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Co-chaperones of the mammalian endoplasmic reticulum.

Authors
Type
Published Article
Journal
Sub-cellular biochemistry
Publication Date
Volume
78
Pages
179–200
Identifiers
DOI: 10.1007/978-3-319-11731-7_9
PMID: 25487022
Source
Medline

Abstract

In mammalian cells, the rough endoplasmic reticulum or ER plays a central role in the biogenesis of most extracellular plus many organellar proteins and in cellular calcium homeostasis. Therefore, this organelle comprises molecular chaperones that are involved in import, folding/assembly, export, and degradation of polypeptides in millimolar concentrations. In addition, there are calcium channels/pumps and signal transduction components present in the ER membrane that affect and are affected by these processes. The ER lumenal Hsp70, termed immunoglobulin-heavy chain binding protein or BiP, is the central player in all these activities and involves up to seven different co-chaperones, i.e. ER-membrane integrated as well as ER-lumenal Hsp40s, which are termed ERj or ERdj, and two nucleotide exchange factors.

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