HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum.
Sign Up to like & getrecommendations! Published in 2017 at "Gene"
DOI: 10.1016/j.gene.2017.03.005
Abstract: The HSPA5 gene encodes the binding immunoglobulin protein (BiP), an Hsp70 family chaperone localized in the ER lumen. As a highly conserved molecular chaperone, BiP assists in a wide range of folding processes via its… read more here.
Keywords: protein; hspa5 gene; chaperone bip; bip ... See more keywords
Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
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DOI: 10.1038/s41467-021-22596-0
Abstract: To adapt to fluctuating protein folding loads in the endoplasmic reticulum (ER), the Hsp70 chaperone BiP is reversibly modified with adenosine monophosphate (AMP) by the ER-resident Fic-enzyme FICD/HYPE. The structural basis for BiP binding and… read more here.
Keywords: tpr motifs; chaperone bip; motifs ficd; ampylation ... See more keywords
Infancy‐onset diabetes caused by de‐regulated AMPylation of the human endoplasmic reticulum chaperone BiP
Sign Up to like & getrecommendations! Published in 2023 at "EMBO Molecular Medicine"
DOI: 10.15252/emmm.202216491
Abstract: Dysfunction of the endoplasmic reticulum (ER) in insulin‐producing beta cells results in cell loss and diabetes mellitus. Here we report on five individuals from three different consanguineous families with infancy‐onset diabetes mellitus and severe neurodevelopmental… read more here.
Keywords: endoplasmic reticulum; onset diabetes; infancy onset; bip ... See more keywords