Role and regulation of the ER chaperone BiP

doi:10.1006/scdb.1999.0318

Seminars in Cell & Developmental Biology

Volume 10, Issue 5, October 1999, Pages 465-472

https://doi.org/10.1006/scdb.1999.0318 Get rights and content

Abstract

BiP, an HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum (ER), binds newly-synthesized proteins as they are translocated into the ER and maintains them in a state competent for subsequent folding and oligomerization. BiP is also an essential component of the translocation machinery, as well as playing a role in retrograde transport across the ER membrane of aberrant proteins destined for degradation by the proteasome. BiP is an abundant protein under all growth conditions, but its synthesis is markedly induced under conditions that lead to the accumulation of unfolded polypeptides in the ER. This attribute provides a marker for disease states that result from misfolding of secretory and transmembrane proteins.

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Regular ArticleRole and regulation of the ER chaperone BiP☆

Abstract

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BiP/Kar2p serves as a molecular chaperone during carboxypepidase Y folding in yeast

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The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocation inSaccharomyces cerevisiae

J Cell Biol

Specific molecular chaperone interactions and an ATP-dependent conformational change are required during post-translational protein translocation into the yeast ER

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Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation

Nature

Regular Article
Role and regulation of the ER chaperone BiP☆