Difference between revisions of "Endoplasmic stress"

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(Autoloading by CXLParser)
(Autoloading by CXLParser)
 
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(.//.)<html><!--Pop-up for: TRAF2 !Pop-up-->
 
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</div>(...)<!--Pop-up for: Transport to the nucleus !Pop-up-->
 
</div>(...)<!--Pop-up for: Transport to the nucleus !Pop-up-->
 
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<div class="1J1L8R47S-23R784G-D8N" style="display:none;">
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<div class="1J1L87CZ6-14Q64NP-C3S" style="display:none;">
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</div>(...)<!--Pop-up for: Transportation of ATF6 (P)  Into Golgi apparatus !Pop-up-->
 
</div>(...)<!--Pop-up for: Transportation of ATF6 (P)  Into Golgi apparatus !Pop-up-->
 
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</div>(...)<!--Pop-up for: Oxidative stress !Pop-up-->
 
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<div class="1J1L6Y32G-NVBWJS-9JD" style="display:none;">
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</div>(...)<!--Pop-up for: Bak/Bak in membrane of  Endoplasmic reticulum !Pop-up-->
 
</div>(...)<!--Pop-up for: Bak/Bak in membrane of  Endoplasmic reticulum !Pop-up-->
 
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</div>(...)<!--Pop-up for: ATF6(P) !Pop-up-->
 
</div>(...)<!--Pop-up for: ATF6(P) !Pop-up-->
 
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<div class="1J1KLRQ4V-2DY8ZHL-W6" style="display:none;">
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</div>(...)<!--Pop-up for: Peptidyl-proline  Isomerase !Pop-up-->
 
</div>(...)<!--Pop-up for: Peptidyl-proline  Isomerase !Pop-up-->
 
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<div class="1N9Z51VF9-2BZK5TV-29ZR" style="display:none;">
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</div>(...)<!--Pop-up for: Serum  Amyloid P !Pop-up-->
 
</div>(...)<!--Pop-up for: Serum  Amyloid P !Pop-up-->
 
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<div class="1N9Z3VGH0-NZJFNX-2BYH" style="display:none;">
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</div>(...)<!--Pop-up for: Transmembrane endoplasmic  Stress sensors !Pop-up-->
 
</div>(...)<!--Pop-up for: Transmembrane endoplasmic  Stress sensors !Pop-up-->
 
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<div class="1J1KLND8T-711B2D-PR" style="display:none;">
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<h3>Transmembrane endoplasmic  Stress sensors</h3>
 
<h3>Transmembrane endoplasmic  Stress sensors</h3>
<div class="links"><a href=" ">Transmembrane endoplasmic  Stress sensors</a><br /></div>
+
<div class="links"><a href="No links!"></a><br /><a href=" ">Transmembrane endoplasmic  Stress sensors</a><br /></div>
 
</div>(...)<!--Pop-up for: Impaired ability to attach proteins to native conformation !Pop-up-->
 
</div>(...)<!--Pop-up for: Impaired ability to attach proteins to native conformation !Pop-up-->
 
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<div class="1J1L81LBN-M79PVB-BQZ" style="display:none;">
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</div>(...)<!--Pop-up for: IRE1 !Pop-up-->
 
</div>(...)<!--Pop-up for: IRE1 !Pop-up-->
 
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<div class="1J1KLQK5X-1FQPL6B-TL" style="display:none;">
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</div>(...)<!--Pop-up for: Reduced energy status of cells !Pop-up-->
 
</div>(...)<!--Pop-up for: Reduced energy status of cells !Pop-up-->
 
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<div class="1J1L7Z5JL-5DFMBX-BMY" style="display:none;">
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</div>(...)<!--Pop-up for: Proteolysis of ATF6 (P)  !Pop-up-->
 
</div>(...)<!--Pop-up for: Proteolysis of ATF6 (P)  !Pop-up-->
 
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</div>(...)<!--Pop-up for: Gene Expression !Pop-up-->
 
</div>(...)<!--Pop-up for: Gene Expression !Pop-up-->
 
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</div>(...)<!--Pop-up for: Misfolded proteins  In ER lumen !Pop-up-->
 
</div>(...)<!--Pop-up for: Misfolded proteins  In ER lumen !Pop-up-->
 
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<div class="1J1KL4FH3-12MNT6Z-JK" style="display:none;">
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</div>(...)<!--Pop-up for: Glutathione  Biosynthesis !Pop-up-->
 
</div>(...)<!--Pop-up for: Glutathione  Biosynthesis !Pop-up-->
 
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<div class="1N9Z52TSV-1ST6Z0W-2B08" style="display:none;">
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<div class="1J1KMBJ3Q-1PJYLYG-178" style="display:none;">
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</div>(...)<!--Pop-up for: IkB !Pop-up-->
 
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</div>(...)<!--Pop-up for: Reduced load due newly  Synthesized proteins !Pop-up-->
 
</div>(...)<!--Pop-up for: Reduced load due newly  Synthesized proteins !Pop-up-->
 
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<div class="1J1L50JT3-26Y2Q90-6MN" style="display:none;">
 +
  
  
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<h3>Reduced load due newly  Synthesized proteins</h3>
 
<h3>Reduced load due newly  Synthesized proteins</h3>
<div class="links"><a href=" ">Reduced load due newly  Synthesized proteins</a><br /></div>
+
<div class="links"><a href="No links!"></a><br /><a href=" ">Reduced load due newly  Synthesized proteins</a><br /></div>
 
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</div>(...)<!--Pop-up for: Ca2+-ATPase 2 !Pop-up-->
 
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<div class="1J1KMYRT6-24ZTD7M-1CK" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Restoration of damaged proteins !Pop-up-->
 
</div>(...)<!--Pop-up for: Restoration of damaged proteins !Pop-up-->
 
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<div class="1J1L63KFN-1HR5BJW-7TZ" style="display:none;">
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</div>(...)<!--Pop-up for: Protein disulfide  Isomerase PDI !Pop-up-->
 
</div>(...)<!--Pop-up for: Protein disulfide  Isomerase PDI !Pop-up-->
 
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 +
  
  
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 +
  
  
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</div>(...)<!--Pop-up for: ATF6 !Pop-up-->
 
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<div class="1N9Z2VJS8-1QJT8NW-28Q4" style="display:none;">
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<div class="1J1LB1CJ3-11J313N-FWQ" style="display:none;">
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</div>(...)<!--Pop-up for: Further accumulation of  Misfolded proteins !Pop-up-->
 
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<div class="1N9Z3KZ6X-29DG3HW-2994" style="display:none;">
 +
  
  
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<h3>Further accumulation of  Misfolded proteins</h3>
 
<h3>Further accumulation of  Misfolded proteins</h3>
<div class="links"><a href=" ">Further accumulation of  Misfolded proteins</a><br /></div>
+
<div class="links"><a href="No links!"></a><br /><a href=" ">Further accumulation of  Misfolded proteins</a><br /></div>
 
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</div>(...)<!--Pop-up for: Apoptosis !Pop-up-->
 
<div class="1J1KP35CX-1LLB537-2DJ" style="display:none;">
 
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<div class="1J1L3DHLD-1WL4CD4-61M" style="display:none;">
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</div>(...)<!--Pop-up for: Resuming  Translation  Genes !Pop-up-->
 
</div>(...)<!--Pop-up for: Resuming  Translation  Genes !Pop-up-->
 
<div class="1N9Z52BQD-1GM48LV-2B00" style="display:none;">
 
<div class="1N9Z52BQD-1GM48LV-2B00" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Ca2+ release from  Endoplasmic reticulum !Pop-up-->
 
</div>(...)<!--Pop-up for: Ca2+ release from  Endoplasmic reticulum !Pop-up-->
 
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<div class="1J1KP29JR-1J6VW3X-29K" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: ATF4 !Pop-up-->
 
</div>(...)<!--Pop-up for: ATF4 !Pop-up-->
 
<div class="1J1KPQVS8-26PMWCH-2SV" style="display:none;">
 
<div class="1J1KPQVS8-26PMWCH-2SV" style="display:none;">
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</div>(...)<!--Pop-up for: Stress response  Genes expression !Pop-up-->
 
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<div class="1J1KN4BV3-187B51F-1FJ" style="display:none;">
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</div>(...)<!--Pop-up for: EIF2a !Pop-up-->
 
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<div class="1J1KPPQ2Y-1V1DCB-2RT" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: PERC !Pop-up-->
 
</div>(...)<!--Pop-up for: PERC !Pop-up-->
 
<div class="1J1KLR9FP-J1C5ZV-VJ" style="display:none;">
 
<div class="1J1KLR9FP-J1C5ZV-VJ" style="display:none;">
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</div>(...)<!--Pop-up for: Calcium into mitochondria !Pop-up-->
 
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<div class="1J1KQBTD0-1Q9KMKN-3JC" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Alpha-/beta- secretases of  Endoplasmic reticulum/Golgi !Pop-up-->
 
</div>(...)<!--Pop-up for: Alpha-/beta- secretases of  Endoplasmic reticulum/Golgi !Pop-up-->
 
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<div class="1J1KNH1TY-18HDT79-1W6" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: PERC !Pop-up-->
 
</div>(...)<!--Pop-up for: PERC !Pop-up-->
 
<div class="1N9Z2VDKL-246BRHS-28Q0" style="display:none;">
 
<div class="1N9Z2VDKL-246BRHS-28Q0" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Endoplasmic stress !Pop-up-->
 
</div>(...)<!--Pop-up for: Endoplasmic stress !Pop-up-->
 
<div class="1P03B0KCK-M3RDSM-2S1" style="display:none;">
 
<div class="1P03B0KCK-M3RDSM-2S1" style="display:none;">
 +
  
 
<h3>Endoplasmic stress</h3>
 
<h3>Endoplasmic stress</h3>
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</div>(...)<!--Pop-up for: GRP78/BiP binds to defective protein  And dissociates from IRE1, PERC, ATF6 !Pop-up-->
 
</div>(...)<!--Pop-up for: GRP78/BiP binds to defective protein  And dissociates from IRE1, PERC, ATF6 !Pop-up-->
 
<div class="1J1KLHSZJ-19BBWRR-PM" style="display:none;">
 
<div class="1J1KLHSZJ-19BBWRR-PM" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: NRF2 !Pop-up-->
 
</div>(...)<!--Pop-up for: NRF2 !Pop-up-->
 
<div class="1J1LBDKKP-25TS5HH-GGC" style="display:none;">
 
<div class="1J1LBDKKP-25TS5HH-GGC" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Caspase 12 !Pop-up-->
 
</div>(...)<!--Pop-up for: Caspase 12 !Pop-up-->
 
<div class="1J1L37043-9DGJ4F-5QW" style="display:none;">
 
<div class="1J1L37043-9DGJ4F-5QW" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Assembly of active  Apoptosome !Pop-up-->
 
</div>(...)<!--Pop-up for: Assembly of active  Apoptosome !Pop-up-->
 
<div class="1J1KQB2PC-19VQ3VH-3H6" style="display:none;">
 
<div class="1J1KQB2PC-19VQ3VH-3H6" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Release of cytochrome c  From mitochondria !Pop-up-->
 
</div>(...)<!--Pop-up for: Release of cytochrome c  From mitochondria !Pop-up-->
 
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<div class="1J1KQ73R2-1JNCSKN-3D9" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Amino acids  Importing !Pop-up-->
 
</div>(...)<!--Pop-up for: Amino acids  Importing !Pop-up-->
 
<div class="1N9Z52L0V-264WD7Q-2B04" style="display:none;">
 
<div class="1N9Z52L0V-264WD7Q-2B04" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: ATF6(N) !Pop-up-->
 
</div>(...)<!--Pop-up for: ATF6(N) !Pop-up-->
 
<div class="1J1L6B1MJ-1M0R0S2-86D" style="display:none;">
 
<div class="1J1L6B1MJ-1M0R0S2-86D" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Overloading of  Endoplasmic reticulum  By proteins !Pop-up-->
 
</div>(...)<!--Pop-up for: Overloading of  Endoplasmic reticulum  By proteins !Pop-up-->
 
<div class="1J1L6TD90-1V65FXM-958" style="display:none;">
 
<div class="1J1L6TD90-1V65FXM-958" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Elimination of misfolded proteins from  ER by ubiquitin-proteasome system !Pop-up-->
 
</div>(...)<!--Pop-up for: Elimination of misfolded proteins from  ER by ubiquitin-proteasome system !Pop-up-->
 
<div class="1J1L60T2G-1BP9GNP-7QF" style="display:none;">
 
<div class="1J1L60T2G-1BP9GNP-7QF" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Caspase 4 !Pop-up-->
 
</div>(...)<!--Pop-up for: Caspase 4 !Pop-up-->
 
<div class="1J1LB8VFM-13DYXS9-G8C" style="display:none;">
 
<div class="1J1LB8VFM-13DYXS9-G8C" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: CHOP/GADD153 !Pop-up-->
 
</div>(...)<!--Pop-up for: CHOP/GADD153 !Pop-up-->
 
<div class="1J1KPRMXS-16R8J8G-2TJ" style="display:none;">
 
<div class="1J1KPRMXS-16R8J8G-2TJ" style="display:none;">
 +
  
  
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</div>(...)<!--Pop-up for: Translation !Pop-up-->
 
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Latest revision as of 09:26, 2 August 2015

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

Endoplasmic stress

The endoplasmic reticulum is responsible for much of a cell’s protein synthesis and folding, but it also has an important role in sensing cellular stress. The endoplasmic reticulum (ER) is the site of synthesis, folding and modification of secretory and cell-surface proteins, as well as the resident proteins of the secretory pathway. The quality control machinery in the ER operates in conjunction with protein folding pathways and is so selective that even relatively minor perturbations in the efficiency of protein folding can cause the rejection of nascent proteins as misfolded and, consequently, the accumulation or degradation of these proteins. Thus, the ER also contains resident molecules with a primary function of sensing protein misfolding in this organelle and initiating changes in gene expression, which impact the folding capacity of the ER.

The accumulation of unfolded proteins in the lumen of the endoplasmic reticulum (ER) induces a coordinated adaptive program called the unfolded protein response (UPR). The UPR alleviates stress by upregulating protein folding and degradation pathways in the ER and inhibiting protein synthesis. Physiological conditions that induce the UPR by causing protein misfolding include: the differentiation and development of professional secretory cells, such as plasma or pancreatic b cells; altered metabolic conditions, such as glucose deprivation, hyperhomocysteinemia and ischemia; mutations in the genes encoding secretory or transmembrane proteins, which normally fold in the ER, such as a-1 antitrypsin and insulin; and infection by certain pathogens, such as hepatitis C. To date, three ER-resident transmembrane proteins have been identified as proximal sensors of the presence of ER stress: the kinase and endoribonuclease IRE1 (a and b), the PERK kinase and the basic leucine-zipper transcription factor ATF6 (a and b). In the cases of IRE1 and PERK, which both have cytoplasmic serine/threonine kinase domains, ER stress induces lumenal-domaindriven homodimerization, autophosphorylation and activation. The activation of all three components of the UPR depends on the dissociation of the proximal signaling molecule from the abundant lumenal chaperone BiP. The combined effects of the activation of these molecules are an upregulation of genes encoding proteins that are involved in the secretory pathway, such as ER-resident chaperones and proteins involved in ER-associated protein degradation, and a downregulation of protein synthesis, reducing the influx of nascent proteins into the ER. Sustained unresolved ER stress leads to apoptosis.

Aging linked declines in expression and activity of key ER molecular chaperones and folding enzymes compromise proper protein folding and the adaptive response of the UPR. One mechanism to explain age-associated declines in cellular functions and age-related diseases is a progressive failure of chaperoning systems. In many of these diseases, proteins or fragments of proteins convert from their normally soluble forms to insoluble fibrils or plaques that accumulate in a variety of organs including the liver, brain or spleen. This group of diseases, which typically occur late in life includes Alzheimer's, Parkinson's, type II diabetes and a host of less well known but often equally serious conditions such as fatal familial insomnia. The UPR is implicated in many of these neurodegenerative and familial protein folding diseases as well as several cancers and a host of inflammatory diseases including diabetes, atherosclerosis, inflammatory bowel disease and arthritis.