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Interaction of U‐box‐type ubiquitin‐protein ligases (E3s) with molecular chaperones
Author(s) -
Hatakeyama Shigetsugu,
Matsumoto Masaki,
Yada Masayoshi,
Nakayama Keiichi I.
Publication year - 2004
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1356-9597.2004.00742.x
Subject(s) - biology , ubiquitin , ubiquitin protein ligases , computational biology , co chaperone , microbiology and biotechnology , genetics , ubiquitin ligase , hsp90 , heat shock protein , gene
Members of the U‐box family of proteins constitute a class of ubiquitin‐protein ligases (E3s) distinct from the HECT‐type and RING finger‐containing E3 families. Two representative mammalian U‐box proteins, UFD2a and CHIP, interact with the molecular chaperones VCP and either Hsp90 or Hsc70, respectively, and are implicated in the degradation of damaged proteins. We have now investigated the roles of mammalian U‐box proteins by performing a comprehensive screen for molecules that interact with these proteins in the yeast two‐hybrid system. All mammalian U‐box proteins tested were found to interact with molecular chaperones or cochaperones, including Hsp90, Hsp70, DnaJc7, EKN1, CRN, and VCP. These observations suggest that the function of U box‐type E3s is to mediate the degradation of unfolded or misfolded proteins in conjunction with molecular chaperones as receptors that recognize such abnormal proteins.