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

doi:10.1074/jbc.M112.436758

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 journal › Article › peer-review

32 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 language	English
Pages (from-to)	7158-7168
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	10
DOIs	https://doi.org/10.1074/jbc.M112.436758
Publication status	Published - Mar 8 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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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.",

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AU - Yamaguchi, Fuminori

AU - Tokumitsu, Hiroshi

AU - Kobayashi, Ryoji

PY - 2013/3/8

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AB - 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.

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

Abstract

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