scholarly journals Syk, Activated by Cross-linking the B-cell Antigen Receptor, Localizes to the Cytosol Where It Interacts with and Phosphorylates α-Tubulin on Tyrosine

1996 ◽  
Vol 271 (9) ◽  
pp. 4755-4762 ◽  
Author(s):  
Jennifer D. Peters ◽  
Michael T. Furlong ◽  
David J. Asai ◽  
Marietta L. Harrison ◽  
Robert L. Geahlen
2003 ◽  
Vol 197 (11) ◽  
pp. 1511-1524 ◽  
Author(s):  
Hae Won Sohn ◽  
Hua Gu ◽  
Susan K. Pierce

Members of the Cbl family of molecular adaptors play key roles in regulating tyrosine kinase-dependent signaling in a variety of cellular systems. Here we provide evidence that in B cells Cbl-b functions as a negative regulator of B cell antigen receptor (BCR) signaling during the normal course of a response. In B cells from Cbl-b–deficient mice cross-linking the BCRs resulted in sustained phosphorylation of Igα, Syk, and phospholipase C (PLC)-γ2, leading to prolonged Ca2+ mobilization, and increases in extracellular signal–regulated kinase (ERK) and c-Jun NH2-terminal protein kinase (JNK) phosphorylation and surface expression of the activation marker, CD69. Image analysis following BCR cross-linking showed sustained polarization of the BCRs into large signaling-active caps associated with phosphorylated Syk in Cbl-b–deficient B cells in contrast to the BCRs in Cbl-b–expressing B cells that rapidly proceeded to form small, condensed, signaling inactive caps. Significantly, prolonged phosphorylation of Syk correlated with reduced ubiquitination of Syk indicating that Cbl-b negatively regulates BCR signaling by targeting Syk for ubiquitination.


1997 ◽  
Vol 94 (24) ◽  
pp. 13152-13157 ◽  
Author(s):  
A. B. Satterthwaite ◽  
H. Cheroutre ◽  
W. N. Khan ◽  
P. Sideras ◽  
O. N. Witte

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