title: Coupling of Ribostasis and Proteostasis: Hsp70 Proteins in mRNA Metabolism.
abstract: A key aspect of the control of gene expression is the differential rates of mRNA translation and degradation, including alterations due to extracellular inputs. Surprisingly, multiple examples now argue that Hsp70 protein chaperones and their associated Hsp40 partners modulate both mRNA degradation and translation. Hsp70 proteins affect mRNA metabolism by various mechanisms including regulating nascent polypeptide chain folding, activating signal transduction pathways, promoting clearance of stress granules, and controlling mRNA degradation in an mRNA-specific manner. Taken together, these observations highlight the general principle that mRNA metabolism is coupled to the proteostatic state of the cell, often as assessed by the presence of unfolded or misfolded proteins.
authors.affiliation: Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO, USA.
authors.forename: Robert W
authors.initials: RW
authors.lastname: Walters
authors.affiliation: Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO, USA; Howard Hughes Medical Institute, University of Colorado at Boulder, Boulder, CO, USA. Electronic address: roy.parker@colorado.edu.
authors.forename: Roy
authors.initials: R
authors.lastname: Parker
mesh_terms: D000818:Animals; D050956:HSP40 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D017510:Protein Folding; D012333:RNA, Messenger / Q000378:metabolism*
chemical_list: D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D012333:RNA, Messenger