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Receptor tyrosine kinase substrates: src homology domains and signal transduction
Author(s) -
Carpenter Graham
Publication year - 1992
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.6.14.1385243
Subject(s) - proto oncogene tyrosine protein kinase src , microbiology and biotechnology , signal transduction , receptor tyrosine kinase , tyrosine kinase , biology , ror1 , platelet derived growth factor receptor , tyrosine phosphorylation , tyrosine , phosphorylation , protein tyrosine phosphatase , sh2 domain , cell signaling , chemistry , receptor , biochemistry , growth factor
Among the intracellular milieu of proteins are molecules with defined biochemical functions that serve as substrates for ligand‐activated tyrosine kinase receptors. It seems likely that some of these substrate molecules are elements of a critical signaling pathway used by growth factors to control cell proliferation and subverted by oncogenes to deregulate this process. Although the process of cell growth and division is relatively slow compared with other hormonally regulated responses, homeostasis in a human being requires approximately 20 × 10 6 cell divisions per second for the renewal of various cell populations. This review summarizes the present understanding of tyrosine kinase substrates that seem likely to have key roles in the signal transduction pathway that regulates cell proliferation. This includes structural features of these molecules, the influence of tyrosine phosphorylation on their functions, the biological roles of these proteins, and the capacity of these substrates to associate with activated receptor tyrosine kinases.— Carpenter, G. Receptor tyrosine kinase substrates: src homology domains and signal transduction. FASEB J. 6: 3283‐3289; 1992.