Pseudokinase

Pseudokinases are catalytically-deficient pseudoenzyme[1] variants of protein kinases that are represented in all kinomes across the kingdoms of life. Pseudokinases have both physiological (signal transduction) and pathophysiological functions.[2][3][4][5][6][7][8]

  1. ^ Murphy JM, Farhan H, Eyers PA (April 2017). "Bio-Zombie: the rise of pseudoenzymes in biology". Biochemical Society Transactions. 45 (2): 537–544. doi:10.1042/BST20160400. PMID 28408493.
  2. ^ Jacobsen AV, Murphy JM (June 2017). "The secret life of kinases: insights into non-catalytic signalling functions from pseudokinases". Biochemical Society Transactions. 45 (3): 665–681. doi:10.1042/BST20160331. PMID 28620028.
  3. ^ Murphy JM, Zhang Q, Young SN, Reese ML, Bailey FP, Eyers PA, Ungureanu D, Hammaren H, Silvennoinen O, Varghese LN, Chen K, Tripaydonis A, Jura N, Fukuda K, Qin J, Nimchuk Z, Mudgett MB, Elowe S, Gee CL, Liu L, Daly RJ, Manning G, Babon JJ, Lucet IS (January 2014). "A robust methodology to subclassify pseudokinases based on their nucleotide-binding properties". The Biochemical Journal. 457 (2): 323–34. doi:10.1042/BJ20131174. PMC 5679212. PMID 24107129.
  4. ^ Kannan N, Taylor SS (April 2008). "Rethinking pseudokinases". Cell. 133 (2): 204–5. doi:10.1016/j.cell.2008.04.005. PMC 6226312. PMID 18423189.
  5. ^ Mukherjee K, Sharma M, Urlaub H, Bourenkov GP, Jahn R, Südhof TC, Wahl MC (April 2008). "CASK Functions as a Mg2+-independent neurexin kinase". Cell. 133 (2): 328–39. doi:10.1016/j.cell.2008.02.036. PMC 3640377. PMID 18423203.
  6. ^ Bailey FP, Byrne DP, Oruganty K, Eyers CE, Novotny CJ, Shokat KM, Kannan N, Eyers PA (April 2015). "The Tribbles 2 (TRB2) pseudokinase binds to ATP and autophosphorylates in a metal-independent manner". The Biochemical Journal. 467 (1): 47–62. doi:10.1042/BJ20141441. PMC 4844368. PMID 25583260.
  7. ^ Shi F, Telesco SE, Liu Y, Radhakrishnan R, Lemmon MA (April 2010). "ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation". Proceedings of the National Academy of Sciences of the United States of America. 107 (17): 7692–7. Bibcode:2010PNAS..107.7692S. doi:10.1073/pnas.1002753107. PMC 2867849. PMID 20351256.
  8. ^ Zeqiraj E, Filippi BM, Deak M, Alessi DR, van Aalten DM (December 2009). "Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation". Science. 326 (5960): 1707–11. Bibcode:2009Sci...326.1707Z. doi:10.1126/science.1178377. PMC 3518268. PMID 19892943.