Abstract
The Src family of protein tyrosine kinases consists of at least nine enzymes in birds and mammals. Src family kinases share a high degree of structural similarity, including domain architecture and regulation. Topographically (from amino to carboxy terminus) they have: amino terminal acylation sites (responsible for membrane anchoring); a unique domain (40–80 amino acids that distinguish each member of the family); a Src Homology (SH) 3 domain; an SH2 domain; the catalytic domain; and carboxy terminal regulatory sequences (“the tail”). All members of the family are negatively regulated by the phosphorylation of a tyrosine residue in the tail. This phosphorylation is carried out by an enzyme called Csk. The importance of the tail is demonstrated by two observations: firstly, in the many cases tested, mutation of the tail such that it can no longer be phosphorylated is sufficient to convert proto-oncogene to oncogene; secondly, mice lacking Csk have constitutively active Src family kinases and die during embryogenesis (reviewed in 1,2,3).
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Courtneidge, S.A. (1996). Src Family Kinases and the Cell Cycle. In: Mihich, E., Housman, D. (eds) Cancer Genes. Pezcoller Foundation Symposia, vol 7. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5895-8_3
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DOI: https://doi.org/10.1007/978-1-4615-5895-8_3
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