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Curr Opin Immunol. 1999 Jun;11(3):270-6.

The regulation of antigen-receptor signaling by protein tyrosine phosphatases: a hole in the story.

Author information

1
Howard Hughes Medical Institute, Box 8118, Departments of Pathology andMolecular Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA. mthomas@pathbox.wustl.edu

Abstract

Antigen-receptor signaling requires Src-family kinases to initiate tyrosine phosphorylation. CD45 dephosphorylates the inhibitory site in Src-family kinases before antigen-receptor engagement and thus serves to 'prime' the kinases. It has been unclear why CD45 does not also dephosphorylate 'activated' kinases or motifs within the cytoplasmic domains of antigen-receptors and thus prevent signal transduction. Recent reports raise the possibility that CD45 is excluded from engaged antigen-receptors by mechanisms that may include the formation of lipid microdomains.

PMID:
10375547
DOI:
10.1016/s0952-7915(99)80044-2
[Indexed for MEDLINE]

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