Conformational plasticity and navigation of signaling proteins in antigen-activated B lymphocytes.

摘要: Over the past two decades our view of B cell antigen receptor (BCR) has fundamentally changed. Being initially regarded as a mute antibody orphan surface, BCR turned out to be complex multimolecular machine monitoring almost all stages development, selection, and activation through plethora ubiquitously cell-type-specific effector proteins. A comprehensive understanding many signaling facets is still but few common biochemical principles outlined in this review operate at level orchestrate specific wiring intracellular transducer cascades. First, initiation processing antigen-induced signal transduction relies on transient conformational changes proteins trigger their physical interaction with downstream elements. Second, dynamic assembly signalosomes occurs distinct subcellular locations, most prominently plasma membrane, which requires relocalization one or more engaged molecules. For both, precise formation efficient targeting, components are equipped variety protein domains. Here we provide an overview how these simple rules applied by limited number transmembrane cytosolic convert ligation into Ca(2+) mobilization Ras adjustable manner.