Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones.
Heat shock protein 40 (Hsp40) co-chaperones assist in cellular protein folding and degradation through the binding and delivery of non-native proteins to heat shock protein 70 (Hsp70). The mechanism for substrate transfer from Hsp40s to Hsp70 is unknown. Two recent studies provide new details that shed light on novel mechanisms for substrate recognition by Hsp40s and a common mechanism for polypeptide transfer to Hsp70.
Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, NC 27599-7090, USA.
Daniel W
DW
Summers
Peter M
PM
Douglas
Carlos H I
CH
Ramos
Douglas M
DM
Cyr
D000818:Animals; D050956:HSP40 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D018832:Molecular Chaperones / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding
D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D010455:Peptides