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Syk tyrosine kinase required for mouse viability and B-cell development

Cheng, Alec M., Rowley, Bruce, Pao, William, Hayday, Adrian, Bolen, Joseph B., Pawson, Tony·1995·Nature
DOI 10.1038/378303a0
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Abstract

The Syk cytoplasmic protein-tyrosine kinase has two amino-terminal SH2 domains and a carboxy-terminal catalytic domain. Syk, and its close relative ZAP-70, are apparently pivotal in coupling antigen- and Fc-receptors to downstream signalling events. Syk associates with activated Fc receptors, the T cell receptor complex and the B-cell antigen-receptor complex (BCR) in immature and mature B lymphocytes. On receptor activation, the tandem SH2 domains of Syk bind dual phosphotyrosine sites in the conserved ITAM motifs of receptor signalling chains, such as the immunoglobulin alpha and beta-chains of the BCR, leading to Syk activation. Here we have investigated Syk function in vivo by generating a mouse strain with a targeted mutation in the syk gene. Homozygous syk mutants suffered severe haemorrhaging as embryos and died perinatally, indicating that Syk has a critical role in maintaining vascular integrity or in wound healing during embryogenesis. Analysis of syk-/- lymphoid cells showed that the syk mutation impaired the differentiation of B-lineage cells, apparently by disrupting signalling from the pre-BCR complex and thereby preventing the clonal expansion, and further maturation, of pre-B cells.

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Metadata

Authors
Cheng, A. M., Rowley, B., Pao, W., Hayday, A., Bolen, J. B., & Pawson, T.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
1995-11-16
Volume
378
Issue
6554
Pages
303-306
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/378303a0
Cited by
528
References
0
Language
en
Update notices
correction (1996-02-15)
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