ArticleProceedings of the National Academy of Sciences of the United States of America2026
Coordinated expression and assembly of BiP, p58
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Proper proinsulin folding in the endoplasmic reticulum (ER) is prerequisite to producing bioactive insulin, and proinsulin misfolding causing β cell ER stress accompanies pancreatic β cell dysfunction in type 2 diabetes (T2D). How (and which) ER chaperones coordinate to prevent proinsulin misfolding is largely unknown other than an unspecified dependence on the hsp70 member, BiP. A genetically engineered mouse enables efficient, specific pulldown of endogenous islet β cell BiP (GRP78, the major HSP70 ER chaperone) in complexes with client proteins. We demonstrate that BiP assembles in various protein complexes (including cochaperones p58
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