Abstract.
The endoplasmic reticulum (ER) is involved in a variety of essential and interconnected processes in human cells, including protein biogenesis, signal transduction, and calcium homeostasis. The central player in all these processes is the ER-lumenal polypeptide chain binding protein BiP that acts as a molecular chaperone. BiP belongs to the heat shock protein 70 (Hsp70) family and crucially depends on a number of interaction partners, including co-chaperones, nucleotide exchange factors, and signaling molecules. In the course of the last five years, several diseases have been linked to BiP and its interaction partners, such as a group of infectious diseases that are caused by Shigella toxin producing E. coli. Furthermore, the inherited diseases Marinesco-Sjögren syndrome, autosomal dominant polycystic liver disease, Wolcott-Rallison syndrome, and several cancer types can be considered BiP-related diseases. This review summarizes the physiological and pathophysiological characteristics of BiP and its interaction partners.
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Received 20 November 2008; received after revision 09 December 2008; accepted 12 December 2008
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Dudek, J., Benedix, J., Cappel, S. et al. Functions and pathologies of BiP and its interaction partners. Cell. Mol. Life Sci. 66, 1556–1569 (2009). https://doi.org/10.1007/s00018-009-8745-y
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DOI: https://doi.org/10.1007/s00018-009-8745-y