The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones

International Journal of Molecular Sciences

Lorea Velasco¹  Leire Dublang¹  Fernando Moro¹  Arturo Muga¹ 

[1] Biofisika Institute (UPV/EHU, CSIC) and Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country (UPV/EHU), Barrio Sarriena s/n, 48940 Leioa, Spain;

关键词: chaperones;    post-translational modification;    phosphorylation;    human disaggregase;    Hsp40;    Hsp70;    Hsp110;   

DOI  :  10.3390/ijms20174122

来源: DOAJ

【 摘 要 】

Proteins must fold into their native structure and maintain it during their lifespan to display the desired activity. To ensure proper folding and stability, and avoid generation of misfolded conformations that can be potentially cytotoxic, cells synthesize a wide variety of molecular chaperones that assist folding of other proteins and avoid their aggregation, which unfortunately is unavoidable under acute stress conditions. A protein machinery in metazoa, composed of representatives of the Hsp70, Hsp40, and Hsp110 chaperone families, can reactivate protein aggregates. We revised herein the phosphorylation sites found so far in members of these chaperone families and the functional consequences associated with some of them. We also discuss how phosphorylation might regulate the chaperone activity and the interaction of human Hsp70 with its accessory and client proteins. Finally, we present the information that would be necessary to decrypt the effect that post-translational modifications, and especially phosphorylation, could have on the biological activity of the Hsp70 system, known as the “chaperone code”.

【 授权许可】

Unknown