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GRP94 in ER quality control and stress responses
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The best recognized role of gp96 is in the folding and assembly of membrane proteins of the secretory pathway.
“Gp96 has several biological functions, of which the best recognized is its role in the folding and assembly of membrane proteins of the secretory pathway.”
Gp96 is a ubiquitously expressed chaperone and the only ER resident member of the HSP90 family.
“Gp96 (also known as gpr94 or HSP90b1) is a ubiquitously expressed chaperone and the only ER resident member of the HSP90 family.1”
In the absence of gp96, membrane proteins of the secretory pathway are targeted for ER-associated degradation (ERAD).
“In the absence of gp96 these proteins are targeted for ER-associated degradation (ERAD).1”
The known gp96 clients, integrins and TLRs, fail to reach the cell surface in the absence of gp96 due to misfolding; it is therefore likely that LDLR family members are similarly affected in the absence of gp96.
“The known gp96 clients, integrins and TLRs, fail to reach the cell surface in the absence of gp96 due to misfolding1−8—it is therefore likely that LDLR family members are similarly affected in the absence of gp96.”
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Research works printed but not linked: 92
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Metadata
- Authors
- Eletto, D., Dersh, D., & Argon, Y.
- Venue
- Seminars in Cell & Developmental Biology
- Publisher
- Elsevier BV
- Published
- 2010-07
- Volume
- 21
- Issue
- 5
- Pages
- 479-485
- ISSN
- 1084-9521
- Cited by
- 209
- References
- 0
- Language
- en
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