Jump to content

Pseudokinase

From Wikipedia, the free encyclopedia
(Redirected from Pseudokinase domain)

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]

History

[edit]

The phrase pseudokinase was first coined in 2002.[9] They were subsequently sub-classified into different 'classes'.[10][8][11][12][13] Several pseudokinase-containing families are found in the human kinome, including the Tribbles pseudokinases, which are at the interface between kinase and ubiquitin E3 ligase signalling.[14][15][16]

The human pseudokinases (and their pseudophosphatase cousins) are implicated in a wide variety of diseases,[17][18] which has made them potential drug targets and antitargets).[19][20][21][22] Pseudokinases are made up of an evolutionary mixture of eukaryotic protein kinase (ePK) and non ePK-related pseudoenzyme proteins (e.g., FAM20A, which binds ATP[23] and is pseudokinase due to a conserved glutamate to glutamine swap in the alpha-C helix.[24] FAM20A is implicated in periodontal disease, and serves to control the catalytic activity of FAM20C, an important physiological casein kinase that controls phosphorylation of proteins in the Golgi apparatus that are destined for secretion,[25] such as the milk protein casein.

A comprehensive evolutionary analysis confirms that pseudokinases group into multiple subfamilies, and these are found in the annotated kinome of organisms across the kingdoms of life, including prokaryotes, archaea and all eukaryotic lineages with an annotated proteome; this data is searchable in ProKino (http://vulcan.cs.uga.edu/prokino/about/browser). [26]

See also

[edit]

References

[edit]
  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. ^ a b 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.
  9. ^ Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S (December 2002). "The protein kinase complement of the human genome". Science. 298 (5600): 1912–34. Bibcode:2002Sci...298.1912M. doi:10.1126/science.1075762. PMID 12471243. S2CID 26554314.
  10. ^ Boudeau J, Miranda-Saavedra D, Barton GJ, Alessi DR (September 2006). "Emerging roles of pseudokinases". Trends in Cell Biology. 16 (9): 443–52. doi:10.1016/j.tcb.2006.07.003. PMID 16879967.
  11. ^ Zeqiraj E, van Aalten DM (December 2010). "Pseudokinases-remnants of evolution or key allosteric regulators?". Current Opinion in Structural Biology. 20 (6): 772–81. doi:10.1016/j.sbi.2010.10.001. PMC 3014569. PMID 21074407.
  12. ^ Scheeff ED, Eswaran J, Bunkoczi G, Knapp S, Manning G (January 2009). "Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site". Structure. 17 (1): 128–38. doi:10.1016/j.str.2008.10.018. PMC 2639636. PMID 19141289.
  13. ^ Eyers PA, Murphy JM (August 2013). "Dawn of the dead: protein pseudokinases signal new adventures in cell biology". Biochemical Society Transactions. 41 (4): 969–74. doi:10.1042/BST20130115. PMID 23863165.
  14. ^ Eyers PA, Keeshan K, Kannan N (April 2017). "Tribbles in the 21st Century: The Evolving Roles of Tribbles Pseudokinases in Biology and Disease". Trends in Cell Biology. 27 (4): 284–298. doi:10.1016/j.tcb.2016.11.002. PMC 5382568. PMID 27908682.
  15. ^ Foulkes DM, Byrne DP, Yeung W, Shrestha S, Bailey FP, Ferries S, Eyers CE, Keeshan K, Wells C, Drewry DH, Zuercher WJ, Kannan N, Eyers PA (September 2018). "Covalent inhibitors of EGFR family protein kinases induce degradation of human Tribbles 2 (TRIB2) pseudokinase in cancer cells". Science Signaling. 11 (549): eaat7951. doi:10.1126/scisignal.aat7951. PMC 6553640. PMID 30254057.
  16. ^ Jamieson SA, Ruan Z, Burgess AE, Curry JR, McMillan HD, Brewster JL, Dunbier AK, Axtman AD, Kannan N, Mace PD (September 2018). "Substrate binding allosterically relieves autoinhibition of the pseudokinase TRIB1". Science Signaling. 11 (549): eaau0597. doi:10.1126/scisignal.aau0597. PMC 6553639. PMID 30254053.
  17. ^ Reiterer V, Eyers PA, Farhan H (September 2014). "Day of the dead: pseudokinases and pseudophosphatases in physiology and disease". Trends in Cell Biology. 24 (9): 489–505. doi:10.1016/j.tcb.2014.03.008. PMID 24818526.
  18. ^ Chen MJ, Dixon JE, Manning G (April 2017). "Genomics and evolution of protein phosphatases". Science Signaling. 10 (474): eaag1796. doi:10.1126/scisignal.aag1796. PMID 28400531. S2CID 41041971.
  19. ^ Byrne DP, Foulkes DM, Eyers PA (January 2017). "Pseudokinases: update on their functions and evaluation as new drug targets". Future Medicinal Chemistry. 9 (2): 245–265. doi:10.4155/fmc-2016-0207. PMID 28097887.
  20. ^ Bailey FP, Byrne DP, McSkimming D, Kannan N, Eyers PA (January 2015). "Going for broke: targeting the human cancer pseudokinome". The Biochemical Journal. 465 (2): 195–211. doi:10.1042/BJ20141060. PMID 25559089.
  21. ^ Cowan-Jacob SW, Jahnke W, Knapp S (April 2014). "Novel approaches for targeting kinases: allosteric inhibition, allosteric activation and pseudokinases". Future Medicinal Chemistry. 6 (5): 541–61. doi:10.4155/fmc.13.216. PMID 24649957.
  22. ^ Foulkes DM, Byrne DP, Bailey FP, Eyers PA (October 2015). "Tribbles pseudokinases: novel targets for chemical biology and drug discovery?". Biochemical Society Transactions. 43 (5): 1095–103. doi:10.1042/BST20150109. PMID 26517930.
  23. ^ Cui J, Zhu Q, Zhang H, Cianfrocco MA, Leschziner AE, Dixon JE, Xiao J (April 2017). "Structure of Fam20A reveals a pseudokinase featuring a unique disulfide pattern and inverted ATP-binding". eLife. 6. doi:10.7554/eLife.23990. PMC 5413348. PMID 28432788.
  24. ^ Cui J, Xiao J, Tagliabracci VS, Wen J, Rahdar M, Dixon JE (March 2015). "A secretory kinase complex regulates extracellular protein phosphorylation". eLife. 4: e06120. doi:10.7554/eLife.06120. PMC 4421793. PMID 25789606.
  25. ^ Tagliabracci VS, Wiley SE, Guo X, Kinch LN, Durrant E, Wen J, Xiao J, Cui J, Nguyen KB, Engel JL, Coon JJ, Grishin N, Pinna LA, Pagliarini DJ, Dixon JE (June 2015). "A Single Kinase Generates the Majority of the Secreted Phosphoproteome". Cell. 161 (7): 1619–32. doi:10.1016/j.cell.2015.05.028. PMC 4963185. PMID 26091039.
  26. ^ Kwon A, Scott S, Taujale R, Yeung W, Kochut KJ, Eyers PA, Kannan N (April 2019). "Tracing the origin and evolution of pseudokinases across the tree of life". Science Signaling. 12 (578): eaav3810. doi:10.1126/scisignal.aav3810. PMC 6997932. PMID 31015289.

Further reading

[edit]
[edit]
Retrieved from "https://en.wikipedia.org/w/index.php?title=Pseudokinase&oldid=1188211490"