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

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HSC70 Heat-Shock Proteins
S100 Proteins
Ligases
Ubiquitin
Degradation
Signal transduction
Proteins
Ubiquitin-Protein Ligases
Ubiquitination
Proteasome Endopeptidase Complex
Proteolysis
Signal Transduction

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Cite this

Ca2+/S100 proteins act as upstream regulators of the chaperone-associated ubiquitin ligase chip (c terminus of hsc70-interacting protein). / Shimamoto, Seiko; Kubota, Yasuo; Yamaguchi, Fuminori; Tokumitsu, Hiroshi; Kobayashi, Ryoji.

In: Journal of Biological Chemistry, Vol. 288, No. 10, 08.03.2013, p. 7158-7168.

Research output: Contribution to journalArticle

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