Abstract
Since their discovery as signaling subunits of the B cell antigen receptor (BCR), Ig-alpha and Ig-beta are discussed to serve either a redundant or distinct function for B cell development, maintenance, and activation. Dependent upon the experimental system that has been used to address this issue, evidence could be provided to support both possibilities. Only recently has it become clear that Ig-alpha and Ig-beta possess a unique signaling identity but that both together are required to orchestrate proper B cell function in vivo. Here we discuss some of the underlying mechanisms that may involve direct coupling to discrete subsets of BCR effector proteins, such as protein tyrosine kinases or the intracellular adaptor SLP-65/BLNK.
MeSH terms
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Adaptor Proteins, Signal Transducing
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Animals
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Antigens, CD / chemistry
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Antigens, CD / metabolism*
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B-Lymphocytes / immunology*
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B-Lymphocytes / metabolism
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CD79 Antigens
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Calcium Signaling
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Carrier Proteins / metabolism
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Humans
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Mice
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Models, Immunological
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Phosphoprotein Phosphatases / metabolism
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Phosphoproteins / metabolism
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Protein Serine-Threonine Kinases / metabolism
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Protein Tyrosine Phosphatases / metabolism
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Protein-Tyrosine Kinases / metabolism
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Receptors, Antigen, B-Cell / chemistry
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Receptors, Antigen, B-Cell / metabolism*
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Signal Transduction
Substances
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Adaptor Proteins, Signal Transducing
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Antigens, CD
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B cell linker protein
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CD79 Antigens
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CD79A protein, human
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CD79B protein, human
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Carrier Proteins
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Cd79a protein, mouse
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Cd79b protein, mouse
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Phosphoproteins
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Receptors, Antigen, B-Cell
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Protein-Tyrosine Kinases
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Protein Serine-Threonine Kinases
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Phosphoprotein Phosphatases
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Protein Tyrosine Phosphatases