期刊
NATURE IMMUNOLOGY
卷 2, 期 9, 页码 870-875出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ni0901-870
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- NIDDK NIH HHS [R01DK56558] Funding Source: Medline
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 (PI3K) 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 through its E3 ubiquitin ligase activity. The enhanced activation of Cbl-b(-/-)T cells was suppressed by the inhibition of PI3K. The results suggest a proteolysis-independent function for Cbl.b in the modification of protein recruitment.
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