Affiliation:
1. Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA
Abstract
Maintenance of protein homeostasis in eukaryotes under normal growth and stress conditions requires the functions of Hsp70 chaperones and associated cochaperones. Here, we investigate an evolutionarily conserved serine phosphorylation that occurs at the site of communication between the nucleotide-binding and substrate-binding domains of Hsp70. Ser151 phosphorylation in yeast Hsp70 (Ssa1) is promoted by cyclin-dependent kinase (Cdk1) during normal growth. Phosphomimetic substitutions at this site (S151D) dramatically downregulate heat shock responses, a result conserved with HSC70 S153 in human cells.
Funder
Taiwan Ministry of Education
Howard Hughes Medical Institute
Publisher
American Society for Microbiology
Subject
Cell Biology,Molecular Biology
Cited by
5 articles.
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