Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones

Daniel W. Summers, Peter M. Douglas, Carlos H.I. Ramos, Douglas M. Cyr

Research output: Contribution to journalShort survey

49 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)230-233
Number of pages4
JournalTrends in Biochemical Sciences
Volume34
Issue number5
DOIs
StatePublished - May 1 2009

Fingerprint

HSP40 Heat-Shock Proteins
Molecular Chaperones
HSP70 Heat-Shock Proteins
Peptides
Protein folding
Protein Folding
Substrates
Proteolysis
Degradation
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones. / Summers, Daniel W.; Douglas, Peter M.; Ramos, Carlos H.I.; Cyr, Douglas M.

In: Trends in Biochemical Sciences, Vol. 34, No. 5, 01.05.2009, p. 230-233.

Research output: Contribution to journalShort survey

Summers, Daniel W. ; Douglas, Peter M. ; Ramos, Carlos H.I. ; Cyr, Douglas M. / Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones. In: Trends in Biochemical Sciences. 2009 ; Vol. 34, No. 5. pp. 230-233.
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