Pseudokinase

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Pseudokinases bụ ụdị na_ezughi dịka katalist nke pseudoenzyme na-enweghị ihe ọ bụla [1] nke protin kinases nke a na-anọchite anya na kinomes niile gafee alaeze nke ndụ. Pseudokinases nwere ma ọrụ fisiolojikal (ihe ngosi transdokshon ) na ọrụ pathophysiological.[2][3][4][5][6][7][8]

Akụkọ ihe mere eme[dezie | dezie ebe o si]

E chepụtara okwu pseudokinase n'afọ puku abụọ na abụọ .[9] E mechara kewaa ha n'ime 'Klaasị' dị iche iche.[10][8][11][12][13] A na-ahụ ọtụtụ ezinụlọ nwere pseudokinase na kinome mmadụ, gụnyere Tribbles pseudokinases, nke dị na intafeesi n'etiti kinase na ubiquitin E3 ligase signaling. [14][15][16]

Pseudokinases nke mmadụ (na ụmụnne ha pseudophosphatase) na-emetụta ọrịa dịgasị iche iche, [17] [18] nke mere ka ha bụrụ ndị ọgwụ na ndị na-egbochi ọrịa. [19] [20] [21][22] Pseudokinases mejupụtara ngwakọta evolushọn nke ukariotik protin kinase (ePK) na protein pseudoenzyme na-abụghị ePK (dịka, FAM20A, nke na-ejikọta ATP ma bụrụ pseudokinase n'ihi glutamate echekwara na glutamine swap na alpha-C helix. [23][24] FAM20A na-emetụta Ọrịa periodontal, ma na-arụ ọrụ iji chịkwaa ọrụ katalik nke FAM20C, casein kinase dị mkpa nke na-achịkwa phosphorylation nke protin na ngwaọrụ Golgi nke a kara aka maka ịgbapụta dị ka protein mmiri ara ehi casein.[25]

Nnyocha zuru oke nke evolushọn na-akwado na pseudokinases na-agbakọta n'ime ọtụtụ ndị okpuru ezinaụlọ a na-ahụkwa ndị a na kinome nke ihe ndị dị ndụ gafee alaeze nke ndụ, gụnyere prokaryotes, archaea na usoro ọmụmụ niile eukaryotic nwere proteome; nchọcho a nwere ike ịchọ na ProKino (http://vulcan.cs.edu/prokino/about/browser). [26]

  1. ↑ (April 2017) "Bio-Zombie: the rise of pseudoenzymes in biology". Biochemical Society Transactions 45 (2): 537–544. DOI:10.1042/BST20160400. PMID 28408493. 
  2. ↑ (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. ↑ (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. PMID 24107129. 
  4. ↑ (April 2008) "Rethinking pseudokinases". Cell 133 (2): 204–5. DOI:10.1016/j.cell.2008.04.005. PMID 18423189. 
  5. ↑ (April 2008) "CASK Functions as a Mg2+-independent neurexin kinase". Cell 133 (2): 328–39. DOI:10.1016/j.cell.2008.02.036. PMID 18423203. 
  6. ↑ (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. PMID 25583260. 
  7. ↑ (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. DOI:10.1073/pnas.1002753107. PMID 20351256. 
  8. ↑ 8.0 8.1 (December 2009) "Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation". Science 326 (5960): 1707–11. DOI:10.1126/science.1178377. PMID 19892943.  Kpọpụta njehie: Invalid <ref> tag; name "pmid19892943" defined multiple times with different content
  9. ↑ (December 2002) "The protein kinase complement of the human genome". Science 298 (5600): 1912–34. DOI:10.1126/science.1075762. PMID 12471243. 
  10. ↑ (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. ↑ (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. PMID 21074407. 
  12. ↑ (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. PMID 19141289. 
  13. ↑ (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. ↑ (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. PMID 27908682. 
  15. ↑ (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. PMID 30254057. 
  16. ↑ (September 2018) "Substrate binding allosterically relieves autoinhibition of the pseudokinase TRIB1". Science Signaling 11 (549): eaau0597. DOI:10.1126/scisignal.aau0597. PMID 30254053. 
  17. ↑ (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. ↑ (April 2017) "Genomics and evolution of protein phosphatases". Science Signaling 10 (474): eaag1796. DOI:10.1126/scisignal.aag1796. PMID 28400531. 
  19. ↑ (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. ↑ (January 2015) "Going for broke: targeting the human cancer pseudokinome". The Biochemical Journal 465 (2): 195–211. DOI:10.1042/BJ20141060. PMID 25559089. 
  21. ↑ (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. ↑ (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. ↑ (April 2017) "Structure of Fam20A reveals a pseudokinase featuring a unique disulfide pattern and inverted ATP-binding". eLife 6. DOI:10.7554/eLife.23990. PMID 28432788. 
  24. ↑ (March 2015) "A secretory kinase complex regulates extracellular protein phosphorylation". eLife 4: e06120. DOI:10.7554/eLife.06120. PMID 25789606. 
  25. ↑ (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. PMID 26091039. 
  26. ↑ (April 2019) "Tracing the origin and evolution of pseudokinases across the tree of life". Science Signaling 12 (578): eaav3810. DOI:10.1126/scisignal.aav3810. PMID 31015289. 
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