OpenLB
Open Library of Bioscience
Advanced Search
Life (Basel, Switzerland)
May 08, 2020;10 (5):

Targeting the C-Terminal Domain Small Phosphatase 1.

Harikrishna Reddy Rallabandi, Palanivel Ganesan, Young Jun Kim
Author Information
  1. Harikrishna Reddy Rallabandi: Department of Medicinal Biosciences and Nanotechnology Research Center, Konkuk University, Chungju 27478, Korea.
  2. Palanivel Ganesan: Department of Medicinal Biosciences and Nanotechnology Research Center, Konkuk University, Chungju 27478, Korea.
  3. Young Jun Kim: Department of Medicinal Biosciences and Nanotechnology Research Center, Konkuk University, Chungju 27478, Korea.
PMID: 32397221 DOI: 10.3390/life10050057

Abstract

The human C-terminal domain small phosphatase 1 (CTDSP1/SCP1) is a protein phosphatase with a conserved catalytic site of DXDXT/V. CTDSP1's major activity has been identified as dephosphorylation of the 5th Ser residue of the tandem heptad repeat of the RNA polymerase II C-terminal domain (RNAP II CTD). It is also implicated in various pivotal biological activities, such as acting as a driving factor in repressor element 1 (RE-1)-silencing transcription factor (REST) complex, which silences the neuronal genes in non-neuronal cells, G1/S phase transition, and osteoblast differentiation. Recent findings have denoted that negative regulation of CTDSP1 results in suppression of cancer invasion in neuroglioma cells. Several researchers have focused on the development of regulating materials of CTDSP1, due to the significant roles it has in various biological activities. In this review, we focused on this emerging target and explored the biological significance, challenges, and opportunities in targeting CTDSP1 from a drug designing perspective.

Keywords

CTDSP1 allosteric docking drug design ensemble docking

References

  1. Sci Rep. 2018 Jan 16;8(1):849 [PMID: 29339792]
  2. J Mol Biol. 1996 Aug 23;261(3):470-89 [PMID: 8780787]
  3. EMBO J. 2006 Jun 21;25(12):2757-67 [PMID: 16724108]
  4. Curr Pharm Des. 2019;25(31):3339-3349 [PMID: 31480998]
  5. ChemMedChem. 2007 Dec;2(12):1674-92 [PMID: 17952881]
  6. J Chem Inf Model. 2012 Jan 23;52(1):187-98 [PMID: 22146074]
  7. Curr Pharm Des. 2012;18(20):2936-45 [PMID: 22571662]
  8. Chem Biol. 2003 Sep;10(9):787-97 [PMID: 14522049]
  9. Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6596-601 [PMID: 17420445]
  10. Mol Biol Cell. 2015 Jul 15;26(14):2698-711 [PMID: 26023089]
  11. Mol Cell. 2008 Nov 21;32(4):478-90 [PMID: 19026779]
  12. Neuropsychopharmacology. 2009 Jan;34(1):106-25 [PMID: 18800070]
  13. Bioorg Med Chem. 2010 Jul 15;18(14):5148-56 [PMID: 20573514]
  14. Curr Top Med Chem. 2019;19(19):1694-1711 [PMID: 31237210]
  15. RNA. 2015 Jun;21(6):1135-46 [PMID: 25883047]
  16. J Mol Model. 2019 Aug 26;25(9):272 [PMID: 31451955]
  17. Comput Struct Biotechnol J. 2013 Apr 02;5:e201302011 [PMID: 24688704]
  18. Cardiovasc Drugs Ther. 2016 Feb;30(1):59-64 [PMID: 26768480]
  19. Methods Mol Biol. 2018;1824:195-215 [PMID: 30039408]
  20. J Comput Aided Mol Des. 2012 Jun;26(6):675-86 [PMID: 22569591]
  21. J Chem Inf Model. 2010 Jan;50(1):186-93 [PMID: 20000587]
  22. Med Chem. 2013 Nov;9(7):955-67 [PMID: 23106285]
  23. Methods Mol Biol. 2017;1561:109-138 [PMID: 28236236]
  24. Essays Biochem. 2017 Nov 8;61(5):431-437 [PMID: 29118091]
  25. Int J Mol Sci. 2019 Sep 15;20(18): [PMID: 31540192]
  26. Proteins. 2007 Feb 1;66(2):399-421 [PMID: 17096427]
  27. J Mol Graph Model. 2017 Jun;74:193-202 [PMID: 28499269]
  28. J Comput Aided Mol Des. 1997 May;11(3):209-28 [PMID: 9263849]
  29. J Med Chem. 2005 Oct 6;48(20):6504-15 [PMID: 16190776]
  30. J Comput Aided Mol Des. 2014 Jul;28(7):779-94 [PMID: 24980648]
  31. Am J Transl Res. 2015 Jun 15;7(6):1106-15 [PMID: 26279754]
  32. J Mol Biol. 1997 Apr 4;267(3):727-48 [PMID: 9126849]
  33. J Mol Graph Model. 2016 Nov;70:275-283 [PMID: 27771575]
  34. Nucleic Acids Res. 2011 Jan;39(Database issue):D663-9 [PMID: 21051350]
  35. Curr Top Med Chem. 2018;18(12):998-1006 [PMID: 30101712]
  36. Proc Natl Acad Sci U S A. 2011 Aug 30;108(35):14509-14 [PMID: 21873248]
  37. Proteins. 1998 Oct 1;33(1):74-87 [PMID: 9741846]
  38. PLoS One. 2015 Mar 30;10(3):e0117955 [PMID: 25822509]
  39. Nat Commun. 2016 Aug 26;7:12477 [PMID: 27561351]
  40. Biophys Rev. 2017 Apr;9(2):91-102 [PMID: 28510083]
  41. J Biomol Struct Dyn. 2019 Dec 26;:1-16 [PMID: 31838955]
  42. ChemMedChem. 2009 Jun;4(6):923-33 [PMID: 19434656]
  43. Proc Natl Acad Sci U S A. 2011 Nov 15;108(46):18649-54 [PMID: 21949367]
  44. J Chem Inf Model. 2018 Nov 26;58(11):2331-2342 [PMID: 30299094]
  45. J Comput Aided Mol Des. 2017 Aug;31(8):743-753 [PMID: 28653253]
  46. J Med Chem. 2004 Mar 25;47(7):1739-49 [PMID: 15027865]
  47. Nat Protoc. 2016 May;11(5):905-19 [PMID: 27077332]
  48. Expert Opin Drug Metab Toxicol. 2013 Apr;9(4):441-57 [PMID: 23286281]
  49. Protein Sci. 2020 Jan;29(1):76-86 [PMID: 31576621]
  50. Mol Pharmacol. 2013 Dec;84(6):794-807 [PMID: 24021214]
  51. J Biol Chem. 2006 Dec 29;281(52):40412-9 [PMID: 17085434]
  52. Cancer Res. 2014 Dec 1;74(23):6935-46 [PMID: 25293974]
  53. Curr Opin Chem Biol. 2006 Jun;10(3):194-202 [PMID: 16675286]
  54. Quant Imaging Med Surg. 2017 Oct;7(5):532-536 [PMID: 29184765]
  55. Sensors (Basel). 2016 Apr 08;16(4): [PMID: 27070617]
  56. Int J Mol Sci. 2019 Jun 06;20(11): [PMID: 31174387]
  57. Proteins. 2003 Sep 1;52(4):609-23 [PMID: 12910460]
  58. ACS Chem Biol. 2011 May 20;6(5):511-9 [PMID: 21348431]
  59. J Chem Inf Model. 2015 Feb 23;55(2):343-53 [PMID: 25564966]
  60. PLoS One. 2014 May 15;9(5):e97668 [PMID: 24831294]
  61. Ann Oncol. 2006 Dec;17(12):1772-6 [PMID: 17071934]
  62. Mol Pharmacol. 2009 Jun;75(6):1249-61 [PMID: 19299564]
  63. BMC Pharmacol Toxicol. 2017 Apr 28;18(1):18 [PMID: 28449705]
  64. J Med Chem. 2005 Feb 24;48(4):1088-97 [PMID: 15715476]
  65. J Microbiol Biotechnol. 2017 May 28;27(5):878-895 [PMID: 28238001]
  66. Biochemistry. 2015 Jan 20;54(2):497-504 [PMID: 25519989]
  67. J Cell Biochem. 2014 Dec;115(12):2208-17 [PMID: 25147082]
  68. Proteins. 2017 May;85(5):924-937 [PMID: 28168752]
  69. J Chem Inf Model. 2014 Jul 28;54(7):2127-38 [PMID: 24881672]
  70. Nat Rev Mol Cell Biol. 2017 Apr;18(4):263-273 [PMID: 28248323]
  71. PeerJ. 2019 Jul 25;7:e7362 [PMID: 31380152]
  72. Cell Discov. 2020 Mar 16;6:14 [PMID: 32194980]
  73. J Comput Aided Mol Des. 2008 Sep;22(9):621-7 [PMID: 18253700]
  74. Cell Cycle. 2016;15(3):357-67 [PMID: 26637059]
  75. J Chem Inf Model. 2006 Jul-Aug;46(4):1795-805 [PMID: 16859311]
  76. Curr Comput Aided Drug Des. 2020;16(4):389-401 [PMID: 31244429]
  77. Biosci Rep. 2019 Dec 20;39(12): [PMID: 31774910]
  78. Int J Mol Sci. 2016 Apr 20;17(4): [PMID: 27104528]
  79. Infect Dis Clin North Am. 2009 Jun;23(2):277-93 [PMID: 19393909]
  80. Adv Protein Chem Struct Biol. 2013;92:63-91 [PMID: 23954099]
  81. Elife. 2017 Mar 31;6: [PMID: 28440748]
  82. Mol Cell. 2006 Dec 8;24(5):759-770 [PMID: 17157258]
  83. Mol Cell. 2004 Aug 13;15(3):399-407 [PMID: 15304220]
  84. Biochem Biophys Res Commun. 2014 May 30;448(2):189-94 [PMID: 24769477]
  85. J Biol Chem. 2016 May 27;291(22):11518-28 [PMID: 26975371]
  86. PLoS Comput Biol. 2018 Dec 7;14(12):e1006651 [PMID: 30532261]
  87. FEBS Lett. 2015 Sep 14;589(19 Pt B):2769-75 [PMID: 26296318]
  88. Biochem Soc Trans. 2011 Oct;39(5):1327-33 [PMID: 21936810]
  89. Breast Cancer Res. 2012 Sep 20;14(5):R127 [PMID: 22995475]
  90. Biopolymers. 2007 Jan;85(1):38-59 [PMID: 17009317]
  91. Acta Pharmacol Sin. 2020 Mar 9;: [PMID: 32152439]
  92. Oncogene. 2016 Jan 28;35(4):491-500 [PMID: 25893300]
  93. Oncotarget. 2015 Aug 14;6(23):19580-91 [PMID: 26023736]
  94. AAPS J. 2012 Mar;14(1):133-41 [PMID: 22281989]
  95. ChemMedChem. 2013 Oct;8(10):1629-33 [PMID: 23894090]
  96. Adv Exp Med Biol. 2010;680:481-8 [PMID: 20865533]
  97. Structure. 1994 Jul 15;2(7):577-87 [PMID: 7922037]
  98. J Pharmacol Exp Ther. 2007 Jan;320(1):1-13 [PMID: 16803859]
  99. Endocrinol Metab Clin North Am. 2010 Dec;39(4):811-26 [PMID: 21095547]
  100. J Mol Biol. 2016 Jun 19;428(12):2607-2622 [PMID: 26876604]
  101. PLoS One. 2017 Oct 31;12(10):e0186869 [PMID: 29088253]
  102. Curr Comput Aided Drug Des. 2011 Jun;7(2):146-57 [PMID: 21534921]
  103. BMB Rep. 2014 Apr;47(4):192-6 [PMID: 24755554]
  104. PLoS One. 2013 May 07;8(5):e62981 [PMID: 23667555]
  105. J Cheminform. 2016 Jan 18;8:1 [PMID: 26807156]
  106. Diabetes. 2017 Jul;66(7):2019-2032 [PMID: 28341696]
  107. Curr Opin Struct Biol. 2011 Apr;21(2):189-99 [PMID: 21292475]
  108. J Med Chem. 2013 Sep 26;56(18):7382-95 [PMID: 23961916]
  109. J Chem Inf Model. 2012 Oct 22;52(10):2697-704 [PMID: 23005250]
  110. J Cell Physiol. 2018 Jan;233(1):559-571 [PMID: 28345763]
  111. Proc Natl Acad Sci U S A. 2014 Sep 16;111(37):E3929-36 [PMID: 25197063]
  112. Methods Mol Biol. 2012;819:105-26 [PMID: 22183533]
  113. Mini Rev Med Chem. 2004 Sep;4(7):779-91 [PMID: 15379645]
  114. Curr Med Chem. 2010;17(1):25-41 [PMID: 19941480]
  115. Oncogene. 2016 Sep 8;35(36):4730-40 [PMID: 26804175]
  116. Mol Cell Biol. 2002 Nov;22(21):7543-52 [PMID: 12370301]
  117. Expert Opin Drug Discov. 2010 Nov;5(11):1039-45 [PMID: 21116481]
  118. J Comput Aided Mol Des. 2011 Jan;25(1):13-9 [PMID: 21053052]
  119. Oncogene. 2016 Sep 29;35(39):5191-201 [PMID: 26996671]
  120. J Comput Aided Mol Des. 2018 Jan;32(1):187-198 [PMID: 28887659]
  121. Methods Mol Biol. 2012;819:157-68 [PMID: 22183536]
  122. J Phys Chem B. 2015 Jan 22;119(3):1026-34 [PMID: 25198248]
  123. J Biol Chem. 2003 Jul 11;278(28):26078-85 [PMID: 12721286]
  124. J Cell Mol Med. 2016 Apr;20(4):666-77 [PMID: 26828791]
  125. Science. 2005 Jan 28;307(5709):596-600 [PMID: 15681389]
  126. Nat Biotechnol. 2014 Nov;32(11):1113-20 [PMID: 25380447]
  127. Biophys Chem. 2010 Aug;150(1-3):88-97 [PMID: 20167416]
  128. J Photochem Photobiol B. 2017 Feb;167:299-308 [PMID: 28122297]
  129. Nat Rev Cancer. 2013 Jun;13(6):425-31 [PMID: 23660784]
  130. Expert Opin Biol Ther. 2016 Dec;16(12):1469-1478 [PMID: 27618260]
  131. Protein Sci. 2010 May;19(5):974-86 [PMID: 20222012]
  132. Bioorg Med Chem. 2016 Oct 15;24(20):4928-4935 [PMID: 27543390]
  133. J Biol Chem. 2018 Oct 26;293(43):16851-16861 [PMID: 30217818]
  134. Int J Mol Sci. 2020 Jan 28;21(3): [PMID: 32013012]
  135. Curr Top Med Chem. 2017;17(20):2235-2259 [PMID: 28240180]
  136. J Comput Aided Mol Des. 2001 May;15(5):411-28 [PMID: 11394736]
  137. J Chem Inf Model. 2017 Apr 24;57(4):742-756 [PMID: 28388074]
  138. J Struct Funct Genomics. 2007 Sep;8(2-3):121-40 [PMID: 18058037]
  139. Trials. 2014 Jul 29;15:303 [PMID: 25069975]
  140. J Med Chem. 2004 Mar 25;47(7):1750-9 [PMID: 15027866]
  141. Expert Opin Investig Drugs. 2015 May;24(5):673-87 [PMID: 25599887]
  142. Methods Mol Biol. 2007;365:335-46 [PMID: 17200573]
  143. Molecules. 2015 Sep 10;20(9):16435-45 [PMID: 26378508]
  144. J Chem Inf Model. 2010 Apr 26;50(4):511-24 [PMID: 20222690]
  145. Breast Cancer Res. 2014 Jan 30;16(1):R16 [PMID: 24479521]
  146. Curr Top Med Chem. 2019;19(29):2687-2707 [PMID: 31702505]
  147. J Biol Chem. 1998 Oct 16;273(42):27593-601 [PMID: 9765293]
  148. Biochem J. 2015 Jul 15;469(2):289-98 [PMID: 25990325]
  149. Future Med Chem. 2014 Apr;6(5):541-61 [PMID: 24649957]
  150. Signal Transduct Target Ther. 2020 Feb 7;5(1):8 [PMID: 32296030]

Grants

  1. 2019R1F1A1059216 and 2016R1D1A1B03932519/National Research Foundation of Korea
Journal Article Review
Article has an altmetric score of 1

Word Cloud

Created with Highcharts 10.0.0CTDSP11biologicalC-terminaldomainphosphataseIIvariousactivitiesfactorcellsfocuseddrugdockinghumansmallCTDSP1/SCP1proteinconservedcatalyticsiteDXDXT/VCTDSP1'smajoractivityidentifieddephosphorylation5thSerresiduetandemheptadrepeatRNApolymeraseRNAPCTDalsoimplicatedpivotalactingdrivingrepressorelementRE-1-silencingtranscriptionRESTcomplexsilencesneuronalgenesnon-neuronalG1/SphasetransitionosteoblastdifferentiationRecentfindingsdenotednegativeregulationresultssuppressioncancerinvasionneurogliomaSeveralresearchersdevelopmentregulatingmaterialsduesignificantrolesreviewemergingtargetexploredsignificancechallengesopportunitiestargetingdesigningperspectiveTargetingC-TerminalDomainSmallPhosphataseallostericdesignensemble

Similar Articles

Cited By