Anti-immunoglobulin stimulation of B lymphocytes activates src-related protein-tyrosine kinases.

Burkhardt, Anne L.; Brunswick, Mark; Bolen, Joseph B.; Mond, James J.

doi:10.1073/pnas.88.16.7410

Cited by 374 publications

(257 citation statements)

References 32 publications

Supporting

Mentioning

242

Contrasting

Order By: Relevance

“…This receptor complex participates in signal transduction events resulting from engagement of mIg (51). In addition, multiple protein tyrosine kinases have been found to associate with mIg and to be activated after crosslinking of the mIg receptor (52)(53)(54) . Many other target substrates havebeen identified downstream from the mIgM receptor (55).…”

Section: Y2b In B Cell Developmentmentioning

confidence: 99%

Immunoglobulin gamma 2b transgenes inhibit heavy chain gene rearrangement, but cannot promote B cell development.

Roth

Doglio

Manz

et al. 1993

The Journal of Experimental Medicine

View full text Add to dashboard Cite

SummaryTransgenic mice with a y2b transgene were produced to investigate whether y2b can replace P in the development of B lymphocytes . Transgenic y2b is present on the surface of B cells. Young transgenic mice have a dramatic decrease in B cell numbers, however, older mice have almost normal B cell numbers . Strikingly, all y2b-expressing B cells in the spleen also express h . The same is true for mice with a hybrid transgene in which the A. transmembrane and intracytoplasmic sequences replace those of y2b (72b-,umem) . The B cell defect is not due to toxicity of y2b since crosses between y2b transgenic and A transgenic mice have normal numbers of B cells. Presence of the y2b transgene strongly enhances the feedback inhibition of endogenous heavy chain gene rearrangement. Light chain genes are expressed normally, and the early expression of transgenic light chains does not improve B cell maturation. When the endogenous A locus is inactivated, B cells do not develop at all in y2b transgenic mice. The data suggest that y2b cannot replace A in promoting the developmental maturation of B cells, but that it can cause feedback inhibition ofheavy chain gene rearrangement . Thus, the signals for heavy chain feedback and B cell maturation appear to be different .

show abstract

Section: Y2b In B Cell Developmentmentioning

confidence: 99%

Immunoglobulin gamma 2b transgenes inhibit heavy chain gene rearrangement, but cannot promote B cell development.

Roth

Doglio

Manz

et al. 1993

The Journal of Experimental Medicine

View full text Add to dashboard Cite

show abstract

“…2 on B cells by antigen triggers first the activation of the Src family kinase Lyn (1)(2)(3)(4), which is known to phosphorylate the immunoreceptor tyrosine-based activation motifs within the cytoplasmic domains of the Ig-␣ and Ig-␤ subunits that are part of the BCR complex (5). The phosphorylation of the immunoreceptor tyrosine-based activation motif then leads to the activation of the tyrosine kinase Syk (6,7), which leads in turn to the phosphorylation of various downstream proteins such as BLNK, phospholipase C␥2, and Btk (8).…”

Section: Engagement Of the B Cell Antigen Receptor (Bcr)mentioning

confidence: 99%

Leupaxin Negatively Regulates B Cell Receptor Signaling

Chew

Lam

2007

Journal of Biological Chemistry

View full text Add to dashboard Cite

The role of the paxillin superfamily of adaptor proteins in B cell antigen receptor (BCR) signaling has not been studied previously. We show here that leupaxin (LPXN), a member of this family, was tyrosine-phosphorylated and recruited to the plasma membrane of human BJAB lymphoma cells upon BCR stimulation and that it interacted with Lyn (a critical Src family tyrosine kinase in BCR signaling) in a BCR-induced manner. LPXN contains four leucine-rich sequences termed LD motifs, and serial truncation and specific domain deletion of LPXN indicated that its LD3 domain is involved in the binding of Lyn.

show abstract

“…Receptor-associated kinases phosphorylate these immunoreceptor tyrosine-based activation motif (ITAM) tyrosines upon engagement with a polyvalent ligand (27)(28)(29). Phosphorylation of the Ig␣ ITAM serves both to recruit and activate the tyrosine kinase Syk (30,31).…”

mentioning

confidence: 99%

Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα

Siemasko

Skaggs

Kabak

et al. 2002

The Journal of Immunology

View full text Add to dashboard Cite

Ags that cross-link the B cell Ag receptor are preferentially and rapidly delivered to the MHC class II-enriched compartment for processing into peptides and subsequent loading onto MHC class II. Proper sorting of Ag/receptor complexes requires the recruitment of Syk to the phosphorylated immunoreceptor tyrosine-based activation motif tyrosines of the B cell Ag receptor constituent Igα. We postulated that the Igα nonimmunoreceptor tyrosine-based activation motif tyrosines, Y176 and Y204, contributed to receptor trafficking. Igα(YΔF176,204)/Igβ receptors were targeted to late endosomes, but were excluded from the vesicle lumen and could not facilitate the presentation of Ag to T cells. Subsequent analysis demonstrated that phosphorylation of Y176/Y204 recruited the B cell linker protein, Vav, and Grb2. Reconstitution of Igα(YΔF176,204)/Igβ with the B cell linker protein rescued both receptor-facilitated Ag presentation and entry into the MHC class II-enriched compartment. Thus, aggregation accelerates receptor trafficking by recruiting two separate signaling modules required for transit through sequential checkpoints.

show abstract

Anti-immunoglobulin stimulation of B lymphocytes activates src-related protein-tyrosine kinases.

Cited by 374 publications

References 32 publications

Immunoglobulin gamma 2b transgenes inhibit heavy chain gene rearrangement, but cannot promote B cell development.

Immunoglobulin gamma 2b transgenes inhibit heavy chain gene rearrangement, but cannot promote B cell development.

Leupaxin Negatively Regulates B Cell Receptor Signaling

Receptor-Facilitated Antigen Presentation Requires the Recruitment of B Cell Linker Protein to Igα

Contact Info

Product

Resources

About