Interdomain A is crucial for ITAM-dependent and -independent regulation of Syk
2007 | journal article. A publication with affiliation to the University of Göttingen.
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- Authors
- Adachi, Takahiro; Wienands, Juergen ; Tsubata, Takeshi; Kurosaki, Tomohiro
- Abstract
- Non-receptor type protein tyrosine kinase (PTK) Syk is essential for the signaling via the B cell antigen receptor (BCR). Upon BCR crosslinking, Syk is recruited via its tandem SH2 domains to tyrosine-phosphorylated Ig-alpha/Ig-beta constituting components of BCR, and is then activated. The interdomain A lying between the two SH2 domains is highly conserved among different species of Syk and between Syk and ZAP-70. The mutant Syk carrying a deletion in the interdomain A (Delta 140-159) became phosphorylated regardless of BCR ligation and did not induce Ca2+ mobilization upon crosslinking of BCR. Furthermore, in vitro binding assay revealed that deletion of a part of the interdomain A abolished its binding activity to phosphorylated Ig-alpha/Ig-beta. These results indicate that the interdomain A of Syk is required for activation of Syk by binding to the phosphorylated Ig-alpha/Ig-beta upon BCR ligation and inhibition of spontaneous activation at the resting state. (C) 2007 Elsevier Inc. All rights reserved.
- Issue Date
- 2007
- Status
- published
- Publisher
- Academic Press Inc Elsevier Science
- Journal
- Biochemical and Biophysical Research Communications
- ISSN
- 0006-291X