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

Deyu Fang; Yun Cai Liu

doi:10.1038/ni0901-870

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

Deyu Fang, Yun Cai Liu^*

^*Corresponding author for this work

Pathology

Research output: Contribution to journal › Article › peer-review

246 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 language	English (US)
Pages (from-to)	870-875
Number of pages	6
Journal	Nature Immunology
Volume	2
Issue number	9
DOIs	https://doi.org/10.1038/ni0901-870
State	Published - 2001

ASJC Scopus subject areas

Immunology and Allergy
Immunology

Access to Document

10.1038/ni0901-870

Cite this

@article{5514a78ab3f348b7a3fffb4cc266d678,

title = "Proteolysis-independent regulation of P13K by Cbl-b-mediated ubiquitination in T cells",

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.",

author = "Deyu Fang and Liu, {Yun Cai}",

year = "2001",

doi = "10.1038/ni0901-870",

language = "English (US)",

volume = "2",

pages = "870--875",

journal = "Nature Immunology",

issn = "1529-2908",

publisher = "Nature Publishing Group",

number = "9",

}

TY - JOUR

T1 - Proteolysis-independent regulation of P13K by Cbl-b-mediated ubiquitination in T cells

AU - Fang, Deyu

AU - Liu, Yun Cai

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0035555195&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035555195&partnerID=8YFLogxK

U2 - 10.1038/ni0901-870

DO - 10.1038/ni0901-870

M3 - Article

C2 - 11526404

AN - SCOPUS:0035555195

SN - 1529-2908

VL - 2

SP - 870

EP - 875

JO - Nature Immunology

JF - Nature Immunology

IS - 9

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this