Response of EIF2AK4 (GCN2) to amino acid deficiency (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="Response of EIF2AK4 (GCN2) to amino acid deficiency" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">EIF2AK4 (GCN2) senses amino acid deficiency by binding uncharged tRNAs near the ribosome and responds by phosphorylating EIF2S1, the alpha subunit of the translation initiation factor EIF2 (inferred from yeast homologs and mouse homologs, reviewed in Chaveroux et al. 2010, Castilho et al. 2014, Gallinetti et al. 2013, Bröer and Bröer 2017, Wek 2018). Phosphorylated EIF2S1 reduces translation of most mRNAs but increases translation of downstream ORFs in mRNAs such as ATF4 that contain upstream ORFs (inferred from mouse homologs in Vattem and Wek 2004, reviewed in Hinnebusch et al. 2016, Sonenberg and Hinnebusch 2009). ATF4, in turn, activates expression of genes involved in responding to amino acid deficiency such as DDIT3 (CHOP), ASNS (asparagine synthetase), CEBPB, and ATF3 (reviewed in Kilberg et al. 2012, Wortel et al. 2017). In mice, EIF2AK4 in the brain may responsible for avoidance of diets lacking essential amino acids (Hao et al. 2005, Maurin et al. 2005, see also Leib and Knight 2015, Gietzen et al. 2016, reviewed in Dever and Hinnebusch 2005).&lt;br&gt;EIF2AK4 is bound to both the ribosome and GCN1, which is required for activation of EIF2AK4 and may act by shuttling uncharged tRNAs from the A site of the ribosome to EIF2AK4. Upon binding tRNA, EIF2AK4 trans-autophosphorylates. Phosphorylated EIF2AK4 then phosphorylates EIF2S1 on serine-52, the same serine residue phosphorylated by other kinases of the integrated stress response: EIF2AK1 (HRI, activated by heme deficiency and other stresses), EIF2AK2 (PKR, activated by double-stranded RNA), and EIF2AK3 (PERK, activated by unfolded proteins) (reviewed in Hinnebusch 1994, Wek et al. 2006, Donnelly et al. 2013, Pakos-Zebrucka et al. 2016, Wek 2018), View original pathway at [http://www.reactome.org/PathwayBrowser/#DIAGRAM=9633012 Reactome].</Comment> <Comment Source="Reactome-Converter">Pathway is converted from Reactome ID: 9633012</Comment> <Comment Source="Reactome-version">Reactome version: 73</Comment> <Comment Source="Reactome Author">Reactome Author: May, Bruce</Comment> <BiopaxRef>ad9</BiopaxRef> <BiopaxRef>a2e</BiopaxRef> <BiopaxRef>ddc</BiopaxRef> <BiopaxRef>ffc</BiopaxRef> <BiopaxRef>d3b</BiopaxRef> <BiopaxRef>fe7</BiopaxRef> <BiopaxRef>e6c</BiopaxRef> <BiopaxRef>cad</BiopaxRef> 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<Graphics CenterX="100.0" CenterY="2123.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P46778" /> </DataNode> <DataNode TextLabel="EIF2S2 " GraphId="bf370" Type="Protein" GroupRef="f9194"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9633006" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1223.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P20042" /> </DataNode> <DataNode TextLabel="RPL27 " GraphId="bf4ed" Type="Protein" GroupRef="f4479"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9633013" /> <Attribute Key="copies_num" Value="21" /> <Graphics CenterX="240.0" CenterY="2203.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P61353" /> </DataNode> <DataNode 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GroupRef="a56d0"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9633821" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1583.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P61247" /> </DataNode> <DataNode TextLabel="5S rRNA " GraphId="ce42f" Type="Protein" GroupRef="e5600"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9634665" /> <Attribute Key="copies_num" Value="27" /> <Graphics CenterX="660.0" CenterY="2663.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="EMBL" ID="V00589" /> </DataNode> <DataNode TextLabel="RPS7 " GraphId="ce6b6" Type="Protein" GroupRef="f4479"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9633013" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="240.0" CenterY="1643.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62081" /> </DataNode> <DataNode TextLabel="RPLP2 " GraphId="ce702" Type="Protein" GroupRef="a56d0"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9633821" /> <Attribute Key="copies_num" Value="23" /> <Graphics CenterX="380.0" CenterY="1883.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P05387" /> </DataNode> <DataNode TextLabel="RPL23A " GraphId="ce78f" Type="Protein" GroupRef="e3f29"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9633014" /> <Attribute Key="copies_num" Value="19" /> <Graphics CenterX="100.0" CenterY="2163.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62750" /> </DataNode> <DataNode TextLabel="ATF4" 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/> <Attribute Key="complex_id" Value="R-HSA-9633821" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="380.0" CenterY="1483.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62979" /> </DataNode> <DataNode TextLabel="RPL32 " GraphId="d4034" Type="Protein" GroupRef="a0c39"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9634679" /> <Attribute Key="copies_num" Value="25" /> <Graphics CenterX="520.0" CenterY="2523.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62910" /> </DataNode> <DataNode TextLabel="RPS27 " GraphId="d418e" Type="Protein" GroupRef="e3f29"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9633014" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1743.0" Width="100.0" Height="20.0" ZOrder="32768" 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<Graphics CenterX="100.0" CenterY="2283.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62888" /> </DataNode> <DataNode TextLabel="28S rRNA " GraphId="fda70" Type="Protein" GroupRef="e3f29"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9633014" /> <Attribute Key="copies_num" Value="19" /> <Graphics CenterX="100.0" CenterY="2703.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="EMBL" ID="M11167" /> </DataNode> <DataNode TextLabel="RPL11 " GraphId="fdc4d" Type="Protein" GroupRef="a56d0"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9633821" /> <Attribute Key="copies_num" Value="23" /> <Graphics CenterX="380.0" CenterY="1923.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62913" /> </DataNode> <DataNode 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Value="R-HSA-9634679" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1663.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62854" /> </DataNode> <DataNode TextLabel="RPS26 " GraphId="ff806" Type="Protein" GroupRef="e3f29"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9633014" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="100.0" CenterY="1463.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P62854" /> </DataNode> <DataNode TextLabel="EIF2S1 " GraphId="ff9d9" Type="Protein" GroupRef="fb7ef"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-72515" /> <Attribute Key="copies_num" Value="1" /> <Graphics CenterX="520.0" CenterY="1123.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P05198" /> </DataNode> <DataNode TextLabel="RPLP2 " GraphId="ffe99" Type="Protein" GroupRef="a0c39"> <Attribute Key="cellular_location" Value="cytosol" /> <Attribute Key="complex_id" Value="R-HSA-9634679" /> <Attribute Key="copies_num" Value="25" /> <Graphics CenterX="520.0" CenterY="2083.0" Width="100.0" Height="20.0" ZOrder="32768" FontSize="10" Valign="Middle" /> <Xref Database="Uniprot-TrEMBL" ID="P05387" /> </DataNode> <Interaction GraphId="a14ca"> <Comment Source="Reactome">IMPACT, a mammalian homolog of yeast YIH1, competes with EIF2AK4 (GCN2) for binding to GCN1, which is required for activation of EIF2AK4 and may act by transferring unacylated tRNAs from the ribosome to EIF2AK4 (inferred from mouse homologs). IMPACT thereby inhibits phosphorylation of EIF2A by EIF2AK4 in response to amino acid deficiency (inferred from mouse homologs). IMPACT is preferentially expressed in neurons, associates with translating ribosomes, enhances translation initiation, and promotes neuritogenesis (inferred from mouse homologs).</Comment> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="93.0" Y="265.0" /> <Point X="93.0" Y="316.0" /> <Anchor Position="0.0" Shape="None" GraphId="a9056" /> <Anchor Position="0.99" Shape="None" GraphId="e69d0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9634669" /> </Interaction> <Interaction GraphId="a1e32"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="410.0" Y="739.0" GraphRef="e7b6e" RelX="0.9753086419753086" RelY="-0.0196078431372549" /> <Point X="420.0" Y="716.0" GraphRef="ca8e8" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1791118" /> </Interaction> <Interaction GraphId="a3278"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="524.0" Y="584.0" GraphRef="cd4cb" RelX="0.5800000000000409" RelY="-0.01999999999998181" /> <Point X="527.0" Y="582.0" GraphRef="a4ed3" RelX="-1.0" RelY="-0.04" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635892" /> </Interaction> <Interaction GraphId="a37b1"> <Comment Source="Reactome">The Asparagine Synthetase (ASNS) gene is transcribed to yield mRNA and the mRNA is translated to yield protein (Chen et al. 2004, Lee et al. 2008, Gjymishka et al. 2009, Sikalidis et al. 2011, Balasubramanian et al. 2013, inferred from the mouse homolog). Transcription of ASNS is activated by the unfolded protein response (Gjymishka et al. 2009), amino acid deficiency (Chen et al. 2004, Lee et al. 2008, Sikalidis et al. 2011, Balasubramanian et al. 2013, inferred from the mouse homolog), and heme deficiency (inferred from the mouse homolog).</Comment> <BiopaxRef>b2a</BiopaxRef> <BiopaxRef>bc9</BiopaxRef> <BiopaxRef>b6c</BiopaxRef> <BiopaxRef>e53</BiopaxRef> <BiopaxRef>aec</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="420.0" Y="716.0" /> <Point X="829.0" Y="722.0" /> <Anchor Position="0.0" Shape="None" GraphId="ca8e8" /> <Anchor Position="0.99" Shape="None" GraphId="a1cc5" /> <Anchor Position="0.5" Shape="None" GraphId="cef2e" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1791118" /> </Interaction> <Interaction GraphId="a3c46"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="430.0" Y="474.0" GraphRef="ff9d1" RelX="0.4200000000000159" RelY="-0.01999999999998181" /> <Point X="433.0" Y="474.0" GraphRef="edce9" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635804" /> </Interaction> <Interaction GraphId="a496f"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="588.0" Y="140.0" GraphRef="f775b" RelX="-1.0" RelY="0.0" /> <Point X="554.0" Y="173.0" GraphRef="a79b9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9633742" /> </Interaction> <Interaction GraphId="a62b7"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="403.0" Y="846.0" GraphRef="c87c9" RelX="0.9770114942528736" RelY="-0.0196078431372549" /> <Point X="413.0" Y="823.0" GraphRef="e9ef8" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635918" /> </Interaction> <Interaction GraphId="a70e6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="94.0" Y="210.0" GraphRef="bad49" RelX="-0.008695652173913044" RelY="1.0" /> <Point X="93.0" Y="265.0" GraphRef="a9056" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9634669" /> </Interaction> <Interaction GraphId="a753e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="430.0" Y="636.0" GraphRef="f9f03" RelX="1.0" RelY="-0.0196078431372549" /> <Point X="466.0" Y="586.0" GraphRef="b0501" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635892" /> </Interaction> <Interaction GraphId="a96f9"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="232.0" Y="380.0" GraphRef="e571b" RelX="-1.0" RelY="-0.04" /> <Point X="163.0" Y="473.0" GraphRef="f6bb4" RelX="-16.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-381128" /> </Interaction> <Interaction GraphId="a9a62"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="544.0" Y="514.0" GraphRef="c63ad" RelX="1.6000000000000227" RelY="0.029999999999972715" /> <Point X="547.0" Y="516.0" GraphRef="e57fc" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9644926" /> </Interaction> <Interaction GraphId="a9b2b"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="829.0" Y="722.0" GraphRef="a1cc5" RelX="4.089999999999918" RelY="0.05999999999994543" /> <Point X="832.0" Y="723.0" GraphRef="aa779" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1791118" /> </Interaction> <Interaction GraphId="aa12d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="663.0" Y="516.0" GraphRef="e57fc" RelX="0.9829059829059829" RelY="0.0" /> <Point X="667.0" Y="514.0" GraphRef="fcdd0" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9650722" /> </Interaction> <Interaction GraphId="ab2ba"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="360.0" Y="271.0" GraphRef="bb965" RelX="-1.0" RelY="0.0" /> <Point X="330.0" Y="293.0" GraphRef="b4898" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9633008" /> </Interaction> <Interaction GraphId="ab2d1"> <Comment Source="Reactome">The TRIB3 (TRB3, NIPK) gene is transcribed to yield mRNA and the mRNA is translated to yield TRIB3 protein (Ohoka et al. 2005, Ord and Ord 2005, Lee et al. 2008, Sikalidis et al. 2011, Ord et al. 2016, and inferred from the mouse homolog). Transcription of TRIB3 is enhanced in response to amino acid deficiency (Lee et al. 2008, Sikalidis et al. 2011, and inferred from mouse homologs), endoplasmic reticulum stress (Ohoka et al. 2005, Ord and Ord 2005), oxidative stress (Ord and Ord 2005, Ord et al. 2016) and heme deficiency (inferred from mouse homologs). ATF4 bound with a CEBP family protein to the promoter of TRIB3 (NIPK, TRB3) enhances transcription of TRIB3 (Ohoka et al. 2005, Ord and Ord 2005, Lee et al. 2008, Sikalidis et al. 2011, Ord et al. 2016, and inferred from mouse homologs).</Comment> <BiopaxRef>b19</BiopaxRef> <BiopaxRef>f84</BiopaxRef> <BiopaxRef>e53</BiopaxRef> <BiopaxRef>aec</BiopaxRef> <BiopaxRef>ad5</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="384.0" Y="955.0" /> <Point X="731.0" Y="955.0" /> <Anchor Position="0.0" Shape="None" GraphId="c1859" /> <Anchor Position="0.99" Shape="None" GraphId="f7079" /> <Anchor Position="0.5" Shape="None" GraphId="ef673" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635912" /> </Interaction> <Interaction GraphId="ab529"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="488.0" Y="683.0" GraphRef="d98ed" RelX="-1.0" RelY="0.0" /> <Point X="696.0" Y="719.0" GraphRef="cef2e" RelX="71.5" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1791118" /> </Interaction> <Interaction GraphId="ab617"> <Comment Source="Reactome">The ATF3 gene is transcribed to yield mRNA and the mRNA is translated to yield protein (Chen et al. 2004, Pan et al. 2007, Lee et al. 2008, Armstrong et al. 2010, Sikalidis et al. 2011, Fu and Kilberg 2013, Lee et al. 2013, Hayner et al. 2018). Transcription of ATF3 is enhanced in response to amino acid deficiency (Chen et al. 2004, Pan et al. 2007, Lee et al. 2008, Sikaldis et al. 2011, Fu and Kilberg 2013, Hayner et al. 2018). ATF4 binds a CEBP-ATF response element (CARE) and an additional upstream element in the promoter of the ATF3 gene, resulting in enhanced transcription (Pan et al. 2007, Armstrong et al. 2010, Fu and Kilberg 2013, Lee et al. 2013, Hayner et al. 2018, and inferred from mouse homologs). CEBPB and ATF3 bind later and correlate with reduced expression of ATF4 (Pan et al. 2007)</Comment> <BiopaxRef>fa3</BiopaxRef> <BiopaxRef>cbc</BiopaxRef> <BiopaxRef>a57</BiopaxRef> <BiopaxRef>fac</BiopaxRef> <BiopaxRef>ff7</BiopaxRef> <BiopaxRef>b6c</BiopaxRef> <BiopaxRef>e53</BiopaxRef> <BiopaxRef>aec</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="439.0" Y="613.0" /> <Point X="737.0" Y="615.0" /> <Anchor Position="0.0" Shape="None" GraphId="b4ea2" /> <Anchor Position="0.99" Shape="None" GraphId="a6e49" /> <Anchor Position="0.5" Shape="None" GraphId="f7070" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1791173" /> </Interaction> <Interaction GraphId="ad580"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="480.0" Y="785.0" GraphRef="ec282" RelX="-1.0" RelY="-0.037037037037037035" /> <Point X="680.0" Y="821.0" GraphRef="ee419" RelX="114.5" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635918" /> </Interaction> <Interaction GraphId="b0c5b"> <Comment Source="Reactome">ATF4 binds an amino acid response element (AARE) in the promoter of the ATF3 gene (Chen et al. 2004, Pan et al. 2007, Fu and Kilberg 2013, Hayner et al. 2018). ATF4 initially binds the ATF3 promoter with phosphorylated ATF2, then with JUN (c-Jun), then with CEBPB (Fu and Kilberg 2013, Hayner et al. 2018). ATF3 and CEBPB bind later and correlate with reduced expression of ATF3 (Pan et al. 2007, Fu and Kilberg 2013, Hayner et al. 2018).</Comment> <BiopaxRef>b6c</BiopaxRef> <BiopaxRef>ff7</BiopaxRef> <BiopaxRef>fac</BiopaxRef> <BiopaxRef>cbc</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="466.0" Y="586.0" /> <Point X="524.0" Y="584.0" /> <Anchor Position="0.0" Shape="None" GraphId="b0501" /> <Anchor Position="0.99" Shape="None" GraphId="cd4cb" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635892" /> </Interaction> <Interaction GraphId="b260a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="504.0" Y="144.0" GraphRef="e700b" RelX="1.0" RelY="-0.02564102564102564" /> <Point X="554.0" Y="173.0" GraphRef="a79b9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9633742" /> </Interaction> <Interaction GraphId="b2f8e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="504.0" Y="144.0" GraphRef="e700b" RelX="1.0" RelY="-0.02564102564102564" /> <Point X="554.0" Y="198.0" GraphRef="aada5" RelX="0.0" RelY="1.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9633742" /> </Interaction> <Interaction GraphId="b30e2"> <Comment Source="Reactome">ATF4 binds an enhancer downstream of the protein coding region of the CEBPB gene (Chen et al. 2005). The binding site resembles a composite CEBP-ATF element. Therefore ATF4 may form a heterodimer with a CEBP protein at the element (Chen et al. 2005).</Comment> <BiopaxRef>d73</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="419.0" Y="791.0" /> <Point X="477.0" Y="788.0" /> <Anchor Position="0.0" Shape="None" GraphId="e2fd1" /> <Anchor Position="0.99" Shape="None" GraphId="e0a29" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635936" /> </Interaction> <Interaction GraphId="b98af"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="270.0" Y="476.0" GraphRef="ce901" RelX="1.0" RelY="0.0" /> <Point X="466.0" Y="586.0" GraphRef="b0501" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635892" /> </Interaction> <Interaction GraphId="bc928"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="330.0" Y="342.0" GraphRef="c513f" RelX="0.0" RelY="0.4900000000000091" /> <Point X="332.0" Y="368.0" GraphRef="e571b" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9633008" /> </Interaction> <Interaction GraphId="bceb1"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="270.0" Y="476.0" GraphRef="ce901" RelX="1.0" RelY="0.0" /> <Point X="431.0" Y="686.0" GraphRef="ca8e9" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635915" /> </Interaction> <Interaction GraphId="bd0bb"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="485.0" Y="685.0" GraphRef="f25e7" RelX="0.5400000000000205" RelY="-0.009999999999990905" /> <Point X="488.0" Y="683.0" GraphRef="d98ed" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635915" /> </Interaction> <Interaction GraphId="be992"> <Comment Source="Reactome">The promoter of the DDIT3 (CHOP) gene contains an Amino Acid Response Element (AARE) that binds ATF4 and ATF2. ATF2 and ATF4 are required for full activation of gene transcription in response to amino acid deprivation (Bruhat et al. 2000, Averous et al. 2004). Phospho-ATF2 is essential in the acetylation of histone H4 and H2B (Bruhat et al. 2007). ATF4 recruits PCAF to enhance transcription (Chérasse et al. 2007). ATF4 appears to be a monomer in the absence of DNA and a dimer after binding DNA (Podust et al. 2001).</Comment> <BiopaxRef>ce5</BiopaxRef> <BiopaxRef>eff</BiopaxRef> <BiopaxRef>e0e</BiopaxRef> <BiopaxRef>d16</BiopaxRef> <BiopaxRef>b56</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="388.0" Y="476.0" /> <Point X="430.0" Y="474.0" /> <Anchor Position="0.0" Shape="None" GraphId="ffe66" /> <Anchor Position="0.99" Shape="None" GraphId="ff9d1" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9635804" /> </Interaction> <Interaction GraphId="c0182"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="83.0" Y="232.0" GraphRef="b1b21" RelX="1.0" RelY="0.0" /> <Point X="93.0" Y="265.0" GraphRef="a9056" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9634669" /> </Interaction> <Interaction GraphId="c17c3"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="430.0" Y="636.0" GraphRef="f9f03" RelX="1.0" RelY="-0.0196078431372549" /> <Point X="439.0" Y="613.0" GraphRef="b4ea2" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1791173" /> </Interaction> <Interaction GraphId="c221d"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="331.0" Y="241.0" GraphRef="f0d29" RelX="0.0" RelY="0.92" /> <Point X="330.0" Y="293.0" GraphRef="b4898" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9633008" /> </Interaction> <Interaction GraphId="c3dad"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="527.0" Y="582.0" GraphRef="a4ed3" RelX="-1.0" RelY="-0.04" /> <Point X="691.0" Y="613.0" GraphRef="f7070" RelX="103.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1791173" /> </Interaction> <Interaction GraphId="c447a"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="433.0" Y="474.0" GraphRef="edce9" RelX="-1.0" RelY="0.0" /> <Point X="515.0" Y="514.0" GraphRef="b6d11" RelX="51.0" RelY="1.5" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9644926" /> </Interaction> <Interaction GraphId="c5472"> <Comment Source="Reactome">The DDIT3 (CHOP) gene is transcribed to yield mRNA and the mRNA is translated to yield protein (Bartlett et al. 1992, Carlson et al. 1993, Bruhat et al. 1997, Yoshida et al. 2000, Lee et al. 2008, Sikalidis et al. 2011). In response to amino acid starvation, transcription of DDIT3 s enhanced by ATF4 and phosphorylated ATF2 (Bruhat et al. 2000, Averous et al. 2004, Bruhat et al. 2007)</Comment> <BiopaxRef>e0e</BiopaxRef> <BiopaxRef>b59</BiopaxRef> <BiopaxRef>e53</BiopaxRef> <BiopaxRef>aec</BiopaxRef> <BiopaxRef>d16</BiopaxRef> <BiopaxRef>b56</BiopaxRef> <BiopaxRef>dc8</BiopaxRef> <BiopaxRef>d4a</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="384.0" Y="511.0" /> <Point X="544.0" Y="514.0" /> <Anchor Position="0.0" Shape="None" GraphId="a37c0" /> <Anchor Position="0.99" Shape="None" GraphId="c63ad" /> <Anchor Position="0.5" Shape="None" GraphId="b6d11" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-9644926" /> </Interaction> <Interaction GraphId="c7694"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="737.0" Y="615.0" GraphRef="a6e49" RelX="2.980000000000018" RelY="0.01999999999998181" /> <Point X="740.0" Y="617.0" GraphRef="a769b" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1791173" /> </Interaction> <Interaction GraphId="c98c1"> <Comment Source="Reactome">ATF4 mRNA is translated to yield ATF4 protein, which then transits to the nucleus (Blais et al. 2004, Ross et al. 2018). The mRNA of ATF4 contains 2 upstream ORFs (uORFs) (Ross et al. 2018 and inferred from the mouse homolog). The second uORF overlaps the ORF encoding ATF4 and thus prevents translation of ATF4. When EIF2S1 (eIF2-alpha) is phosphorylated, translation initiation is decreased overall, translation of the uORFs is suppressed, and translation of the ORF encoding ATF4 is increased (Blais et al. 2004, Ross et al. 2018, and inferred from mouse homologs).</Comment> <BiopaxRef>a71</BiopaxRef> <BiopaxRef>df7</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="141.0" Y="473.0" /> <Point X="217.0" Y="475.0" /> <Anchor Position="0.0" Shape="None" GraphId="c5f87" /> <Anchor Position="0.99" Shape="None" GraphId="c1d86" /> <Anchor Position="0.5" Shape="None" GraphId="f6bb4" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-381128" /> </Interaction> <Interaction GraphId="ca608"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="731.0" Y="955.0" GraphRef="f7079" RelX="3.4700000000000273" RelY="0.0" /> <Point X="734.0" Y="955.0" GraphRef="b9e4d" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref 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histidyl-tRNA synthetase-like domain of EIF2AK4 (GCN2) binds uncharged tRNA, resulting in activation of the protein kinase domain of EIF2AK4 (Inglis et al. 2019 and inferred from yeast homologs and mouse homologs). 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Return to Response of EIF2AK4 (GCN2) to amino acid deficiency (Homo sapiens).