Autophosphorylation

Fig. 1: Activation of the epidermal growth factor receptor by autophosphorylation. Adapted from Pecorino (2008)[1]
Fig. 2: Regulation of Src-kinase by autophosphorylation. Adapted from Frame (2002)[2]

Autophosphorylation is a type of post-translational modification of proteins. It is generally defined as the phosphorylation of the kinase by itself. In eukaryotes, this process occurs by the addition of a phosphate group to serine, threonine or tyrosine residues within protein kinases, normally to regulate the catalytic activity.[3][4] Autophosphorylation may occur when a kinases' own active site catalyzes the phosphorylation reaction (cis autophosphorylation), or when another kinase of the same type provides the active site that carries out the chemistry (trans autophosphorylation). The latter often occurs when kinase molecules dimerize.[3] In general, the phosphate groups introduced are gamma phosphates from nucleoside triphosphates, most commonly ATP.[3]

  1. ^ Pecorino, L 2008, 'Molecular biology of cancer', Oxford University Press Inc., New York, U.S.A
  2. ^ Frame MC (Jun 2002). "Src in cancer: deregulation and consequences for cell behaviour". Biochimica et Biophysica Acta (BBA) - Reviews on Cancer. 1602 (2): 114–30. doi:10.1016/s0304-419x(02)00040-9. PMID 12020799.
  3. ^ a b c Petsko, GA and Ringe, D 2009, 'Protein Structure and Function', Oxford University Press Inc., New York, U.S.A
  4. ^ Summers KC, Shen F, Sierra Potchanant EA, Phipps EA, Hickey RJ, Malkas LH (2011). "Phosphorylation: the molecular switch of double-strand break repair". International Journal of Proteomics. 2011: 373816. doi:10.1155/2011/373816. PMC 3200257. PMID 22084686.