Proteolysis-independent regulation of P13K by Cbl-b-mediated ubiquitination in T cells

Deyu Fang, Yun Cai Liu*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

225 Scopus citations

Abstract

Cbl-b, a ring-type E3 ubiquitin protein ligase, is implicated in setting the threshold of T lymphocyte activation. The p85 regulatory subunit of phosphatidylinositol 3 kinase (P13K) was identified as a substrate for Cbl-b. We have shown that Cbl-b negatively regulated p85 in a proteolysis-independent manner, Cbl-b is involved in the recruitment of p85 to CD28 and T cell antigen receptor ζ through its E3 ubiquitin ligase activity. The enhanced activation of Cbl-b-/-T cells was suppressed by the inhibition of P13K. The results suggest a proteolysis-independent function for Cbl-b in the modification of protein recruitment.

Original languageEnglish (US)
Pages (from-to)870-875
Number of pages6
JournalNature Immunology
Volume2
Issue number9
DOIs
StatePublished - 2001

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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