxRef>b1b</BiopaxRef> <BiopaxRef>eb9</BiopaxRef> <Attribute Key="reactome_id" Value="1655829"/> <Graphics BoardWidth="1301.0" BoardHeight="1621.0"/> <DataNode TextLabel="SREBP1A,1C,2:SCAP:Cop II Coat" GraphId="ff302" Type="Complex"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Graphics CenterX="619.5" CenterY="100.0" Width="211.0" Height="24.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-1655765"/> </DataNode> <DataNode TextLabel="GTP " GraphId="a95ca" Type="Metabolite" GroupRef="aed50"> <Attribute Key="cellular_location" Value="cytosol"/> <Attribute Key="complex_id" Value="R-HSA-1655765"/> <Attribute Key="copies_num" Value="4"/> <Graphics CenterX="100.0" 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membrane"/> <Attribute Key="complex_id" Value="R-HSA-1655765"/> <Attribute Key="copies_num" Value="19"/> <Graphics CenterX="100.0" CenterY="901.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O94855"/> </DataNode> <DataNode TextLabel="SEC23A " GraphId="a1b4b" Type="Protein" GroupRef="aed50"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" Value="R-HSA-1655765"/> <Attribute Key="copies_num" Value="22"/> <Graphics CenterX="100.0" CenterY="921.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q15436"/> </DataNode> <DataNode TextLabel="SCAP " GraphId="a283f" Type="Protein" GroupRef="aed50"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" Value="R-HSA-1655765"/> <Attribute Key="copies_num" Value="25"/> <Graphics CenterX="100.0" CenterY="941.0" 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Type="Protein" GroupRef="e0024"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" Value="R-HSA-2317522"/> <Attribute Key="copies_num" Value="4"/> <Graphics CenterX="380.0" CenterY="1201.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P36956-1"/> </DataNode> <DataNode TextLabel="SREBF1-3 " GraphId="ce6eb" Type="Protein" GroupRef="e0024"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" Value="R-HSA-2317522"/> <Attribute Key="copies_num" Value="7"/> <Graphics CenterX="380.0" CenterY="1221.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P36956-3"/> </DataNode> <DataNode TextLabel="SREBF2(1-1141) " GraphId="d8477" Type="Protein" GroupRef="e0024"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" 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FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="O15503"/> </DataNode> <DataNode TextLabel="INSIG2 " GraphId="f0fe6" Type="Protein" GroupRef="e0024"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" Value="R-HSA-2317522"/> <Attribute Key="copies_num" Value="19"/> <Graphics CenterX="380.0" CenterY="1301.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q9Y5U4"/> </DataNode> <DataNode TextLabel="oxysterol " GraphId="b6f5b" Type="Metabolite" GroupRef="e0024"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" Value="R-HSA-2317522"/> <Attribute Key="copies_num" Value="22"/> <Graphics CenterX="380.0" CenterY="1321.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:53030"/> </DataNode> <DataNode TextLabel="KPNB1" GraphId="d5167" Type="Protein"> <Attribute Key="cellular_location" Value="cytosol"/> <Graphics CenterX="903.0" CenterY="539.0" Width="116.0" Height="24.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q14974"/> </DataNode> <DataNode TextLabel="SREBP1A,1C,2:SCAP" GraphId="e491d" Type="Complex"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Graphics CenterX="214.5" CenterY="51.0" Width="149.0" Height="28.0" ZOrder="32768" FontSize="10" Valign="Middle" ShapeType="Hexagon" Color="a52a2a"/> <Xref Database="Reactome" ID="R-HSA-2317520"/> </DataNode> <DataNode TextLabel="SCAP " GraphId="c5e71" Type="Protein" GroupRef="dfc85"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" Value="R-HSA-2317520"/> <Attribute Key="copies_num" Value="4"/> <Graphics CenterX="380.0" CenterY="1381.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q12770"/> </DataNode> <DataNode TextLabel="SREBF1-1 " GraphId="b7de5" Type="Protein" GroupRef="dfc85"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" Value="R-HSA-2317520"/> <Attribute Key="copies_num" Value="7"/> <Graphics CenterX="380.0" CenterY="1401.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P36956-1"/> </DataNode> <DataNode TextLabel="SREBF1-3 " GraphId="dc5c5" Type="Protein" GroupRef="dfc85"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" Value="R-HSA-2317520"/> <Attribute Key="copies_num" Value="10"/> <Graphics CenterX="380.0" CenterY="1421.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="P36956-3"/> </DataNode> <DataNode TextLabel="SREBF2(1-1141) " GraphId="d0ebb" Type="Protein" GroupRef="dfc85"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Attribute Key="complex_id" Value="R-HSA-2317520"/> <Attribute Key="copies_num" Value="13"/> <Graphics CenterX="380.0" CenterY="1441.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle"/> <Xref Database="Uniprot-TrEMBL" ID="Q12772"/> </DataNode> <DataNode TextLabel="CHOL" GraphId="ab8da" Type="Metabolite"> <Attribute Key="cellular_location" Value="endoplasmic reticulum membrane"/> <Graphics CenterX="412.5" CenterY="165.0" Width="81.0" Height="30.0" ZOrder="32768" FontSize="10" Valign="Middle" Color="0000ff"/> <Xref Database="ChEBI" ID="CHEBI:16113"/> </DataNode> <DataNode TextLabel="Activation of gene&#10;expression by SREBF&#10;(SREBP)" GraphId="a1ca9" Type="Pathway"> <Comment Source="Reactome">After transiting to the nucleus SREBPs (SREBP1A/1C/2, SREBFs) bind short sequences, sterol regulatory elements (SREs), in the promoters of target genes (reviewed in Eberle et al. 2004, Weber et al. 2004). SREBPs alone are relatively weak activators of transcription, with SREBP1C being significantly weaker than SREBP1A or SREBP2. In combination with other transcription factors such as SP1 and NF-Y the SREBPs are much stronger activators. SREBP1C seems to more specifically target genes involved in fatty acid synthesis while SREBP2 seems to target genes involved in cholesterol synthesis (Pai et al. 1998).</Comment> <BiopaxRef>dc5</BiopaxRef> <BiopaxRef>cea</BiopaxRef> <BiopaxRef>eb9</BiopaxRef> <Attribute Key="org.pathvisio.DoubleLineProperty" Value="Double"/> <Graphics CenterX="285.5" CenterY="632.5" Width="343.0" Height="75.0" ZOrder="32768" FontSize="10" Valign="Middle" LineThickness="0.0" Color="14961e"/> <Xref Database="Reactome" ID="R-HSA-2426168"/> </DataNode> <Interaction GraphId="df643"> <Comment Source="Reactome">SREBPs (SREBP1A, SREBP1C, SREBP2, also known as SREBFs) are transmembrane proteins that bind SCAP in the endoplasmic reticulum membrane. In the presence of cholesterol or oxysterols SCAP:SREBP1A/1C/2 binds INSIG and is retained in the endoplasmic reticulum. At cholesterol concentrations below 5 mol% SCAP changes conformation, SCAP:SREBP1A/1C/2 loses interaction with INSIG, binds the CopII coat complex, and is translocated to the Golgi.</Comment> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="448.0" Y="50.0"/> <Point X="593.0" Y="85.0"/> <Anchor Position="0.0" Shape="None" GraphId="ab41c"/> <Anchor Position="0.99" Shape="None" GraphId="f381e"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-1655825"/> </Interaction> <Interaction GraphId="d0c63"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="477.0" Y="91.0" GraphRef="c12da" RelX="1.0" RelY="-0.037037037037037035"/> <Point X="448.0" Y="50.0" GraphRef="ab41c" RelX="0.0" RelY="0.0"/> </Graphics> <Xref Database="Reactome" ID="R-HSA-1655825"/> </Interaction> <Interaction GraphId="e3414"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="288.0" Y="51.0" GraphRef="e491d" 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rdf:datatype="http://www.w3.org/2001/XMLSchema#string">10805775</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">Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Ye J, Davé UP, Grishin NV, Goldstein JL, Brown MS.</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="c05"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">10644685</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">Biosynthesis and enzymatic characterization of human SKI-1/S1P and the processing of its inhibitory prosegment.</bp:TITLE> 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rdf:datatype="http://www.w3.org/2001/XMLSchema#string">11283257</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">Dimerization of sterol regulatory element-binding protein 2 via the helix-loop-helix-leucine zipper domain is a prerequisite for its nuclear localization mediated by importin beta.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Nagoshi E, Yoneda Y.</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="b44"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">14645851</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 structure of importin-beta bound to SREBP-2: nuclear import of a transcription factor.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Lee SJ, Sekimoto T, Yamashita E, Nagoshi E, Nakagawa A, Imamoto N, Yoshimura M, Sakai H, Chong KT, Tsukihara T, Yoneda Y.</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="ffb"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">9634703</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">Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 A resolution.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Párraga A, Bellsolell L, Ferré-D'Amaré AR, Burley SK.</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="b1b"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">19933148</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">Evolutionary conservation and adaptation in the mechanism that regulates SREBP action: what a long, strange tRIP it's been.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Osborne TF, Espenshade PJ.</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="ed8"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">8156598</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">SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Wang X, Sato R, Brown MS, Hua X, Goldstein JL.</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="cf2"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">12242332</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">Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Yabe D, Brown MS, Goldstein JL.</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="f39"> <bp:ID 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Evidence from in vivo competition studies.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Sakai J, Nohturfft A, Goldstein JL, Brown MS.</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="f76"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">18974038</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">Cholesterol feedback: from Schoenheimer's bottle to Scap's MELADL.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Brown MS, Goldstein JL.</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="aa3"> <bp:ID 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S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Rawson RB, Zelenski NG, Nijhawan D, Ye J, Sakai J, Hasan MT, Chang TY, Brown MS, Goldstein JL.</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="b03"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">17428920</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">Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Radhakrishnan A, Ikeda Y, Kwon HJ, Brown MS, Goldstein JL.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref 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