✦ LIBER ✦

CD45 and Src-family kinases: and now for something completely different

✍ Scribed by Jonathan D Ashwell; Ugo D'Oro

Publisher: Elsevier Science
Year: 1999
Tongue: English
Weight: 184 KB
Volume: 20
Category: Article
ISSN: 0167-5699
DOI: 10.1016/s0167-5699(99)01505-4

No coin nor oath required. For personal study only.

✦ Synopsis

xamination of contemporary immunology textbooks 1,2 and review articles 3 for the relationship between the CD45 protein tyrosine phosphatase and Src-family protein tyrosine kinases yields a simple and straightforward story: CD45 dephosphorylates the C-terminal negative regulatory tyrosine common to Src-family members, resulting in an increase in activity. Because Src-family kinases (Lck in particular) are essential for proximal signaling via the T-cell antigen receptor (TCR), this neatly explains why CD45-deficient T cells have profound defects in TCR-initiated activation events [4][5][6][7][8] . Although the simplicity of this widely accepted model is attractive, it has a major problem: it does not explain the experimental observations of many groups who have analyzed the interplay between CD45 and Src-family kinases in vivo.

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