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Cited by 179

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

The Cochaperone HspBP1 Inhibits the CHIP Ubiquitin Ligase and Stimulates the Maturation of the Cystic Fibrosis Transmembrane Conductance Regulator

Open access
Alberti, Simon, Böhse, Karsten, Arndt, Verena, Schmitz, Anton, Höhfeld, Jörg·2004·Molecular Biology of the Cell

Abstract

The CHIP ubiquitin ligase turns molecular chaperones into protein degradation factors. CHIP associates with the chaperones Hsc70 and Hsp90 during the regulation of signaling pathways and during protein quality control, and directs chaperone-bound clients to the proteasome for degradation. Obviously, this destructive activity should be carefully controlled. Here, we identify the cochaperone HspBP1 as an inhibitor of CHIP. HspBP1 attenuates the ubiquitin ligase activity of CHIP when complexed with Hsc70. As a consequence, HspBP1 interferes with the CHIP-induced degradation of immature forms of the cystic fibrosis transmembrane conductance regulator (CFTR) and stimulates CFTR maturation. Our data reveal a novel regulatory mechanism that determines folding and degradation activities of molecular chaperones.

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Metadata

Authors
Alberti, S., Böhse, K., Arndt, V., Schmitz, A., & Höhfeld, J.
Venue
Molecular Biology of the Cell
Published
2004-09
Volume
15
Issue
9
Pages
4003-4010
ISSN
  • 1059-1524 (ISSN-L)
  • 1939-4586
OpenAlex
W2116511323
Cited by
179
References
2
FWCI
4.26
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The Cochaperone HspBP1 Inhibits the CHIP Ubiquitin Ligase and Stimulates the Maturation of the Cystic Fibrosis Transmembrane Conductance Regulator. https://app.cochat.ai/papers/10.1091/mbc.e04-04-0293
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Alberti, S., Böhse, K., Arndt, V., Schmitz, A., & Höhfeld, J. (2004). The Cochaperone HspBP1 Inhibits the CHIP Ubiquitin Ligase and Stimulates the Maturation of the Cystic Fibrosis Transmembrane Conductance Regulator. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.e04-04-0293

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