Unfolded Protein Response (Homo sapiens)

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<Pathway xmlns="http://genmapp.org/GPML/2010a" Name="Unfolded Protein Response" Organism="Homo sapiens" Data-Source="Reactome - http://www.reactome.org" Version="release 35" Author="May, B" Maintainer="May, B, Gopinathrao, G">
  <Comment Source="WikiPathways-description">The Unfolded Protein Response (UPR) is a regulatory system that protects the Endoplasmic Reticulum (ER) from overload. The UPR is provoked by the accumulation of improperly folded protein in the ER during times of unusually high secretion activity. Analysis of mutants with altered UPR, however, shows that the UPR is also required for normal development and function of secretory cells.&lt;br&gt;One level at which the URP operates is transcriptional and translational regulation: mobilization of ATF6 and IRE1 leads to increased transcription of genes encoding chaperones, and mobilization of PERK (pancreatic eIF2alpha kinase) leads to phosphorylation of the translation initiation factor eIF2alpha and global down-regulation of protein synthesis. These three regulatory pathways are annotated here.</Comment>
  <Comment Source="WikiPathways-category">Cellular Process</Comment>
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  <DataNode GraphId="n13_REACTOME_381130" TextLabel="unfolded &#10;protein&#10;" Type="Unknown">
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  <DataNode GraphId="n14_REACTOME_381168" TextLabel="ATF6-alpha:BiP &#10;Complex&#10;" Type="Complex">
    <Comment Source="WikiPathways-description">The luminal C-terminus of ATF6-alpha binds BiP, occluding  two Golgi Localization Sequences and causing ATF6-alpha to be retained in the endoplasmic reticulum.</Comment>
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  <DataNode GraphId="n15_REACTOME_381062" TextLabel="BiP:unfolded &#10;protein &#10;complex&#10;" Type="Complex">
    <Comment Source="WikiPathways-description">BiP is a chaperone which binds unfolded proteins as well as the luminal domains of UPR signal transducers ATF6, IRE1, and PERK.</Comment>
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  <DataNode GraphId="n16_REACTOME_381222" TextLabel="ATF6-alpha&#10;" Type="Protein">
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  <DataNode GraphId="n18_REACTOME_381000" TextLabel="ATF6-alpha&#10;" Type="Protein">
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  <DataNode GraphId="n20_REACTOME_420814" TextLabel="ATF6-alpha, C-terminal &#10;cleavage product of S1P&#10;" Type="Protein">
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  <DataNode GraphId="n21_REACTOME_420815" TextLabel="ATF6-alpha, N-terminal &#10;cleavage product of S1P&#10;" Type="Protein">
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  <DataNode GraphId="n22_REACTOME_381108" TextLabel="S1P&#10;" Type="Protein">
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  <DataNode GraphId="n24_REACTOME_420817" TextLabel="ATF6-alpha, C-&#10;terminal cleavage &#10;product of S2P&#10;" Type="Protein">
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  <DataNode GraphId="n25_REACTOME_381075" TextLabel="ATF6-alpha, N-&#10;terminal cleavage &#10;product of S2P&#10;" Type="Protein">
    <Comment Source="WikiPathways-description">ATF6-alpha is cleaved by S1P after amino acid 419 (RHLL). It is also cleaved by S2P at an unknown site. The product of cleavage is about 50 kd.</Comment>
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  <DataNode GraphId="n47_REACTOME_420841" TextLabel="NF-YA&#10;" Type="Protein">
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  <DataNode GraphId="n49_REACTOME_381202" TextLabel="IRE1:BiP &#10;Complex&#10;" Type="Complex">
    <Comment Source="WikiPathways-description">The luminal N-teminal domain of IRE1 binds the ATPase domain of BiP, rendering IRE1 inactive.</Comment>
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  <DataNode GraphId="n50_REACTOME_381076" TextLabel="IRE1&#10;" Type="Protein">
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  <DataNode GraphId="n56_REACTOME_381200" TextLabel="IRE1 &#10;homodimer&#10;" Type="Complex">
    <Comment Source="WikiPathways-description">Crystallographic evidence indicates that the IRE1 homodimer forms by an initial interaction between the luminal N-terminal domains of IRE1 monomers.</Comment>
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  <DataNode GraphId="n58_REACTOME_113592" TextLabel="ATP&#10;" Type="Metabolite">
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  <DataNode GraphId="n59_REACTOME_381154" TextLabel="IRE1 homodimer &#10;(phosphorylated)&#10;" Type="Complex">
    <Comment Source="WikiPathways-description">After juxtaposition of the luminal N-termini of IRE1 to form the IRE1 homodimer, the cytoplasmic C-terminal kinase domains of the IRE1 molecules associate and transphosphorylate each other's A-loop domains. This causes a change in conformation that allows binding of ADP.</Comment>
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  <DataNode GraphId="n60_REACTOME_29370" TextLabel="ADP&#10;" Type="Metabolite">
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  <DataNode GraphId="n63_REACTOME_381078" TextLabel="IRE1 homodimer &#10;(phosphorylated):&#10;ADP&#10;" Type="Complex">
    <Comment Source="WikiPathways-description">Phosphorylated IRE1 homodimers preferentially bind ADP (as opposed to ATP) and this binding promotes association of the cytoplasmic C-termini. Crystallographic evidence indicates that unphosphorylated A-loops of IRE1 interfere with nucleotide binding thus trans-autophosphorylation is a prerequisite to nucleotide binding.</Comment>
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  <DataNode GraphId="n68_REACTOME_381096" TextLabel="XBP1(S)&#10;" Type="Protein">
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  <DataNode GraphId="n70_REACTOME_535579" TextLabel="Proteins &#10;Upregulated &#10;by XBP1(S)&#10;" Type="Protein">
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  <DataNode GraphId="n71_REACTOME_349523" TextLabel="Vacuolar &#10;ATPase &#10;subunit D1&#10;" Type="Protein">
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    <Comment Source="WikiPathways-description">Members of this set have been demonstrated to be upregulated by the transcription factor XBP1(S) in humans. Candidate members of this set are inferred from experimental results in mice.</Comment>
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  <DataNode GraphId="n90_REACTOME_381216" TextLabel="PERK:BiP &#10;Heterodimer&#10;" Type="Complex">
    <Comment Source="WikiPathways-description">The N-terminal luminal domain of PERK binds BiP, rendering PERK inactive.</Comment>
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  <DataNode GraphId="n102_REACTOME_381126" TextLabel="PERK &#10;Homodimer&#10;" Type="Complex">
    <Comment Source="WikiPathways-description">PERK monomers form dimers, resulting in activation of the kinase activity of the cytosolic C-terminal region.</Comment>
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  <DataNode GraphId="n108_REACTOME_72510" TextLabel="eIF2-alpha&#10;" Type="Protein">
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  <DataNode GraphId="n117_REACTOME_381016" TextLabel="ATF4&#10;" Type="Protein">
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  <DataNode GraphId="n132_REACTOME_535543" TextLabel="Cyclic AMP-dependent &#10;transcription factor ATF-3&#10;" Type="Protein">
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  <DataNode GraphId="n134_REACTOME_70597" TextLabel="Asparagine &#10;synthetase&#10;" Type="Protein">
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  <DataNode GraphId="n145_REACTOME_381204" TextLabel="NF-Y&#10;" Type="Complex">
    <Comment Source="WikiPathways-description">NF-Y is a ubiquitous heterotrimeric transcription factor comprising subunits NF-Y A, NF-Y B, and NF-Y C. It binds the sequence CCAAT.</Comment>
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    <Comment Source="WikiPathways-description">ATF6-alpha is a transmembrane protein located in the endoplasmic reticulum (ER) membrane with N-terminal cytoplasmic and C-terminal luminal domains. BiP binds the luminal domain of ATF6-alpha via the substrate binding domain of BiP. Binding of BiP blocks 2 Golgi localization sequences on ATF6-alpha, maintaining ATF6-alpha in the ER. &lt;br&gt; BiP is also a general chaperone capable of binding unfolded proteins in the ER lumen. When chaperone activity in the ER is overwhelmed, BiP dissociates from ATF6-alpha and binds the excess unfolded proteins. It is unclear whether the dissociation is due to competition of unfolded proteins for BiP or to a more specific interaction between BiP and ATF6-alpha. The dissociation exposes the Golgi localization sequences of ATF6-alpha and allows ATF6-alpha to transit to the Golgi.</Comment>
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    <Comment Source="WikiPathways-description">The association between ATF6-alpha and BiP causes ATF6-alpha to be retained in the endoplasmic reticulum (ER). Once dissociated from BiP, the 2 Golgi Localization Sequences on ATF6-alpha are exposed and ATF6-alpha transits from the ER to the Golgi Apparatus.</Comment>
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    <Comment Source="WikiPathways-description">IRE1-alpha is a single-pass transmembrane protein with a luminal N-terminus and a cytoplasmic C-terminus. IRE1-alpha is maintained in an inactive state in the Endoplasmic Reticulum (ER) membrane by interaction between the luminal domain of IRE1-alpha and the ATPase domain of BiP within the ER. &lt;br&gt;BiP is a general chaperone that also binds unfolded proteins within the ER. Thus BiP dissociates from IRE1-alpha when chaperone activity is overwhelmed by unfolded proteins in the ER.</Comment>
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    <Comment Source="WikiPathways-description">Xbp-1 (S) binds the sequence CCACG in ER Stress Responsive Elements (ERSE, consensus sequence CCAAT (N)9 CCACG) located upstream from many genes. The ubiquitous transcription factor NF-Y, a heterotrimer, binds the CCAAT portion of the ERSE and together the IRE1-alpha: NF-Y complex activates transcription of a set of chaperone genes including DNAJB9, EDEM, RAMP4, p58IPK, and others. This results in an increase in protein folding activity in the ER.</Comment>
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