scholarly journals A Balance of Bruton’s Tyrosine Kinase and SHIP Activation Regulates B Cell Receptor Cluster Formation by Controlling Actin Remodeling

2011 ◽  
Vol 187 (1) ◽  
pp. 230-239 ◽  
Author(s):  
Chaohong Liu ◽  
Heather Miller ◽  
King Lam Hui ◽  
Brian Grooman ◽  
Silvia Bolland ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
B Cell ◽  
Cluster Formation ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Bruton’S Tyrosine Kinase ◽  
Bruton's Tyrosine Kinase ◽  
Actin Remodeling ◽  
Receptor Cluster

scholarly journals Bruton's Tyrosine Kinase Links the B Cell Receptor to Nuclear Factor κb Activation

2000 ◽  
Vol 191 (10) ◽  
pp. 1735-1744 ◽  
Author(s):  
Urmila D. Bajpai ◽  
Keming Zhang ◽  
Mark Teutsch ◽  
Ranjan Sen ◽  
Henry H. Wortis
Keyword(s):  
B Cells ◽  
Tyrosine Kinase ◽  
B Cell ◽  
Nuclear Translocation ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Immunoglobulin M ◽  
Bruton’S Tyrosine Kinase ◽  
Nuclear Factor ◽  
Bruton's Tyrosine Kinase

The recognition of antigen by membrane immunoglobulin M (mIgM) results in a complex series of signaling events in the cytoplasm leading to gene activation. Bruton's tyrosine kinase (BTK), a member of the Tec family of tyrosine kinases, is essential for the full repertoire of IgM signals to be transduced. We examined the ability of BTK to regulate the nuclear factor (NF)-κB/Rel family of transcription factors, as the activation of these factors is required for a B cell response to mIgM. We found greatly diminished IgM- but not CD40-mediated NF-κB/Rel nuclear translocation and DNA binding in B cells from X-linked immunodeficient (xid) mice that harbor an R28C mutation in btk, a mutation that produces a functionally inactive kinase. The defect was due, in part, to a failure to fully degrade the inhibitory protein of NF-κB, IκBα. Using a BTK-deficient variant of DT40 chicken B cells, we found that expression of wild-type or gain-of-function mutant BTK, but not the R28C mutant, reconstituted NF-κB activity. Thus, BTK is essential for activation of NF-κB via the B cell receptor.

Activation of NF-κB in B cell receptor signaling through Bruton’s tyrosine kinase-dependent phosphorylation of IκB-α

2019 ◽  
Vol 97 (5) ◽  
pp. 675-690 ◽  
Author(s):  
Marilena Pontoriero ◽  
Giuseppe Fiume ◽  
Eleonora Vecchio ◽  
Annamaria de Laurentiis ◽  
Francesco Albano ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
B Cell ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Bruton’S Tyrosine Kinase ◽  
Receptor Signaling ◽  
Bruton's Tyrosine Kinase ◽  
B Cell Receptor Signaling ◽  
Cell Receptor Signaling

scholarly journals The protein product of the c-cbl protooncogene is phosphorylated after B cell receptor stimulation and binds the SH3 domain of Bruton's tyrosine kinase.

1995 ◽  
Vol 182 (2) ◽  
pp. 611-615 ◽  
Author(s):  
G O Cory ◽  
R C Lovering ◽  
S Hinshelwood ◽  
L MacCarthy-Morrogh ◽  
R J Levinsky ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
B Cell ◽  
Cell Receptor ◽  
Sh3 Domain ◽  
Protein Product ◽  
B Cell Receptor ◽  
Bruton’S Tyrosine Kinase ◽  
B Cell Differentiation ◽  
Receptor Stimulation ◽  
Bruton's Tyrosine Kinase

X-linked agammaglobulinemia, a B cell immunodeficiency, is caused by mutations in the Bruton's tyrosine kinase (Btk) gene. The absence of a functional Btk protein leads to a failure of B cell differentiation and antibody production. B cell receptor stimulation leads to the phosphorylation of the Btk protein and it is, therefore, likely that Btk is involved in B cell receptor signaling. As a nonreceptor tyrosine kinase, Btk is likely to interact with several proteins within the context of a signal transduction pathway. To understand such interactions, we have generated glutathione S-transferase fusion proteins corresponding to different domains of the human Btk protein. We have identified a 120-kD protein present in human B cells as being bound by the SH3 domain of Btk and which, after B cell receptor stimulation, is one of the major substrates of tyrosine phosphorylation. We have shown that this 120-kD protein is the protein product of c-cbl, a protooncogene, which is known to be phosphorylated in response to T cell receptor stimulation and to interact with several other tyrosine kinases. Association of the SH3 domain of Btk with p120cbl provides evidence for an analogous role for p120cbl in B cell signaling pathways. The p120cbl protein is the first identified ligand of the Btk SH3 domain.

scholarly journals Bruton’s Tyrosine Kinase Mediates the Synergistic Signalling between TLR9 and the B Cell Receptor by Regulating Calcium and Calmodulin

PLoS ONE ◽  
2013 ◽  
Vol 8 (8) ◽  
pp. e74103 ◽  
Author(s):  
Elaine F. Kenny ◽  
Susan R. Quinn ◽  
Sarah L. Doyle ◽  
Paul M. Vink ◽  
Hans van Eenennaam ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
B Cell ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Bruton’S Tyrosine Kinase ◽  
Bruton's Tyrosine Kinase
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