Catalysis by the tumor-suppressor enzymes PTEN and PTEN-L

PLoS ONE

Volumn 10, Issue 1, 2015, Pages

  Johnston, Sean B ^a   Raines, Ronald T ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PHOSPHATE; PHOSPHATIDYLINOSITOL (4,5) BISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; UNCLASSIFIED DRUG; INORGANIC SALT; ISOENZYME; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PTEN PROTEIN, HUMAN;

ARTICLE; BINDING SITE; BIOASSAY; BIOCATALYSIS; CONTROLLED STUDY; DNA BINDING MOTIF; ENZYME ACTIVATION; ENZYME ACTIVITY; GENETIC VARIABILITY; MICHAELIS MENTEN KINETICS; NONHUMAN; RNA TRANSLATION; ALTERNATIVE RNA SPLICING; CHEMISTRY; GENETICS; HUMAN; METABOLISM;

ALTERNATIVE SPLICING; BINDING SITES; BIOCATALYSIS; ENZYME ACTIVATION; HUMANS; ISOENZYMES; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; PTEN PHOSPHOHYDROLASE; RNA, MESSENGER; SALTS;

EID: 84921824290     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0116898     Document Type: Article

References (39)

1. Eng C (2003) PTEN: One gene, many syndromes. Hum Mutat 22: 183-198. doi: 10.1002/humu.10257 PMID: 12938083
2. Worby CA, Dixon JE (2014) PTEN. Annu Rev Biochem 83: 641-669. doi: 10.1146/annurev-biochem- 082411-113907 PMID: 24905788
3. Pulido R, Baker SJ, Barata JT, Carracedo A, Cid VJ, et al. (2014) A unified nomenclature and amino acid numbering for human PTEN. Sci Signal 7: pe15. doi: 10.1126/scisignal.2005560 PMID: 24985344
4. Salmena L, Carracedo A, Pandolfi PP (2008) Tenets of PTEN tumor suppression. Cell 133: 403-414. doi: 10.1016/j.cell.2008.04.013 PMID: 18455982
5. Maehama T, Dixon JE (1998) The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 273: 13375-13378. doi: 10. 1074/jbc.273.22.13375 PMID: 9593664
6. Tamura M, Gu J, Danen E, Takino T, Miyamoto S, et al. (1999) PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway. J Biol Chem 274: 20693-20703. doi: 10.1074/jbc.274.29.20693 PMID: 10400703
7. Baker SJ (2007) PTEN enters the nuclear age. Cell 128: 25-28. doi: 10.1016/j.cell.2006.12.023 PMID: 17218252
8. Song MS, Salmena L, Pandolfi PP (2012) The functions and regulation of the PTEN tumour suppressor. Nat Rev Mol Cell Biol 13: 283-296. doi: 10.1038/nrm3330 PMID: 22473468
9. Lee J-O, Yang H, Georgescu M-M, Di Cristofano A, Maehama T, et al. (1999) Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association. Cell 99: 323-334. doi: 10.1016/S0092-8674(00)81663-3 PMID: 10555148
10. Denu JM, Stuckey JA, Saper MA, Dixon JE (1996) Form and function in protein dephosphorylation. Cell 87: 361-364. doi: 10.1016/S0092-8674(00)81356-2 PMID: 8898189
11. Alimonti A, Carracedo A, Clohessy JG, Trotman LC, Nardella C, et al. (2010) Subtle variations in Pten dose determine cancer susceptibility. Nat Genet 42: 454-U136. doi: 10.1038/ng.556 PMID: 20400965
12. Maehama T, Taylor GS, Dixon JE (2001) PTEN and myotubularin: Novel phosphoinositide phosphatases. Annu Rev Biochem 70: 247-279. doi: 10.1146/annurev.biochem.70.1.247 PMID: 11395408
13. Hess HH, Derr JE (1975) Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range. Anal Biochem 63: 607-613. doi: 10.1016/0003-2697(75)90388-7 PMID: 1122033
14. Maehama T, Taylor GS, Slama JT, Dixon JE (2000) A sensitive assay for phosphoinositide phosphatases. Anal Biochem 279: 248-250. doi: 10.1006/abio.2000.4497 PMID: 10706796
15. Taylor GS, Dixon JE (2003) PTEN and myotubularins: Families of phosphoinositide phosphatases. Methods Enzymol 366: 43-56. PMID: 14674238
16. McConnachie G, Pass I, Walker SM, Downes CP (2003) Interfacial kinetic analysis of the tumour suppressor phosphatase, PTEN: Evidence for activation by anionic phospholipids. Biochem J 371: 947-955. doi: 10.1042/BJ20021848 PMID: 12534371
17. Hopkins BD, Fine B, Steinbach N, Dendy M, Rapp Z, et al. (2013) A secreted PTEN phosphatase that enters cells to alter signaling and survival. Science 341: 399-402. doi: 10.1126/science.1234907 PMID: 23744781
18. Liang H, He S, Yang J, Jia X, Wang P, et al. (2014) PTENα, a PTEN isoform translated through alternative initiation, regulates mitochondrial function and energy metabolism. Cell Metab 19: 836-848. doi: 10.1016/j.cmet.2014.03.023 PMID: 24768297
19. Webb MR (1992) A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc Natl Acad Sci USA 89: 4884-4887. doi: 10. 1073/pnas.89.11.4884 PMID: 1534409
20. Campbell R, Liu F, Ross A (2003) Allosteric activation of PTEN phosphatase by phosphatidylinositol 4,5-bisphosphate. J Biol Chem 278: 33617-33620. doi: 10.1074/jbc.C300296200 PMID: 12857747
21. Papa A, Wan L, Bonora M, Salmena L, Song MS, et al. (2014) Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function Cell 157: 595-610. doi: 10.1016/j.cell. 2014.03.027 PMID: 24766807
22. Beck M, Schmidt A, Malmstroem J, Claassen M, Ori A, et al. (2011) The quantitative proteome of a human cell line. Mol Syst Biol 7: 549. doi: 10.1038/msb.2011.82 PMID: 22068332
23. nd ed. New York, NY: Oxford University Press. pp. 1-48.
24. McConnachie G, Pass I, Walker SM, Downes CP (2003) Interfacial kinetic analysis of the tumour suppressor phosphatase, PTEN: evidence for activation by anionic phospholipids. The Biochemical journal 371: 947-955. doi: 10.1042/BJ20021848 PMID: 12534371
25. Lee JO, Yang HJ, Georgescu MM, Di Cristofano A, Maehama T, et al. (1999) Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association. Cell 99: 323-334. doi: 10.1016/S0092-8674(00)81663-3 PMID: 10555148
26. Schaletzky J, Dove SK, Short B, Lorenzo O, Clague MJ, et al. (2003) Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases. Curr Biol 13: 504-509. doi: 10.1016/S0960-9822(03)00132-5 PMID: 12646134
27. Andersen JF, Ribeiro JMC (2006) A secreted salivary inositol polyphosphate 5-phosphatase from a blood-feeding insect: Allosteric activation by soluble phosphoinositides and phosphatidylserine. Biochemistry 45: 5450-5457. doi: 10.1021/bi052444j PMID: 16634626
28. Zhong S, Hsu F, Stefan CJ, Wu X, Patel A, et al. (2012) Allosteric activation of the phosphoinositide phosphatase Sac1 by anionic phospholipids. Biochemistry 51: 3170-3177. doi: 10.1021/bi300086c PMID: 22452743
29. Cornish-Bowden A (2014) Understanding allosteric and cooperative interactions in enzymes. FEBS J 281: 621-632. doi: 10.1111/febs.12469 PMID: 23910900
30. Martin TFJ (1998) Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking. Annu Rev Cell Dev Biol 14: 231-264. doi: 10. 1146/annurev.cellbio.14.1.231 PMID: 9891784
31. Lukesh JC III, Palte MJ, Raines RT (2012) A potent, versatile disulfide-reducing agent from aspartic acid. J Am Chem Soc 134: 4057-4059. doi: 10.1021/ja211931f PMID: 22353145
32. Park C, Raines RT (2001) Quantitative analysis of the effect of salt concentration on enzymatic catalysis. J Am Chem Soc 123: 11472-11479. doi: 10.1021/ja0164834 PMID: 11707126
33. Melander W, Horvath C (1977) Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series. Arch Biochem Biophys 183: 200-215. doi: 10.1016/0003-9861(77)90434-9 PMID: 907351
34. Baldwin RL (1996) How Hofmeister ion interactions affect protein stability. Biophys J 71: 2056-2063. doi: 10.1016/S0006-3495(96)79404-3 PMID: 8889180
35. Porter CM, Miller BG (2012) Cooperativity in monomeric enzymes with single ligand-binding sites. Bioorg Chem 43: 44-50. doi: 10.1016/j.bioorg.2011.11.001 PMID: 22137502
36. Turner T, Van Epps-Fung M, Kassis J, Wells A (1997) Molecular inhibition of phospholipase Cγ signaling abrogates DU-145 prostate tumor cell invasion. Clin Cancer Res 3: 2275-2282. PMID: 9815625
37. Monod J, Wyman J, Changeux JP (1965) On the nature of allosteric transitions: A plausible model. J Mol Biol 12: 88-118. doi: 10.1016/S0022-2836(65)80285-6 PMID: 14343300
38. Gibson DG, Young L, Chuang R-Y, Venter JC, Hutchison CA, et al. (2009) Enzymatic assembly of DNA molecules up to several hundred kilobases. Nature 6: 343-345. doi: 10.1038/nmeth.1318 PMID: 19363495
39. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72: 248-254. doi: 10.1016/0003-2697(76)90527-3 PMID: 942051