Faculty Opinions recommendation of Amplification of B cell antigen receptor signaling by a Syk/ITAM positive feedback loop.

Author(s):  
John Cambier ◽  
Thomas Packard
2002 ◽  
Vol 10 (5) ◽  
pp. 1057-1069 ◽  
Author(s):  
Véronique Rolli ◽  
Maike Gallwitz ◽  
Thomas Wossning ◽  
Alexandra Flemming ◽  
Wolfgang W.A Schamel ◽  
...  

PLoS Biology ◽  
2006 ◽  
Vol 4 (7) ◽  
pp. e200 ◽  
Author(s):  
Ping Hou ◽  
Elizabeth Araujo ◽  
Tong Zhao ◽  
Miao Zhang ◽  
Don Massenburg ◽  
...  

2008 ◽  
Vol 283 (25) ◽  
pp. 16971-16984 ◽  
Author(s):  
Claire A. Walshe ◽  
Stephen A. Beers ◽  
Ruth R. French ◽  
Claude H. T. Chan ◽  
Peter W. Johnson ◽  
...  

1996 ◽  
Vol 16 (9) ◽  
pp. 5026-5035 ◽  
Author(s):  
G Kong ◽  
M Dalton ◽  
J Bubeck Wardenburg ◽  
D Straus ◽  
T Kurosaki ◽  
...  

Biochemical and genetic evidence has implicated two families of protein tyrosine kinases (PTKs), the Src- and Syk-PTKs, in T- and B-cell antigen receptor signaling. ZAP-70 is a member of the Syk-PTKs that associates with the T-cell antigen receptor and undergoes tyrosine phosphorylation following receptor activation. Three tyrosine residues, Tyr-292, -492, and -493, have been identified as sites of phosphorylation following T-cell antigen receptor engagement. Utilizing ZAP-70- and Syk-deficient lymphocytes (Syk-DT40 cells), we provide biochemical and functional evidence that heterologous trans-phosphorylation of Tyr-493 by a Src-PTK is required for antigen receptor-mediated activation of both the calcium and ras pathways. In contrast, cells expressing mutations at Tyr-292 or -492 demonstrate hyperactive T- and B-cell antigen receptor phenotypes. Thus, phosphorylation of ZAP-70 mediates both activation and inactivation of antigen receptor signaling.


2005 ◽  
Vol 17 (10) ◽  
pp. 1277-1282 ◽  
Author(s):  
Atsushi Kumanogoh ◽  
Takashi Shikina ◽  
Chie Watanabe ◽  
Noriko Takegahara ◽  
Kazuhiro Suzuki ◽  
...  

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