Ca2+/S100 proteins act as upstream regulators of the chaperone-associated ubiquitin ligase chip (c terminus of hsc70-interacting protein)

Seiko Shimamoto, Yasuo Kubota, Fuminori Yamaguchi, Hiroshi Tokumitsu, Ryoji Kobayashi

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Background: CHIP is a U-box E3 ubiquitin ligase that facilitates the proteasomal degradation of many client proteins. Results: Ca2+/S100 proteins directly interact with CHIP and suppress the ubiquitination and degradation of the client proteins. Conclusion: We have identified S100 proteins as novel Ca2+-dependent regulators of the CHIP-proteasome pathway. Significance: This is the first indication that S100 proteins form a link between Ca2+ signal transduction and the CHIPproteasome pathway.

Original languageEnglish
Pages (from-to)7158-7168
Number of pages11
JournalJournal of Biological Chemistry
Volume288
Issue number10
DOIs
Publication statusPublished - Mar 8 2013
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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