Selective role of PKCβ enzymatic function in regulating cell survival mediated by B cell antigen receptor cross-linking

2006 ◽  
Vol 105 (1) ◽  
pp. 83-89 ◽  
Author(s):  
C VENKATARAMAN ◽  
X CHEN ◽  
S NA ◽  
L LEE ◽  
K NEOTE ◽  
...  
Keyword(s):  
B Cell ◽  
Cell Survival ◽  
Antigen Receptor ◽  
Cross Linking ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Enzymatic Function

Role of the extracellular and transmembrane domain of Ig-α/β in assembly of the B cell antigen receptor (BCR)

2007 ◽  
Vol 112 (1) ◽  
pp. 47-57 ◽  
Author(s):  
Janis Dylke ◽  
Jared Lopes ◽  
May Dang-Lawson ◽  
Steve Machtaler ◽  
Linda Matsuuchi
Keyword(s):  
B Cell ◽  
Transmembrane Domain ◽  
Antigen Receptor ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen

scholarly journals Cbl-b Negatively Regulates B Cell Antigen Receptor Signaling in Mature B Cells through Ubiquitination of the Tyrosine Kinase Syk

2003 ◽  
Vol 197 (11) ◽  
pp. 1511-1524 ◽  
Author(s):  
Hae Won Sohn ◽  
Hua Gu ◽  
Susan K. Pierce
Keyword(s):  
B Cells ◽  
Tyrosine Kinase ◽  
B Cell ◽  
Antigen Receptor ◽  
Cellular Systems ◽  
Cross Linking ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Bcr Signaling

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.

The role of Ig-α/β in B cell antigen receptor internalization

2010 ◽  
Vol 134 (1) ◽  
pp. 75-82 ◽  
Author(s):  
Caren Jang ◽  
Steven Machtaler ◽  
Linda Matsuuchi
Keyword(s):  
B Cell ◽  
Antigen Receptor ◽  
Receptor Internalization ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen

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
Keyword(s):  
B Cell ◽  
Antigen Receptor ◽  
Cross Linking ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen
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