Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/s41594-017-0012-6.pdf
Reference57 articles.
1. Kim, Y. E., Hipp, M. S., Bracher, A., Hayer-Hartl, M. & Hartl, F. U. Molecular chaperone functions in protein folding and proteostasis. Annu. Rev. Biochem. 82, 323–355 (2013).
2. Kampinga, H. H. & Craig, E. A. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11, 579–592 (2010).
3. Otero, J. H., Lizák, B. & Hendershot, L. M. Life and death of a BiP substrate. Semin. Cell Dev. Biol. 21, 472–478 (2010).
4. Qi, R. et al. Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP. Nat. Struct. Mol. Biol. 20, 900–907 (2013).
5. Marcinowski, M. et al. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nat. Struct. Mol. Biol. 18, 150–158 (2011).
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