BLNK: molecular scaffolding through 'cis'-mediated organization of signaling proteins |
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Authors: | Chiu Christopher W Dalton Mark Ishiai Masamichi Kurosaki Tomohiro Chan Andrew C |
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Affiliation: | Center for Immunology, Washington University School of Medicine, St Louis, MO 63110, USA. |
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Abstract: | Assembly of intracellular macromolecular complexes is thought to provide an important mechanism to coordinate the generation of second messengers upon receptor activation. We have previously identified a B cell linker protein, termed BLNK, which serves such a scaffolding function in B cells. We demonstrate here that phosphorylation of five tyrosine residues within human BLNK nucleates distinct signaling effectors following B cell antigen receptor activation. The phosphorylation of multiple tyrosine residues not only amplifies PLCgamma-mediated signaling but also supports 'cis'-mediated interaction between distinct signaling effectors within a large molecular complex. These data demonstrate the importance of coordinate phosphorylation of molecular scaffolds, and provide insights into how assembly of macromolecular complexes is required for normal receptor function. |
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