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Immunoreceptor tyrosine‐based activation motif (ITAM), a unique module linking antigen and Fc receptors to their signaling cascades
Author(s) -
Isakov Noah
Publication year - 1997
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.61.1.6
Subject(s) - immunoreceptor tyrosine based activation motif , biology , signal transduction , receptor , tyrosine , microbiology and biotechnology , sh2 domain , receptor tyrosine kinase , phosphorylation , tyrosine phosphorylation , proto oncogene tyrosine protein kinase src , t cell receptor , tyrosine kinase , biochemistry , genetics , t cell , immune system
Signal transduction by the T cell and B cell antigen receptors and by receptors for a variety of immunoglobulins' Fc region is strictly dependent on a receptor subunit cytoplasmic module termed immunoreceptor tyrosine‐based activation motif (FE4M). Hris module exists in one or more copies in each of the receptor‐associated signal‐transducing molecules and it possesses two repeats of the consensus sequence Tyr‐X‐X‐Leu/IIe spaced by six to eight amino acids. Receptor engagement is followed by a rapid and transient phosphorylation of tyrosine residues within their ITAMs, thereby creating temporary binding sites for Src homology 2 (SH2)‐containing signaling molecules operating downstream of the activated receptor. The purpose of this review is to discuss recent findings on the functional role of ITAMs in antigen and Fc receptor‐mediated signal transduction, with a particular emphasis on kinases operating upstream and downstream of the ITAMs. J. Leukoc. Biol . 61: 6–16; 1997.