Abstract
Antigen receptors on the surface of T and B lymphocytes and various immunoglobulin Fc receptors are complexed multi-subunit structures that possess unique cytoplasmic modules, termed immunoreceptor tyrosine-based activation motif (ITAM). These modules consist of two repeats of the conserved sequence Tyr-X-X-Leu/Ile spaced by six-to-eight residues and they function as 'on and off' switches that link the receptors to their intracellular signaling machinery. Thus, engagement of ITAM-containing receptors results in a rapid and transient phosphorylation of the ITAMs' tyrosine residues that function as temporal scaffolds for Src homology 2 (SH2) domains of downstream effector molecules. Recruitment and binding of these molecules to phospho-ITAMs initiate a cascade of biochemical events that lead to cell proliferation, differentiation, and acquisition of unique effector functions.
Original language | English |
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Pages (from-to) | 243-253 |
Number of pages | 11 |
Journal | Receptors and Channels |
Volume | 5 |
Issue number | 5 |
State | Published - 1 Jan 1998 |
Keywords
- ITAM
- Lymphocyte activation
- Protein tyrosine kinase
- SH2
- Signal transduction
- Tyrosine phosphorylation
ASJC Scopus subject areas
- Pharmacology
- Endocrinology
- Clinical Biochemistry
- Cell Biology