BLNK: molecular scaffolding through 'cis'-mediated organization of signaling proteins.
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Chiu CW, Dalton M, Ishiai M, Kurosaki T, Chan AC
BLNK: molecular scaffolding through 'cis'-mediated organization of signaling proteins.
EMBO J. 2002 Dec 2;21(23):6461-72.
- PubMed ID
- 12456653 [ View in PubMed]
- 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.