메뉴 건너뛰기




Volumn 83, Issue , 2014, Pages 641-669

Pten

Author keywords

cancer; phosphatase; tumor suppressor

Indexed keywords

LONG UNTRANSLATED RNA; MICRORNA; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; LIPID; OXYGEN; PTEN PROTEIN, HUMAN; UBIQUITIN;

EID: 84902129859     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-082411-113907     Document Type: Review
Times cited : (466)

References (207)
  • 1
    • 0030936323 scopus 로고    scopus 로고
    • PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer
    • Li J, Yen C, Liaw D, Podsypanina K, Bose S, et al. 1997. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science 275:1943-47
    • (1997) Science , vol.275 , pp. 1943-1947
    • Li, J.1    Yen, C.2    Liaw, D.3    Podsypanina, K.4    Bose, S.5
  • 2
    • 17144436629 scopus 로고    scopus 로고
    • Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers
    • Steck PA, Pershouse MA, Jasser SA, Yung WK, Lin H, et al. 1997. Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers. Nat. Genet. 15:356-62
    • (1997) Nat. Genet , vol.15 , pp. 356-362
    • Steck, P.A.1    Pershouse, M.A.2    Jasser, S.A.3    Yung, W.K.4    Lin, H.5
  • 3
    • 0031004088 scopus 로고    scopus 로고
    • Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome
    • Liaw D, Marsh DJ, Li J, Dahia PL, Wang SI, et al. 1997. Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome. Nat. Genet. 16:64-67
    • (1997) Nat. Genet , vol.16 , pp. 64-67
    • Liaw, D.1    Marsh, D.J.2    Li, J.3    Dahia, P.L.4    Wang, S.I.5
  • 4
    • 0031985674 scopus 로고    scopus 로고
    • Phosphatases and tumorigenesis
    • Parsons R. 1998. Phosphatases and tumorigenesis. Curr. Opin. Oncol. 10:88-91
    • (1998) Curr. Opin. Oncol , vol.10 , pp. 88-91
    • Parsons, R.1
  • 5
    • 7344227886 scopus 로고    scopus 로고
    • Point mutation and homozygous deletion of PTEN/MMAC1 in primary bladder cancers
    • Cairns P, Evron E, Okami K, Halachmi N, Esteller M, et al. 1998. Point mutation and homozygous deletion of PTEN/MMAC1 in primary bladder cancers. Oncogene 16:3215-18
    • (1998) Oncogene , vol.16 , pp. 3215-3218
    • Cairns, P.1    Evron, E.2    Okami, K.3    Halachmi, N.4    Esteller, M.5
  • 7
    • 13144249184 scopus 로고    scopus 로고
    • High cancer susceptibility and embryonic lethality associated with mutation of the PTEN tumor suppressor gene in mice
    • Suzuki A, de la Pompa JL, Stambolic V, Elia AJ, Sasaki T, et al. 1998. High cancer susceptibility and embryonic lethality associated with mutation of the PTEN tumor suppressor gene in mice. Curr. Biol. 8:1169-78
    • (1998) Curr. Biol , vol.8 , pp. 1169-1178
    • Suzuki, A.1    De La Pompa, J.L.2    Stambolic, V.3    Elia, A.J.4    Sasaki, T.5
  • 10
    • 0031001041 scopus 로고    scopus 로고
    • TEP1, encoded by a candidate tumor suppressor locus, is a novel protein tyrosine phosphatase regulated by transforming growth factor ?
    • Li DM, Sun H. 1997. TEP1, encoded by a candidate tumor suppressor locus, is a novel protein tyrosine phosphatase regulated by transforming growth factor ?. Cancer Res. 57:2124-29
    • (1997) Cancer Res , vol.57 , pp. 2124-2129
    • Li, D.M.1    Sun, H.2
  • 11
    • 0032486198 scopus 로고    scopus 로고
    • Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN
    • Tamura M, Gu J, Matsumoto K, Aota S, Parsons R, Yamada KM. 1998. Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN. Science 280:1614-17
    • (1998) Science , vol.280 , pp. 1614-1617
    • Tamura, M.1    Gu, J.2    Matsumoto, K.3    Aota, S.4    Parsons, R.5    Yamada, K.M.6
  • 12
    • 0030837555 scopus 로고    scopus 로고
    • P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase
    • Myers MP, Stolarov JP, Eng C, Li J, Wang SI, et al. 1997. P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase. Proc. Natl. Acad. Sci. USA 94:9052-57
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9052-9057
    • Myers, M.P.1    Stolarov, J.P.2    Eng, C.3    Li, J.4    Wang, S.I.5
  • 13
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama T, Dixon JE. 1998. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273:13375-78
    • (1998) J. Biol. Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 14
    • 0032904432 scopus 로고    scopus 로고
    • PTEN: A tumour suppressor that functions as a phospholipid phosphatase
    • Maehama T,Dixon JE. 1999. PTEN: a tumour suppressor that functions as a phospholipid phosphatase. Trends Cell Biol. 9:125-28
    • (1999) Trends Cell Biol , vol.9 , pp. 125-128
    • Maehama, T.1    Dixon, J.E.2
  • 16
    • 0023665111 scopus 로고
    • Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity
    • Kaplan DR,Whitman M, Schaffhausen B, Pallas DC,White M, et al. 1987. Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity. Cell 50:1021-29
    • (1987) Cell , vol.50 , pp. 1021-1029
    • Kaplan, D.R.1    Whitman, M.2    Schaffhausen, B.3    Pallas, D.C.4    White, M.5
  • 17
    • 0021828496 scopus 로고
    • Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation
    • Whitman M, Kaplan DR, Schaffhausen B, Cantley L, Roberts TM. 1985. Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation. Nature 315:239-42
    • (1985) Nature , vol.315 , pp. 239-242
    • Whitman, M.1    Kaplan, D.R.2    Schaffhausen, B.3    Cantley, L.4    Roberts, T.M.5
  • 18
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • Engelman JA, Luo J, Cantley LC. 2006. The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat. Rev. Genet. 7:606-19
    • (2006) Nat. Rev. Genet , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 20
    • 70350405643 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase-regulated adapters in lymphocyte activation
    • Zhang TT, Li H, Cheung SM, Costantini JL, Hou S, et al. 2009. Phosphoinositide 3-kinase-regulated adapters in lymphocyte activation. Immunol. Rev. 232:255-72
    • (2009) Immunol. Rev , vol.232 , pp. 255-272
    • Zhang, T.T.1    Li, H.2    Cheung, S.M.3    Costantini, J.L.4    Hou, S.5
  • 22
    • 84879184496 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,4,5-trisphosphate: Tool of choice for class i PI 3-kinases
    • Salamon RS, Backer JM. 2013. Phosphatidylinositol-3,4,5-trisphosphate: tool of choice for class I PI 3-kinases. BioEssays 35:602-11
    • (2013) BioEssays , vol.35 , pp. 602-611
    • Salamon, R.S.1    Backer, J.M.2
  • 23
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley LC. 2002. The phosphoinositide 3-kinase pathway. Science 296:1655-57
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 25
    • 0036849331 scopus 로고    scopus 로고
    • PKB binding proteins. Getting in on the Akt
    • Brazil DP, Park J, Hemmings BA. 2002. PKB binding proteins. Getting in on the Akt. Cell 111:293-303
    • (2002) Cell , vol.111 , pp. 293-303
    • Brazil, D.P.1    Park, J.2    Hemmings, B.A.3
  • 26
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • Manning BD, Cantley LC. 2007. AKT/PKB signaling: navigating downstream. Cell 129:1261-74
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 27
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • Guertin DA, Sabatini DM. 2007. Defining the role of mTOR in cancer. Cancer Cell 12:9-22
    • (2007) Cancer Cell , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 28
    • 0032053709 scopus 로고    scopus 로고
    • Mechanisms and consequences of activation of protein kinase B/Akt
    • Downward J. 1998. Mechanisms and consequences of activation of protein kinase B/Akt. Curr. Opin. Cell Biol. 10:262-67
    • (1998) Curr. Opin. Cell Biol , vol.10 , pp. 262-267
    • Downward, J.1
  • 29
    • 0032475861 scopus 로고    scopus 로고
    • Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
    • Stambolic V, Suzuki A, de la Pompa JL, Brothers GM, Mirtsos C, et al. 1998. Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN. Cell 95:29-39
    • (1998) Cell , vol.95 , pp. 29-39
    • Stambolic, V.1    Suzuki, A.2    De La Pompa, J.L.3    Brothers, G.M.4    Mirtsos, C.5
  • 30
    • 0032534963 scopus 로고    scopus 로고
    • The PTEN/MMAC1 tumor suppressor induces cell death that is rescued by the AKT/protein kinase B oncogene
    • Li J, Simpson L, Takahashi M, Miliaresis C, Myers MP, et al. 1998. The PTEN/MMAC1 tumor suppressor induces cell death that is rescued by the AKT/protein kinase B oncogene. Cancer Res. 58:5667-72
    • (1998) Cancer Res , vol.58 , pp. 5667-5672
    • Li, J.1    Simpson, L.2    Takahashi, M.3    Miliaresis, C.4    Myers, M.P.5
  • 31
    • 34548643512 scopus 로고    scopus 로고
    • Phosphoinositide phosphatases in a network of signalling reactions
    • Blero D, Payrastre B, Schurmans S, Erneux C. 2007. Phosphoinositide phosphatases in a network of signalling reactions. Pflüg. Arch. 455:31-44
    • (2007) Pflüg. Arch , vol.455 , pp. 31-44
    • Blero, D.1    Payrastre, B.2    Schurmans, S.3    Erneux, C.4
  • 32
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G, De Camilli P. 2006. Phosphoinositides in cell regulation and membrane dynamics. Nature 443:651-57
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 33
    • 84870017064 scopus 로고    scopus 로고
    • An introduction to phosphoinositides
    • Maffucci T. 2012. An introduction to phosphoinositides. Curr. Top. Microbiol. Immunol. 362:1-42
    • (2012) Curr. Top. Microbiol. Immunol , vol.362 , pp. 1-42
    • Maffucci, T.1
  • 34
    • 0028533592 scopus 로고
    • Tensin: A potential link between the cytoskeleton and signal transduction
    • Lo SH, Weisberg E, Chen LB. 1994. Tensin: a potential link between the cytoskeleton and signal transduction. BioEssays 16:817-23
    • (1994) BioEssays , vol.16 , pp. 817-823
    • Lo, S.H.1    Weisberg, E.2    Chen, L.B.3
  • 35
    • 0035128240 scopus 로고    scopus 로고
    • Expression of auxilin or AP180 inhibits endocytosis bymislocalizing clathrin: Evidence for formation of nascent pits containing AP1 or AP2 but not clathrin
    • Zhao X, Greener T, Al-Hasani H, Cushman SW, Eisenberg E, Greene LE. 2001. Expression of auxilin or AP180 inhibits endocytosis bymislocalizing clathrin: evidence for formation of nascent pits containing AP1 or AP2 but not clathrin. J. Cell Sci. 114:353-65
    • (2001) J. Cell Sci , vol.114 , pp. 353-365
    • Zhao, X.1    Greener, T.2    Al-Hasani, H.3    Cushman, S.W.4    Eisenberg, E.5    Greene, L.E.6
  • 36
    • 0029975476 scopus 로고    scopus 로고
    • Crystal structure of the dual specificity protein phosphatase VHR
    • Yuvaniyama J, Denu JM, Dixon JE, Saper MA. 1996. Crystal structure of the dual specificity protein phosphatase VHR. Science 272:1328-31
    • (1996) Science , vol.272 , pp. 1328-1331
    • Yuvaniyama, J.1    Denu, J.M.2    Dixon, J.E.3    Saper, M.A.4
  • 37
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association
    • Lee JO, Yang H, 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 99:323-34
    • (1999) Cell , vol.99 , pp. 323-334
    • Lee, J.O.1    Yang, H.2    Georgescu, M.M.3    Di Cristofano, A.4    Maehama, T.5
  • 39
    • 0033822632 scopus 로고    scopus 로고
    • Genomic structure of a copy of the human TPTE gene which encompasses 87 kb on the short arm of chromosome 21
    • Guipponi M, Yaspo ML, Riesselman L, Chen H, De Sario A, et al. 2000. Genomic structure of a copy of the human TPTE gene which encompasses 87 kb on the short arm of chromosome 21. Hum. Genet. 107:127-31
    • (2000) Hum. Genet , vol.107 , pp. 127-131
    • Guipponi, M.1    Yaspo, M.L.2    Riesselman, L.3    Chen, H.4    De Sario, A.5
  • 40
    • 0345059066 scopus 로고    scopus 로고
    • The TPTE gene family: Cellular expression, subcellular localization and alternative splicing
    • Tapparel C, Reymond A, Girardet C, Guillou L, Lyle R, et al. 2003. The TPTE gene family: cellular expression, subcellular localization and alternative splicing. Gene 323:189-99
    • (2003) Gene , vol.323 , pp. 189-199
    • Tapparel, C.1    Reymond, A.2    Girardet, C.3    Guillou, L.4    Lyle, R.5
  • 41
    • 0032706145 scopus 로고    scopus 로고
    • A testis-specific gene, TPTE, encodes a putative transmembrane tyrosine phosphatase and maps to the pericentromeric region of human chromosomes 21 and 13, and to chromosomes 15, 22, and y
    • Chen H, Rossier C, Morris MA, Scott HS, Gos A, et al. 1999. A testis-specific gene, TPTE, encodes a putative transmembrane tyrosine phosphatase and maps to the pericentromeric region of human chromosomes 21 and 13, and to chromosomes 15, 22, and Y. Hum. Genet. 105:399-409
    • (1999) Hum. Genet , vol.105 , pp. 399-409
    • Chen, H.1    Rossier, C.2    Morris, M.A.3    Scott, H.S.4    Gos, A.5
  • 42
    • 0035605844 scopus 로고    scopus 로고
    • TPIP: A novel phosphoinositide 3-phosphatase
    • Walker SM, Downes CP, Leslie NR. 2001. TPIP: a novel phosphoinositide 3-phosphatase. Biochem. J. 360:277-83
    • (2001) Biochem. J , vol.360 , pp. 277-283
    • Walker, S.M.1    Downes, C.P.2    Leslie, N.R.3
  • 43
    • 82555202982 scopus 로고    scopus 로고
    • A novel human TPIP splice-variant (TPIP-C2) mRNA, expressed in human and mouse tissues, strongly inhibits cell growth in HeLa cells
    • Mishra RR, Chaudhary JK, Bajaj GD, Rath PC. 2011. A novel human TPIP splice-variant (TPIP-C2) mRNA, expressed in human and mouse tissues, strongly inhibits cell growth in HeLa cells. PLoS ONE 6:e28433
    • (2011) PLoS ONE , vol.6
    • Mishra, R.R.1    Chaudhary, J.K.2    Bajaj, G.D.3    Rath, P.C.4
  • 44
    • 84864286604 scopus 로고    scopus 로고
    • Cell cycle arrest and apoptosis by expression of a novel TPIP (TPIP-C2) cDNA encoding a C2-domain in HEK-293 cells
    • Mishra RR, Chaudhary JK, Rath PC. 2012. Cell cycle arrest and apoptosis by expression of a novel TPIP (TPIP-C2) cDNA encoding a C2-domain in HEK-293 cells. Mol. Biol. Rep. 39:7389-402
    • (2012) Mol. Biol. Rep , vol.39 , pp. 7389-7402
    • Mishra, R.R.1    Chaudhary, J.K.2    Rath, P.C.3
  • 45
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • Murata Y, Iwasaki H, Sasaki M, Inaba K, Okamura Y. 2005. Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature 435:1239-43
    • (2005) Nature , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 46
    • 34548725637 scopus 로고    scopus 로고
    • Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2
    • Murata Y, Okamura Y. 2007. Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2. J. Physiol. 583:875-89
    • (2007) J. Physiol , vol.583 , pp. 875-889
    • Murata, Y.1    Okamura, Y.2
  • 47
    • 45849122833 scopus 로고    scopus 로고
    • A voltage-sensing phosphatase, Ci-VSP, which shares sequence identity with PTEN, dephosphorylates phosphatidylinositol 4,5-bisphosphate
    • Iwasaki H, Murata Y, Kim Y, Hossain MI, Worby CA, et al. 2008. A voltage-sensing phosphatase, Ci-VSP, which shares sequence identity with PTEN, dephosphorylates phosphatidylinositol 4,5-bisphosphate. Proc. Natl. Acad. Sci. USA 105:7970-75
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7970-7975
    • Iwasaki, H.1    Murata, Y.2    Kim, Y.3    Hossain, M.I.4    Worby, C.A.5
  • 48
    • 79955069961 scopus 로고    scopus 로고
    • Voltage-sensing phosphatase: Its molecular relationship with PTEN
    • Okamura Y, Dixon JE. 2011. Voltage-sensing phosphatase: its molecular relationship with PTEN. Physiology 26:6-13
    • (2011) Physiology , vol.26 , pp. 6-13
    • Okamura, Y.1    Dixon, J.E.2
  • 49
    • 77955445443 scopus 로고    scopus 로고
    • Self-organization of the phosphatidylinositol lipids signaling system for
    • random cell migration
    • Arai Y, Shibata T, Matsuoka S, Sato MJ, Yanagida T, Ueda M. 2010. Self-organization of the phosphatidylinositol lipids signaling system for random cell migration. Proc. Natl. Acad. Sci. USA 107:12399-404
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12399-12404
    • Arai, Y.1    Shibata, T.2    Matsuoka, S.3    Sato, M.J.4    Yanagida, T.5    Ueda, M.6
  • 50
    • 0037205265 scopus 로고    scopus 로고
    • Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis
    • Funamoto S, Meili R, Lee S, Parry L, Firtel RA. 2002. Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis. Cell 109:611-23
    • (2002) Cell , vol.109 , pp. 611-623
    • Funamoto, S.1    Meili, R.2    Lee, S.3    Parry, L.4    Firtel, R.A.5
  • 51
    • 79951828073 scopus 로고    scopus 로고
    • Disruption of PKB signaling restores polarity to cells lacking tumor suppressor PTEN
    • Tang M, Iijima M, Kamimura Y, Chen L, Long Y, Devreotes P. 2011. Disruption of PKB signaling restores polarity to cells lacking tumor suppressor PTEN. Mol. Biol. Cell 22:437-47
    • (2011) Mol. Biol. Cell , vol.22 , pp. 437-447
    • Tang, M.1    Iijima, M.2    Kamimura, Y.3    Chen, L.4    Long, Y.5    Devreotes, P.6
  • 52
    • 34548258389 scopus 로고    scopus 로고
    • PTEN plays a role in the suppression of lateral pseudopod formation during Dictyostelium motility and chemotaxis
    • Wessels D, Lusche DF, Kuhl S, Heid P, Soll DR. 2007. PTEN plays a role in the suppression of lateral pseudopod formation during Dictyostelium motility and chemotaxis. J. Cell Sci. 120:2517-31
    • (2007) J. Cell Sci , vol.120 , pp. 2517-2531
    • Wessels, D.1    Lusche, D.F.2    Kuhl, S.3    Heid, P.4    Soll, D.R.5
  • 53
    • 0042354714 scopus 로고    scopus 로고
    • Divergent signals and cytoskeletal assemblies regulate self-organizing polarity in neutrophils
    • Xu J, Wang F, Van Keymeulen A,Herzmark P, Straight A, et al. 2003. Divergent signals and cytoskeletal assemblies regulate self-organizing polarity in neutrophils. Cell 114:201-14
    • (2003) Cell , vol.114 , pp. 201-214
    • Xu, J.1    Wang, F.2    Van Keymeulen, A.3    Herzmark, P.4    Straight, A.5
  • 54
    • 0029978202 scopus 로고    scopus 로고
    • The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase
    • Damen JE, Liu L, Rosten P, Humphries RK, Jefferson AB, et al. 1996. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Proc. Natl. Acad. Sci. USA 93:1689-93
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1689-1693
    • Damen, J.E.1    Liu, L.2    Rosten, P.3    Humphries, R.K.4    Jefferson, A.B.5
  • 55
    • 84859417595 scopus 로고    scopus 로고
    • Phosphoinositide lipid phosphatase SHIP1 and PTEN coordinate to regulate cell migration and adhesion
    • Mondal S, Subramanian KK, Sakai J, Bajrami B, Luo HR. 2012. Phosphoinositide lipid phosphatase SHIP1 and PTEN coordinate to regulate cell migration and adhesion. Mol. Biol. Cell 23:1219-30
    • (2012) Mol. Biol. Cell , vol.23 , pp. 1219-1230
    • Mondal, S.1    Subramanian, K.K.2    Sakai, J.3    Bajrami, B.4    Luo, H.R.5
  • 56
    • 45549093769 scopus 로고    scopus 로고
    • PTEN functions to prioritize" chemotactic cues and prevent "distraction" in migrating neutrophils
    • Heit B, Robbins SM, Downey CM, Guan Z, Colarusso P, et al. 2008. PTEN functions to "prioritize" chemotactic cues and prevent "distraction" in migrating neutrophils. Nat. Immunol. 9:743-52
    • (2008) Nat. Immunol , vol.9 , pp. 743-752
    • Heit, B.1    Robbins, S.M.2    Downey, C.M.3    Guan, Z.4    Colarusso, P.5
  • 57
    • 66549115702 scopus 로고    scopus 로고
    • Targeted deletion of tumor suppressor PTEN augments neutrophil function and enhances host defense in neutropenia-Associated pneumonia
    • Li Y, Jia Y, Pichavant M, Loison F, Sarraj B, et al. 2009. Targeted deletion of tumor suppressor PTEN augments neutrophil function and enhances host defense in neutropenia-Associated pneumonia. Blood 113:4930-41
    • (2009) Blood , vol.113 , pp. 4930-4941
    • Li, Y.1    Jia, Y.2    Pichavant, M.3    Loison, F.4    Sarraj, B.5
  • 58
    • 77956211255 scopus 로고    scopus 로고
    • Myeloid PTEN promotes inflammation but impairs bactericidal activities during murine pneumococcal pneumonia
    • Schabbauer G, Matt U, Günzl P, Warszawska J, Furtner T, et al. 2010. Myeloid PTEN promotes inflammation but impairs bactericidal activities during murine pneumococcal pneumonia. J. Immunol. 185:468-76
    • (2010) J. Immunol , vol.185 , pp. 468-476
    • Schabbauer, G.1    Matt, U.2    Günzl, P.3    Warszawska, J.4    Furtner, T.5
  • 59
    • 34247360789 scopus 로고    scopus 로고
    • Tumor suppressor PTEN is a physiologic suppressor of chemoattractant- mediated neutrophil functions
    • Subramanian KK, Jia Y, Zhu D, Simms BT, Jo H, et al. 2007. Tumor suppressor PTEN is a physiologic suppressor of chemoattractant-mediated neutrophil functions. Blood 109:4028-37
    • (2007) Blood , vol.109 , pp. 4028-4037
    • Subramanian, K.K.1    Jia, Y.2    Zhu, D.3    Simms, B.T.4    Jo, H.5
  • 60
    • 0037428084 scopus 로고    scopus 로고
    • Tube morphogenesis: Making and shaping biological tubes
    • Lubarsky B, KrasnowMA. 2003. Tube morphogenesis: making and shaping biological tubes. Cell 112:19-28
    • (2003) Cell , vol.112 , pp. 19-28
    • Lubarsky, B.1    Krasnow, M.A.2
  • 61
    • 33748199154 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,4,5-trisphosphate regulates the formation of the basolateral plasma membrane in epithelial cells
    • Gassama-Diagne A, Yu W, ter BeestM,Martin-Belmonte F, Kierbel A, et al. 2006. Phosphatidylinositol-3,4,5-trisphosphate regulates the formation of the basolateral plasma membrane in epithelial cells. Nat. Cell Biol. 8:963-70
    • (2006) Nat. Cell Biol , vol.8 , pp. 963-970
    • Gassama-Diagne, A.1    Yu, W.2    Ter Beest, M.3    Martin-Belmonte, F.4    Kierbel, A.5
  • 62
    • 33846270032 scopus 로고    scopus 로고
    • PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42
    • Martin-Belmonte F, Gassama A, Datta A, Yu W, Rescher U, et al. 2007. PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42. Cell 128:383-97
    • (2007) Cell , vol.128 , pp. 383-397
    • Martin-Belmonte, F.1    Gassama, A.2    Datta, A.3    Yu, W.4    Rescher, U.5
  • 63
    • 72849130207 scopus 로고    scopus 로고
    • The polycomb group protein Bmi-1 represses the tumor suppressor PTEN and induces epithelial-mesenchymal transition in human nasopharyngeal epithelial cells
    • Song LB, Li J, Liao WT, Feng Y, Yu CP, et al. 2009. The polycomb group protein Bmi-1 represses the tumor suppressor PTEN and induces epithelial-mesenchymal transition in human nasopharyngeal epithelial cells. J. Clin. Investig. 119:3626-36
    • (2009) J. Clin. Investig , vol.119 , pp. 3626-3636
    • Song, L.B.1    Li, J.2    Liao, W.T.3    Feng, Y.4    Yu, C.P.5
  • 64
    • 0032238299 scopus 로고    scopus 로고
    • The C elegans PTEN homolog, DAF-18, acts in the insulin receptor-like metabolic signaling pathway
    • Ogg S, Ruvkun G. 1998. The C. elegans PTEN homolog, DAF-18, acts in the insulin receptor-like metabolic signaling pathway. Mol. Cell 2:887-93
    • (1998) Mol. Cell , vol.2 , pp. 887-893
    • Ogg, S.1    Ruvkun, G.2
  • 65
    • 0027771804 scopus 로고
    • A C elegans mutant that lives twice as long as wild type
    • Kenyon C, Chang J, Gensch E, Rudner A, Tabtiang R. 1993. A C. elegans mutant that lives twice as long as wild type. Nature 366:461-64
    • (1993) Nature , vol.366 , pp. 461-464
    • Kenyon, C.1    Chang, J.2    Gensch, E.3    Rudner, A.4    Tabtiang, R.5
  • 66
    • 0033572644 scopus 로고    scopus 로고
    • Drosophila tumor suppressor PTEN controls cell size and number by antagonizing the Chico/PI3-kinase signaling pathway
    • Goberdhan DC, Paricio N, Goodman EC, Mlodzik M, Wilson C. 1999. Drosophila tumor suppressor PTEN controls cell size and number by antagonizing the Chico/PI3-kinase signaling pathway. Genes Dev. 13:3244-58
    • (1999) Genes Dev , vol.13 , pp. 3244-3258
    • Goberdhan, D.C.1    Paricio, N.2    Goodman, E.C.3    Mlodzik, M.4    Wilson, C.5
  • 67
    • 0034657764 scopus 로고    scopus 로고
    • Drosophila PTEN regulates cell growth and proliferation through PI3K-dependent and -independent pathways
    • Gao X, Neufeld TP, Pan D. 2000. Drosophila PTEN regulates cell growth and proliferation through PI3K-dependent and -independent pathways. Dev. Biol. 221:404-18
    • (2000) Dev. Biol , vol.221 , pp. 404-418
    • Gao, X.1    Neufeld, T.P.2    Pan, D.3
  • 68
    • 0034680008 scopus 로고    scopus 로고
    • The conserved PI3-K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila
    • Scanga SE, Ruel L, Binari RC, Snow B, Stambolic V, et al. 2000. The conserved PI3-K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila. Oncogene 19:3971-77
    • (2000) Oncogene , vol.19 , pp. 3971-3977
    • Scanga, S.E.1    Ruel, L.2    Binari, R.C.3    Snow, B.4    Stambolic, V.5
  • 70
    • 0037072780 scopus 로고    scopus 로고
    • The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes
    • Berwick DC, Hers I, Heesom KJ, Moule SK, Tavare JM. 2002. The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes. J. Biol. Chem. 277:33895-900
    • (2002) J. Biol. Chem , vol.277 , pp. 33895-33900
    • Berwick, D.C.1    Hers, I.2    Heesom, K.J.3    Moule, S.K.4    Tavare, J.M.5
  • 71
    • 0030734345 scopus 로고    scopus 로고
    • Physiological role of Akt in insulinstimulated translocation of GLUT4 in transfected rat adipose cells
    • Cong LN, Chen H, Li Y, Zhou L, McGibbon MA, et al. 1997. Physiological role of Akt in insulinstimulated translocation of GLUT4 in transfected rat adipose cells. Mol. Endocrinol. 11:1881-90
    • (1997) Mol. Endocrinol , vol.11 , pp. 1881-1890
    • Cong, L.N.1    Chen, H.2    Li, Y.3    Zhou, L.4    McGibbon, M.A.5
  • 72
    • 0029908016 scopus 로고    scopus 로고
    • Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation
    • Kohn AD, Summers SA, BirnbaumMJ, Roth RA. 1996. Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J. Biol. Chem. 271:31372-78
    • (1996) J. Biol. Chem , vol.271 , pp. 31372-31378
    • Kohn, A.D.1    Summers, S.A.2    Birnbaum, M.J.3    Roth, R.A.4
  • 74
    • 85047694402 scopus 로고    scopus 로고
    • Hepatocyte-specific Pten deficiency results in steatohepatitis and hepatocellular carcinomas
    • Horie Y, Suzuki A, Kataoka E, Sasaki T, Hamada K, et al. 2004. Hepatocyte-specific Pten deficiency results in steatohepatitis and hepatocellular carcinomas. J. Clin. Investig. 113:1774-83
    • (2004) J. Clin. Investig , vol.113 , pp. 1774-1783
    • Horie, Y.1    Suzuki, A.2    Kataoka, E.3    Sasaki, T.4    Hamada, K.5
  • 75
    • 10744222107 scopus 로고    scopus 로고
    • Liver-specific deletion of negative regulator Pten results in fatty liver and insulin hypersensitivity [corrected]
    • Stiles B,Wang Y, Stahl A, Bassilian S, Lee WP, et al. 2004. Liver-specific deletion of negative regulator Pten results in fatty liver and insulin hypersensitivity [corrected]. Proc. Natl. Acad. Sci. USA 101:2082-87
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2082-2087
    • Stiles, B.1    Wang, Y.2    Stahl, A.3    Bassilian, S.4    Lee, W.P.5
  • 76
    • 51849096491 scopus 로고    scopus 로고
    • The roles of PTEN in development, physiology and tumorigenesis in mouse models: A tissue-by-tissue survey
    • Knobbe CB, Lapin V, Suzuki A, Mak TW. 2008. The roles of PTEN in development, physiology and tumorigenesis in mouse models: a tissue-by-tissue survey. Oncogene 27:5398-415
    • (2008) Oncogene , vol.27 , pp. 5398-5415
    • Knobbe, C.B.1    Lapin, V.2    Suzuki, A.3    Mak, T.W.4
  • 77
    • 84859215796 scopus 로고    scopus 로고
    • Systemic elevation of PTEN induces a tumor-suppressive metabolic state
    • Garcia-Cao I, Song MS, Hobbs RM, Laurent G, Giorgi C, et al. 2012. Systemic elevation of PTEN induces a tumor-suppressive metabolic state. Cell 149:49-62
    • (2012) Cell , vol.149 , pp. 49-62
    • Garcia-Cao, I.1    Song, M.S.2    Hobbs, R.M.3    Laurent, G.4    Giorgi, C.5
  • 79
    • 52649107626 scopus 로고    scopus 로고
    • Cancer cell metabolism: Warburg and beyond
    • Hsu PP, Sabatini DM. 2008. Cancer cell metabolism: Warburg and beyond. Cell 134:703-07
    • (2008) Cell , vol.134 , pp. 703-707
    • Hsu, P.P.1    Sabatini, D.M.2
  • 80
    • 79251502952 scopus 로고    scopus 로고
    • ATP consumption promotes cancermetabolism
    • Israelsen WJ, VanderHeidenMG. 2010. ATP consumption promotes cancermetabolism. Cell 143:669-71
    • (2010) Cell , vol.143 , pp. 669-671
    • Israelsen, W.J.1    Vander Heiden, M.G.2
  • 81
    • 0001221508 scopus 로고
    • On respiratory impairment in cancer cells
    • Warburg O. 1956. On respiratory impairment in cancer cells. Science 124:269-70
    • (1956) Science , vol.124 , pp. 269-270
    • Warburg, O.1
  • 82
    • 0030748651 scopus 로고    scopus 로고
    • Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades
    • Deprez J, Vertommen D, Alessi DR, Hue L, Rider MH. 1997. Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades. J. Biol. Chem. 272:17269-75
    • (1997) J. Biol. Chem , vol.272 , pp. 17269-17275
    • Deprez, J.1    Vertommen, D.2    Alessi, D.R.3    Hue, L.4    Rider, M.H.5
  • 83
    • 0034983918 scopus 로고    scopus 로고
    • Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase
    • Gottlob K, Majewski N, Kennedy S, Kandel E, Robey RB, Hay N. 2001. Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase. Genes Dev. 15:1406-18
    • (2001) Genes Dev , vol.15 , pp. 1406-1418
    • Gottlob, K.1    Majewski, N.2    Kennedy, S.3    Kandel, E.4    Robey, R.B.5    Hay, N.6
  • 85
    • 78649364332 scopus 로고    scopus 로고
    • Hypoxia-inducible factors and the response to hypoxic stress
    • Majmundar AJ, Wong WJ, Simon MC. 2010. Hypoxia-inducible factors and the response to hypoxic stress. Mol. Cell 40:294-309
    • (2010) Mol. Cell , vol.40 , pp. 294-309
    • Majmundar, A.J.1    Wong, W.J.2    Simon, M.C.3
  • 86
    • 84859445000 scopus 로고    scopus 로고
    • Hypoxia-inducible factors: Mediators of cancer progression and targets for cancer therapy
    • Semenza GL. 2012. Hypoxia-inducible factors: mediators of cancer progression and targets for cancer therapy. Trends Pharmacol. Sci. 33:207-14
    • (2012) Trends Pharmacol. Sci , vol.33 , pp. 207-214
    • Semenza, G.L.1
  • 87
    • 77955483125 scopus 로고    scopus 로고
    • Activation of a metabolic gene regulatory network downstream of mTOR complex 1
    • Düvel K, Yecies JL, Menon S, Raman P, Lipovsky AI, et al. 2010. Activation of a metabolic gene regulatory network downstream of mTOR complex 1. Mol. Cell 39:171-83
    • (2010) Mol. Cell , vol.39 , pp. 171-183
    • Düvel, K.1    Yecies, J.L.2    Menon, S.3    Raman, P.4    Lipovsky, A.I.5
  • 88
    • 0037023755 scopus 로고    scopus 로고
    • Signaling networks that link cell proliferation and cell fate
    • Sears RC, Nevins JR. 2002. Signaling networks that link cell proliferation and cell fate. J. Biol. Chem. 277:11617-20
    • (2002) J. Biol. Chem , vol.277 , pp. 11617-11620
    • Sears, R.C.1    Nevins, J.R.2
  • 90
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase AKT pathway in human cancer
    • Vivanco I, Sawyers CL. 2002. The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nat. Rev. Cancer 2:489-501
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 91
    • 9244239811 scopus 로고    scopus 로고
    • G1 cell-cycle control and cancer
    • Massague J. 2004. G1 cell-cycle control and cancer. Nature 432:298-306
    • (2004) Nature , vol.432 , pp. 298-306
    • Massague, J.1
  • 93
    • 84855885803 scopus 로고    scopus 로고
    • Cell cycle regulation in hematopoietic stem cells
    • Pietras EM, Warr MR, Passegu? E. 2011. Cell cycle regulation in hematopoietic stem cells. J. Cell Biol. 195:709-20
    • (2011) J. Cell Biol , vol.195 , pp. 709-720
    • Pietras, E.M.1    Warr, M.R.2    Passegu, E.3
  • 94
    • 33646376411 scopus 로고    scopus 로고
    • Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells
    • Yilmaz OH, Valdez R, Theisen BK, GuoW, Ferguson DO, et al. 2006. Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells. Nature 441:475-82
    • (2006) Nature , vol.441 , pp. 475-482
    • Yilmaz, O.H.1    Valdez, R.2    Theisen, B.K.3    Guo, W.4    Ferguson, D.O.5
  • 95
    • 33646351002 scopus 로고    scopus 로고
    • PTEN maintains haematopoietic stem cells and acts in lineage choice and leukaemia prevention
    • Zhang J, Grindley JC, Yin T, Jayasinghe S, He XC, et al. 2006. PTEN maintains haematopoietic stem cells and acts in lineage choice and leukaemia prevention. Nature 441:518-22
    • (2006) Nature , vol.441 , pp. 518-522
    • Zhang, J.1    Grindley, J.C.2    Yin, T.3    Jayasinghe, S.4    He, X.C.5
  • 96
    • 84866064701 scopus 로고    scopus 로고
    • Temporal changes in PTEN and mTORC2 regulation of hematopoietic stem cell self-renewal and leukemia suppression
    • Magee JA, Ikenoue T, Nakada D, Lee JY, Guan KL, Morrison SJ. 2012. Temporal changes in PTEN and mTORC2 regulation of hematopoietic stem cell self-renewal and leukemia suppression. Cell Stem Cell 11:415-28
    • (2012) Cell Stem Cell , vol.11 , pp. 415-428
    • Magee, J.A.1    Ikenoue, T.2    Nakada, D.3    Lee, J.Y.4    Guan, K.L.5    Morrison, S.J.6
  • 97
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan D,Weinberg RA. 2011. Hallmarks of cancer: the next generation. Cell 144:646-74
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 101
    • 0036545993 scopus 로고    scopus 로고
    • Oxidative processes in the brain and non-neuronal tissues as biomarkers of Alzheimer's disease
    • Gibson GE, Huang HM. 2002. Oxidative processes in the brain and non-neuronal tissues as biomarkers of Alzheimer's disease. Front. Biosci. 7:D1007-15
    • (2002) Front. Biosci , vol.7
    • Gibson, G.E.1    Huang, H.M.2
  • 102
    • 0034467058 scopus 로고    scopus 로고
    • Activation of synovial fibroblasts in rheumatoid arthritis: Lack of expression of the tumour suppressor PTEN at sites of invasive growth and destruction
    • Pap T, Franz JK, Hummel KM, Jeisy E, Gay R, Gay S. 2000. Activation of synovial fibroblasts in rheumatoid arthritis: lack of expression of the tumour suppressor PTEN at sites of invasive growth and destruction. Arthritis Res. 2:59-64
    • (2000) Arthritis Res , vol.2 , pp. 59-64
    • Pap, T.1    Franz, J.K.2    Hummel, K.M.3    Jeisy, E.4    Gay, R.5    Gay, S.6
  • 103
    • 30344485686 scopus 로고    scopus 로고
    • Negative regulation of myofibroblast differentiation by PTEN (phosphatase and tensin homolog deleted on chromosome 10
    • White ES, Atrasz RG, Hu B, Phan SH, Stambolic V, et al. 2006. Negative regulation of myofibroblast differentiation by PTEN (phosphatase and tensin homolog deleted on chromosome 10). Am. J. Respir. Crit. Care Med. 173:112-21
    • (2006) Am. J. Respir. Crit. Care Med , vol.173 , pp. 112-121
    • White, E.S.1    Atrasz, R.G.2    Hu, B.3    Phan, S.H.4    Stambolic, V.5
  • 104
    • 84880737776 scopus 로고    scopus 로고
    • A secreted PTEN phosphatase that enters cells to alter signaling and survival
    • 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
    • (2013) Science , vol.341 , pp. 399-402
    • Hopkins, B.D.1    Fine, B.2    Steinbach, N.3    Dendy, M.4    Rapp, Z.5
  • 105
    • 0025895051 scopus 로고
    • Heterologous basic domain substitutions in the HIV-1 Tat protein reveal an arginine-rich motif required for transactivation
    • Subramanian T, Govindarajan R, Chinnadurai G. 1991. Heterologous basic domain substitutions in the HIV-1 Tat protein reveal an arginine-rich motif required for transactivation. EMBO J. 10:2311-18
    • (1991) EMBO J , vol.10 , pp. 2311-2318
    • Subramanian, T.1    Govindarajan, R.2    Chinnadurai, G.3
  • 106
    • 0036568378 scopus 로고    scopus 로고
    • Nuclear PTEN expression and clinicopathologic features in a population-based series of primary cutaneous melanoma
    • Whiteman DC, Zhou XP, Cummings MC, Pavey S, Hayward NK, Eng C. 2002. Nuclear PTEN expression and clinicopathologic features in a population-based series of primary cutaneous melanoma. Int. J. Cancer 99:63-67
    • (2002) Int. J. Cancer , vol.99 , pp. 63-67
    • Whiteman, D.C.1    Zhou, X.P.2    Cummings, M.C.3    Pavey, S.4    Hayward, N.K.5    Eng, C.6
  • 107
    • 0033843623 scopus 로고    scopus 로고
    • Differential nuclear and cytoplasmic expression of PTEN in normal thyroid tissue, and benign and malignant epithelial thyroid tumors
    • Gimm O, Perren A, Weng LP, Marsh DJ, Yeh JJ, et al. 2000. Differential nuclear and cytoplasmic expression of PTEN in normal thyroid tissue, and benign and malignant epithelial thyroid tumors. Am. J. Pathol. 156:1693-700
    • (2000) Am. J. Pathol , vol.156 , pp. 1693-1700
    • Gimm, O.1    Perren, A.2    Weng, L.P.3    Marsh, D.J.4    Yeh, J.J.5
  • 108
    • 0032857217 scopus 로고    scopus 로고
    • Immunohistochemical evidence of loss of PTEN expression in primary ductal adenocarcinomas of the breast
    • Perren A, Weng LP, Boag AH, Ziebold U, Thakore K, et al. 1999. Immunohistochemical evidence of loss of PTEN expression in primary ductal adenocarcinomas of the breast. Am. J. Pathol. 155:1253-60
    • (1999) Am. J. Pathol , vol.155 , pp. 1253-1260
    • Perren, A.1    Weng, L.P.2    Boag, A.H.3    Ziebold, U.4    Thakore, K.5
  • 109
    • 0037439684 scopus 로고    scopus 로고
    • Increased nuclear phosphatase and tensin homologue deleted on chromosome 10 is associated with G0-G1 in MCF-7 cells
    • Ginn-Pease ME, Eng C. 2003. Increased nuclear phosphatase and tensin homologue deleted on chromosome 10 is associated with G0-G1 in MCF-7 cells. Cancer Res. 63:282-86
    • (2003) Cancer Res , vol.63 , pp. 282-286
    • Ginn-Pease, M.E.1    Eng, C.2
  • 110
    • 43249083765 scopus 로고    scopus 로고
    • PTEN nuclear localization is regulated by oxidative stress and mediates p53-dependent tumor suppression
    • Chang CJ, Mulholland DJ, Valamehr B, Mosessian S, Sellers WR, Wu H. 2008. PTEN nuclear localization is regulated by oxidative stress and mediates p53-dependent tumor suppression. Mol. Cell. Biol. 28:3281-89
    • (2008) Mol. Cell. Biol , vol.28 , pp. 3281-3289
    • Chang, C.J.1    Mulholland, D.J.2    Valamehr, B.3    Mosessian, S.4    Sellers, W.R.5    Wu, H.6
  • 111
    • 78651482046 scopus 로고    scopus 로고
    • Nuclear PTEN regulates the APC-CDH1 tumor-suppressive complex in a phosphatase-independent manner
    • Song MS, Carracedo A, Salmena L, Song SJ, Egia A, et al. 2011. Nuclear PTEN regulates the APC-CDH1 tumor-suppressive complex in a phosphatase- independent manner. Cell 144:187-99
    • (2011) Cell , vol.144 , pp. 187-199
    • Song, M.S.1    Carracedo, A.2    Salmena, L.3    Song, S.J.4    Egia, A.5
  • 112
    • 76449096769 scopus 로고    scopus 로고
    • The anaphase-promoting complex/cyclosome (APC/C): Cell-cycle-dependent and -independent functions
    • Manchado E, Eguren M, MalumbresM. 2010. The anaphase-promoting complex/cyclosome (APC/C): cell-cycle-dependent and -independent functions. Biochem. Soc. Trans. 38:65-71
    • (2010) Biochem. Soc. Trans , vol.38 , pp. 65-71
    • Manchado, E.1    Eguren, M.2    Malumbres, M.3
  • 113
    • 73849129220 scopus 로고    scopus 로고
    • The emerging role of APC/CCdh1 in controlling differentiation, genomic stability and tumor suppression
    • Wäsch R, Robbins JA, Cross FR. 2010. The emerging role of APC/CCdh1 in controlling differentiation, genomic stability and tumor suppression. Oncogene 29:1-10
    • (2010) Oncogene , vol.29 , pp. 1-10
    • Wäsch, R.1    Robbins, J.A.2    Cross, F.R.3
  • 114
    • 33845999615 scopus 로고    scopus 로고
    • Essential role for nuclearPTENinmaintaining chromosomal integrity
    • ShenWH, Balajee AS,Wang J,WuH,Eng C, et al. 2007. Essential role for nuclearPTENinmaintaining chromosomal integrity. Cell 128:157-70
    • (2007) Cell , vol.128 , pp. 157-170
    • Shen, W.H.1    Balajee, A.S.2    Wang, J.3    Wu, H.4    Eng, C.5
  • 115
    • 68049097111 scopus 로고    scopus 로고
    • Cell cycle checkpoint defects contribute to genomic instability in PTEN deficient cells independent of DNA DSB repair
    • Gupta A, Yang Q, Pandita RK, Hunt CR, Xiang T, et al. 2009. Cell cycle checkpoint defects contribute to genomic instability in PTEN deficient cells independent of DNA DSB repair. Cell Cycle 8:2198-210
    • (2009) Cell Cycle , vol.8 , pp. 2198-2210
    • Gupta, A.1    Yang, Q.2    Pandita, R.K.3    Hunt, C.R.4    Xiang, T.5
  • 116
    • 84862815940 scopus 로고    scopus 로고
    • PTEN in DNA damage repair
    • Ming M, He YY. 2012. PTEN in DNA damage repair. Cancer Lett. 319:125-29
    • (2012) Cancer Lett , vol.319 , pp. 125-129
    • Ming, M.1    He, Y.Y.2
  • 118
    • 27444445782 scopus 로고    scopus 로고
    • Cooperative phosphorylation of the tumor suppressor phosphatase and tensin homologue (PTEN) by casein kinases and glycogen synthase kinase 3?
    • Al-Khouri AM, Ma Y, Togo SH, Williams S, Mustelin T. 2005. Cooperative phosphorylation of the tumor suppressor phosphatase and tensin homologue (PTEN) by casein kinases and glycogen synthase kinase 3?. J. Biol. Chem. 280:35195-202
    • (2005) J. Biol. Chem , vol.280 , pp. 35195-35202
    • Al-Khouri, A.M.1    Ma, Y.2    Togo, S.H.3    Williams, S.4    Mustelin, T.5
  • 120
    • 84881308659 scopus 로고    scopus 로고
    • PD-1 increases PTEN phosphatase activity while decreasing PTEN protein stability by inhibiting casein kinase 2
    • Patsoukis N, Li L, Sari D, Petkova V, Boussiotis VA. 2013. PD-1 increases PTEN phosphatase activity while decreasing PTEN protein stability by inhibiting casein kinase 2. Mol. Cell. Biol. 33:3091-98
    • (2013) Mol. Cell. Biol , vol.33 , pp. 3091-3098
    • Patsoukis, N.1    Li, L.2    Sari, D.3    Petkova, V.4    Boussiotis, V.A.5
  • 122
    • 0036644058 scopus 로고    scopus 로고
    • Negative feedback regulation of the tumor suppressor PTEN by phosphoinositide-induced serine phosphorylation
    • Birle D, Bottini N, Williams S, Huynh H, deBelle I, et al. 2002. Negative feedback regulation of the tumor suppressor PTEN by phosphoinositide-induced serine phosphorylation. J. Immunol. 169:286-91
    • (2002) J. Immunol , vol.169 , pp. 286-291
    • Birle, D.1    Bottini, N.2    Williams, S.3    Huynh, H.4    De Belle, I.5
  • 124
    • 14544282456 scopus 로고    scopus 로고
    • Cellular transformation by the MSP58 oncogene is inhibited by its physical interaction with the PTEN tumor suppressor
    • Okumura K, Zhao M, Depinho RA, Furnari FB, Cavenee WK. 2005. Cellular transformation by the MSP58 oncogene is inhibited by its physical interaction with the PTEN tumor suppressor. Proc. Natl. Acad. Sci. USA 102:2703-6
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2703-2706
    • Okumura, K.1    Zhao, M.2    Depinho, R.A.3    Furnari, F.B.4    Cavenee, W.K.5
  • 125
  • 126
    • 84880710673 scopus 로고    scopus 로고
    • Nuclear PTEN controls DNA repair and sensitivity to genotoxic stress
    • Bassi C, Ho J, Srikumar T, Dowling RJ, Gorrini C, et al. 2013. Nuclear PTEN controls DNA repair and sensitivity to genotoxic stress. Science 341:395-99
    • (2013) Science , vol.341 , pp. 395-399
    • Bassi, C.1    Ho, J.2    Srikumar, T.3    Dowling, R.J.4    Gorrini, C.5
  • 127
    • 33845991111 scopus 로고    scopus 로고
    • NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN
    • Wang X, Trotman LC, Koppie T, Alimonti A, Chen Z, et al. 2007. NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN. Cell 128:129-39
    • (2007) Cell , vol.128 , pp. 129-139
    • Wang, X.1    Trotman, L.C.2    Koppie, T.3    Alimonti, A.4    Chen, Z.5
  • 128
    • 63249130027 scopus 로고    scopus 로고
    • Rak functions as a tumor suppressor by regulating PTEN protein stability and function
    • Yim EK, Peng G, Dai H, Hu R, Li K, et al. 2009. Rak functions as a tumor suppressor by regulating PTEN protein stability and function. Cancer Cell 15:304-14
    • (2009) Cancer Cell , vol.15 , pp. 304-314
    • Yim, E.K.1    Peng, G.2    Dai, H.3    Hu, R.4    Li, K.5
  • 129
    • 45849087093 scopus 로고    scopus 로고
    • The ubiquitin ligase Nedd4-1 is dispensable for the regulation of PTEN stability and localization
    • Fouladkou F, Landry T, Kawabe H, Neeb A, Lu C, et al. 2008. The ubiquitin ligase Nedd4-1 is dispensable for the regulation of PTEN stability and localization. Proc. Natl. Acad. Sci. USA 105:8585-90
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8585-8590
    • Fouladkou, F.1    Landry, T.2    Kawabe, H.3    Neeb, A.4    Lu, C.5
  • 130
    • 78149295998 scopus 로고    scopus 로고
    • Oncogenic role of the E3 ubiquitin ligase NEDD4-1, a PTEN negative regulator, in non-small-cell lung carcinomas
    • Amodio N, Scrima M, Palaia L, Salman AN, Quintiero A, et al. 2010. Oncogenic role of the E3 ubiquitin ligase NEDD4-1, a PTEN negative regulator, in non-small-cell lung carcinomas. Am. J. Pathol. 177:2622-34
    • (2010) Am. J. Pathol , vol.177 , pp. 2622-2634
    • Amodio, N.1    Scrima, M.2    Palaia, L.3    Salman, A.N.4    Quintiero, A.5
  • 131
    • 33845977965 scopus 로고    scopus 로고
    • Ubiquitination regulates PTEN nuclear import and tumor suppression
    • Trotman LC, Wang X, Alimonti A, Chen Z, Teruya-Feldstein J, et al. 2007. Ubiquitination regulates PTEN nuclear import and tumor suppression. Cell 128:141-56
    • (2007) Cell , vol.128 , pp. 141-156
    • Trotman, L.C.1    Wang, X.2    Alimonti, A.3    Chen, Z.4    Teruya-Feldstein, J.5
  • 133
    • 70349495862 scopus 로고    scopus 로고
    • Adenovirus-mediated down-regulation of X-linked inhibitor of apoptosis protein inhibits colon cancer
    • Dai Y, Qiao L, Chan KW, YangM, Ye J, et al. 2009. Adenovirus-mediated down-regulation of X-linked inhibitor of apoptosis protein inhibits colon cancer. Mol. Cancer Ther. 8:2762-70
    • (2009) Mol. Cancer Ther , vol.8 , pp. 2762-2770
    • Dai, Y.1    Qiao, L.2    Chan, K.W.3    Yang, M.4    Ye, J.5
  • 134
    • 84863096004 scopus 로고    scopus 로고
    • Targeting X-linked inhibitor of apoptosis protein inhibits pancreatic cancer cell growth through p-Akt depletion
    • Jiang C, Yi XP, Shen H, Li YX. 2012. Targeting X-linked inhibitor of apoptosis protein inhibits pancreatic cancer cell growth through p-Akt depletion. World J. Gastroenterol. 18:2956-65
    • (2012) World J. Gastroenterol , vol.18 , pp. 2956-2965
    • Jiang, C.1    Yi, X.P.2    Shen, H.3    Li, Y.X.4
  • 135
    • 36749045012 scopus 로고    scopus 로고
    • XIAP is highly expressed in esophageal cancer and its downregulation by RNAi sensitizes esophageal carcinoma cell lines to chemotherapeutics
    • Zhang S,Ding F, Luo A, Chen A, Yu Z, et al. 2007. XIAP is highly expressed in esophageal cancer and its downregulation by RNAi sensitizes esophageal carcinoma cell lines to chemotherapeutics. Cancer Biol. Ther. 6:973-80
    • (2007) Cancer Biol. Ther , vol.6 , pp. 973-980
    • Zhang, S.1    Ding, F.2    Luo, A.3    Chen, A.4    Yu, Z.5
  • 136
    • 68949121012 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN ubiquitination, content, and compartmentalization
    • Van Themsche C, Leblanc V, Parent S, Asselin E. 2009. X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN ubiquitination, content, and compartmentalization. J. Biol. Chem. 284:20462-66
    • (2009) J. Biol. Chem , vol.284 , pp. 20462-20466
    • Van Themsche, C.1    Leblanc, V.2    Parent, S.3    Asselin, E.4
  • 137
    • 53649106156 scopus 로고    scopus 로고
    • The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network
    • Song MS, Salmena L, Carracedo A, Egia A, Lo-Coco F, et al. 2008. The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network. Nature 455:813-17
    • (2008) Nature , vol.455 , pp. 813-817
    • Song, M.S.1    Salmena, L.2    Carracedo, A.3    Egia, A.4    Lo-Coco, F.5
  • 138
    • 36048935750 scopus 로고    scopus 로고
    • Protein expression and cellular localization in two prognostic subgroups of diffuse large B-cell lymphoma: Higher expression of ZAP70 and PKC-?II in the non-germinal center group and poor survival in patients deficient in nuclear PTEN
    • Fridberg M, Servin A, Anagnostaki L, Linderoth J, Berglund M, et al. 2007. Protein expression and cellular localization in two prognostic subgroups of diffuse large B-cell lymphoma: higher expression of ZAP70 and PKC-?II in the non-germinal center group and poor survival in patients deficient in nuclear PTEN. Leuk. Lymphoma 48:2221-32
    • (2007) Leuk. Lymphoma , vol.48 , pp. 2221-2232
    • Fridberg, M.1    Servin, A.2    Anagnostaki, L.3    Linderoth, J.4    Berglund, M.5
  • 139
  • 140
    • 11144279346 scopus 로고    scopus 로고
    • The major target of the endogenously generated reactive oxygen species in response to insulin stimulation is phosphatase and tensin homolog and not phosphoinositide-3 kinase (PI-3 kinase) in the PI-3 kinase/Akt pathway
    • Seo JH, Ahn Y, Lee SR, Yeo CY, Hur KC. 2005. The major target of the endogenously generated reactive oxygen species in response to insulin stimulation is phosphatase and tensin homolog and not phosphoinositide-3 kinase (PI-3 kinase) in the PI-3 kinase/Akt pathway. Mol. Biol. Cell 16:348-57
    • (2005) Mol. Biol. Cell , vol.16 , pp. 348-357
    • Seo, J.H.1    Ahn, Y.2    Lee, S.R.3    Yeo, C.Y.4    Hur, K.C.5
  • 141
    • 9344259718 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
    • Kwon J, Lee SR, Yang KS, Ahn Y, Kim YJ, et al. 2004. Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proc. Natl. Acad. Sci. USA 101:16419-24
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16419-16424
    • Kwon, J.1    Lee, S.R.2    Yang, K.S.3    Ahn, Y.4    Kim, Y.J.5
  • 142
    • 67349147914 scopus 로고    scopus 로고
    • Prdx1 inhibits tumorigenesis via regulating PTEN/AKT activity
    • Cao J, Schulte J, Knight A, Leslie NR, Zagozdzon A, et al. 2009. Prdx1 inhibits tumorigenesis via regulating PTEN/AKT activity. EMBO J. 28:1505-17
    • (2009) EMBO J , vol.28 , pp. 1505-1517
    • Cao, J.1    Schulte, J.2    Knight, A.3    Leslie, N.R.4    Zagozdzon, A.5
  • 143
    • 73949097658 scopus 로고    scopus 로고
    • Oxidation of DJ-1-dependent cell transformation through direct binding of DJ-1 to PTEN
    • Kim YC, Kitaura H, Taira T, Iguchi-Ariga SM, Ariga H. 2009. Oxidation of DJ-1-dependent cell transformation through direct binding of DJ-1 to PTEN. Int. J. Oncol. 35:1331-41
    • (2009) Int. J. Oncol , vol.35 , pp. 1331-1341
    • Kim, Y.C.1    Kitaura, H.2    Taira, T.3    Iguchi-Ariga, S.M.4    Ariga, H.5
  • 145
    • 52049102233 scopus 로고    scopus 로고
    • PTEN acetylation modulates its interaction with PDZ domain
    • Ikenoue T, Inoki K, Zhao B, Guan KL. 2008. PTEN acetylation modulates its interaction with PDZ domain. Cancer Res. 68:6908-12
    • (2008) Cancer Res , vol.68 , pp. 6908-6912
    • Ikenoue, T.1    Inoki, K.2    Zhao, B.3    Guan, K.L.4
  • 146
    • 84865429543 scopus 로고    scopus 로고
    • SIRT1 promotes proliferation and inhibits apoptosis of human malignant glioma cell lines
    • Qu Y, Zhang J,Wu S, Li B, Liu S, Cheng J. 2012. SIRT1 promotes proliferation and inhibits apoptosis of human malignant glioma cell lines. Neurosci. Lett. 525:168-72
    • (2012) Neurosci. Lett , vol.525 , pp. 168-172
    • Qu, Y.1    Zhang Jwu, S.2    Li, B.3    Liu, S.4    Cheng, J.5
  • 147
    • 84863336040 scopus 로고    scopus 로고
    • SUMO1 modification of PTEN regulates tumorigenesis by controlling its association with the plasma membrane
    • Huang J, Yan J, Zhang J, Zhu S, Wang Y, et al. 2012. SUMO1 modification of PTEN regulates tumorigenesis by controlling its association with the plasma membrane. Nat. Commun. 3:911
    • (2012) Nat. Commun , vol.3 , pp. 911
    • Huang, J.1    Yan, J.2    Zhang, J.3    Zhu, S.4    Wang, Y.5
  • 149
    • 33644504867 scopus 로고    scopus 로고
    • PTEN tumor suppressor associates with NHERF proteins to attenuate PDGF receptor signaling
    • Takahashi Y, Morales FC, Kreimann EL, Georgescu MM. 2006. PTEN tumor suppressor associates with NHERF proteins to attenuate PDGF receptor signaling. EMBO J. 25:910-20
    • (2006) EMBO J , vol.25 , pp. 910-920
    • Takahashi, Y.1    Morales, F.C.2    Kreimann, E.L.3    Georgescu, M.M.4
  • 150
    • 84858003974 scopus 로고    scopus 로고
    • Pten, nherf1 and phlpp form a tumor suppressor network that is disabled in glioblastoma
    • Molina JR, AgarwalNK, Morales FC, Hayashi Y, AldapeKD, et al. 2012. PTEN, NHERF1 and PHLPP form a tumor suppressor network that is disabled in glioblastoma. Oncogene 31:1264-74
    • (2012) Oncogene , vol.31 , pp. 1264-1274
    • Molina, J.R.1    Agarwal, N.K.2    Morales, F.C.3    Aldapekd, H.Y.4
  • 151
    • 84872825786 scopus 로고    scopus 로고
    • Suppression of survival signalling pathways by the phosphatase PHLPP
    • O'Neill AK, Niederst MJ, Newton AC. 2013. Suppression of survival signalling pathways by the phosphatase PHLPP. FEBS J. 280:572-83
    • (2013) FEBS J , vol.280 , pp. 572-583
    • O'neill, A.K.1    Niederst, M.J.2    Newton, A.C.3
  • 152
    • 0034867746 scopus 로고    scopus 로고
    • Co-downregulation of cell adhesion proteins ?-and ?-catenins, p120CTN, E-cadherin, and CD44 in prostatic adenocarcinomas
    • Kallakury BV, Sheehan CE, Ross JS. 2001. Co-downregulation of cell adhesion proteins ?-and ?-catenins, p120CTN, E-cadherin, and CD44 in prostatic adenocarcinomas. Hum. Pathol. 32:849-55
    • (2001) Hum. Pathol , vol.32 , pp. 849-855
    • Kallakury, B.V.1    Sheehan, C.E.2    Ross, J.S.3
  • 153
    • 0030601350 scopus 로고    scopus 로고
    • Common principles in cell adhesion
    • Ruoslahti E, Obrink B. 1996. Common principles in cell adhesion. Exp. Cell Res. 227:1-11
    • (1996) Exp. Cell Res , vol.227 , pp. 1-11
    • Ruoslahti, E.1    Obrink, B.2
  • 154
    • 14044261474 scopus 로고    scopus 로고
    • Vinculin controls PTEN protein level by maintaining the interaction of the adherens junction protein ?-catenin with the scaffolding protein MAGI-2
    • Subauste MC, Nalbant P, Adamson ED, Hahn KM. 2005. Vinculin controls PTEN protein level by maintaining the interaction of the adherens junction protein ?-catenin with the scaffolding protein MAGI-2. J. Biol. Chem. 280:5676-81
    • (2005) J. Biol. Chem , vol.280 , pp. 5676-5681
    • Subauste, M.C.1    Nalbant, P.2    Adamson, E.D.3    Hahn, K.M.4
  • 155
    • 11244250646 scopus 로고    scopus 로고
    • Implication of the MAGI-1b/PTEN signalosome in stabilization of adherens junctions and suppression of invasiveness
    • Kotelevets L, van Hengel J, Bruyneel E, Mareel M, van Roy F, Chastre E. 2005. Implication of the MAGI-1b/PTEN signalosome in stabilization of adherens junctions and suppression of invasiveness. FASEB J. 19:115-17
    • (2005) FASEB J , vol.19 , pp. 115-117
    • Kotelevets, L.1    Van Hengel, J.2    Bruyneel, E.3    Mareel, M.4    Van Roy, F.5    Chastre, E.6
  • 156
    • 0035945352 scopus 로고    scopus 로고
    • The lipid phosphatase activity of PTEN is critical for stabilizing intercellular junctions and reverting invasiveness
    • Kotelevets L, van Hengel J, Bruyneel E, Mareel M, van Roy F, Chastre E. 2001. The lipid phosphatase activity of PTEN is critical for stabilizing intercellular junctions and reverting invasiveness. J. Cell Biol. 155:1129-35
    • (2001) J. Cell Biol , vol.155 , pp. 1129-1135
    • Kotelevets, L.1    Van Hengel, J.2    Bruyneel, E.3    Mareel, M.4    Van Roy, F.5    Chastre, E.6
  • 157
    • 0033958869 scopus 로고    scopus 로고
    • Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both inhibits and stimulates PDZ binding
    • Adey NB, Huang L, Ormonde PA, Baumgard ML, Pero R, et al. 2000. Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both inhibits and stimulates PDZ binding. Cancer Res. 60:35-37
    • (2000) Cancer Res , vol.60 , pp. 35-37
    • Adey, N.B.1    Huang, L.2    Ormonde, P.A.3    Baumgard, M.L.4    Pero, R.5
  • 158
    • 77953562076 scopus 로고    scopus 로고
    • Dlg1-PTEN interaction regulates myelin thickness to prevent damaging peripheral nerve overmyelination
    • Cotter L, Ozçlik M, Jacob C, Pereira JA, Locher V, et al. 2010. Dlg1-PTEN interaction regulates myelin thickness to prevent damaging peripheral nerve overmyelination. Science 328:1415-18
    • (2010) Science , vol.328 , pp. 1415-1418
    • Cotter, L.1    Ozçlik, M.2    Jacob, C.3    Pereira, J.A.4    Locher, V.5
  • 159
    • 80054912552 scopus 로고    scopus 로고
    • Deciphering tumor-suppressor signaling in flies: Genetic link between Scribble/ Dlg/Lgl and the Hippo pathways
    • EnomotoM, Igaki T. 2011. Deciphering tumor-suppressor signaling in flies: genetic link between Scribble/ Dlg/Lgl and the Hippo pathways. J. Genet. Genomics 38:461-70
    • (2011) J. Genet. Genomics , vol.38 , pp. 461-470
    • Enomoto, M.1    Igaki, T.2
  • 160
    • 0024344416 scopus 로고
    • Molecular cloning of the lethal(1)discs large-1 oncogene of Drosophila
    • Woods DF, Bryant PJ. 1989. Molecular cloning of the lethal(1)discs large-1 oncogene of Drosophila. Dev. Biol. 134:222-35
    • (1989) Dev. Biol , vol.134 , pp. 222-235
    • Woods, D.F.1    Bryant, P.J.2
  • 162
    • 23844473290 scopus 로고    scopus 로고
    • Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-Associated serine/threonine kinases
    • Valiente M, Andr?s-Pons A, Gomar B, Torres J, Gil A, et al. 2005. Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-Associated serine/threonine kinases. J. Biol. Chem. 280:28936-43
    • (2005) J. Biol. Chem , vol.280 , pp. 28936-28943
    • Valiente, M.1    Andrés-Pons, A.2    Gomar, B.3    Torres, J.4    Gil, A.5
  • 163
    • 84865189134 scopus 로고    scopus 로고
    • Interference with the PTEN-MAST2 interaction by a viral protein leads to cellular relocalization of PTEN
    • Terrien E, Chaffotte A, Lafage M, Khan Z, PrehaudC, et al. 2012. Interference with the PTEN-MAST2 interaction by a viral protein leads to cellular relocalization of PTEN. Sci. Signal. 5:ra58
    • (2012) Sci. Signal , vol.5
    • Terrien, E.1    Chaffotte, A.2    Lafage, M.3    Prehaudc, K.Z.4
  • 164
    • 77955293704 scopus 로고    scopus 로고
    • Regulation of PTEN in neurons by myosin-based transport mechanisms
    • Kreis P, van Diepen MT, Eickholt BJ. 2010. Regulation of PTEN in neurons by myosin-based transport mechanisms. Adv. Enzyme Regul. 50:119-24
    • (2010) Adv. Enzyme Regul , vol.50 , pp. 119-124
    • Kreis, P.1    Van Diepen, M.T.2    Eickholt, B.J.3
  • 167
    • 70349636049 scopus 로고    scopus 로고
    • A motor driving PTEN
    • Zhou J, Parada LF. 2009. A motor driving PTEN. Nat. Cell Biol. 11:1177-79
    • (2009) Nat. Cell Biol , vol.11 , pp. 1177-1179
    • Zhou, J.1    Parada, L.F.2
  • 169
    • 69949170092 scopus 로고    scopus 로고
    • Activation of the PI3K pathway in cancer through inhibition of PTEN by exchange factor P-REX2a
    • Fine B, Hodakoski C, Koujak S, Su T, Saal LH, et al. 2009. Activation of the PI3K pathway in cancer through inhibition of PTEN by exchange factor P-REX2a. Science 325:1261-65
    • (2009) Science , vol.325 , pp. 1261-1265
    • Fine, B.1    Hodakoski, C.2    Koujak, S.3    Su, T.4    Saal, L.H.5
  • 170
    • 79955816876 scopus 로고    scopus 로고
    • Mannosidase 2C1 attenuates PTEN function in prostate cancer cells
    • He L, Fan C, Kapoor A, Ingram AJ, Rybak AP, et al. 2011. Mannosidase 2C1 attenuates PTEN function in prostate cancer cells. Nat. Commun. 2:307
    • (2011) Nat. Commun , vol.2 , pp. 307
    • He, L.1    Fan, C.2    Kapoor, A.3    Ingram, A.J.4    Rybak, A.P.5
  • 171
    • 77953213657 scopus 로고    scopus 로고
    • Shank-interacting protein-like 1 promotes tumorigenesis via PTEN inhibition in human tumor cells
    • He L, Ingram A, Rybak AP, Tang D. 2010. Shank-interacting protein-like 1 promotes tumorigenesis via PTEN inhibition in human tumor cells. J. Clin. Investig. 120:2094-108
    • (2010) J. Clin. Investig , vol.120 , pp. 2094-2108
    • He, L.1    Ingram, A.2    Rybak, A.P.3    Tang, D.4
  • 172
    • 0035199914 scopus 로고    scopus 로고
    • The Egr-1 transcription factor directly activates PTEN during irradiation-induced signalling
    • Virolle T, Adamson ED, Baron V, Birle D, Mercola D, et al. 2001. The Egr-1 transcription factor directly activates PTEN during irradiation-induced signalling. Nat. Cell Biol. 3:1124-28
    • (2001) Nat. Cell Biol , vol.3 , pp. 1124-1128
    • Virolle, T.1    Adamson, E.D.2    Baron, V.3    Birle, D.4    Mercola, D.5
  • 173
    • 0041450058 scopus 로고    scopus 로고
    • PTEN tumor suppressor regulates p53 protein levels and activity through phosphatase-dependent and -independent mechanisms
    • Freeman DJ, Li AG, Wei G, Li HH, Kertesz N, et al. 2003. PTEN tumor suppressor regulates p53 protein levels and activity through phosphatase-dependent and -independent mechanisms. Cancer Cell 3:117-30
    • (2003) Cancer Cell , vol.3 , pp. 117-130
    • Freeman, D.J.1    Li, A.G.2    Wei, G.3    Li, H.H.4    Kertesz, N.5
  • 174
    • 33646368397 scopus 로고    scopus 로고
    • Up-regulation of PTEN (phosphatase and tensin homolog deleted on chromosome ten) mediates p38 MAPK stress signal-induced inhibition of insulin signaling A cross-talk between stress signaling and insulin signaling in resistin-treated human endothelial cells
    • Shen YH, Zhang L, Gan Y, Wang X, Wang J, et al. 2006. Up-regulation of PTEN (phosphatase and tensin homolog deleted on chromosome ten) mediates p38 MAPK stress signal-induced inhibition of insulin signaling. A cross-talk between stress signaling and insulin signaling in resistin-treated human endothelial cells. J. Biol. Chem. 281:7727-36
    • (2006) J. Biol. Chem , vol.281 , pp. 7727-7736
    • Shen, Y.H.1    Zhang, L.2    Gan, Y.3    Wang, X.4    Wang, J.5
  • 175
    • 0035873953 scopus 로고    scopus 로고
    • Tumor suppressor and antiinflammatory actions of PPARγagonists are mediated via upregulation of PTEN
    • Patel L, Pass I, Coxon P, Downes CP, Smith SA, Macphee CH. 2001. Tumor suppressor and antiinflammatory actions of PPARγagonists are mediated via upregulation of PTEN. Curr. Biol. 11:764-68
    • (2001) Curr. Biol , vol.11 , pp. 764-768
    • Patel, L.1    Pass, I.2    Coxon, P.3    Downes, C.P.4    Smith, S.A.5    Macphee, C.H.6
  • 176
    • 79953683693 scopus 로고    scopus 로고
    • Evi1 represses PTEN expression and activates PI3K/AKT/mTOR via interactions with polycomb proteins
    • Yoshimi A, Goyama S, Watanabe-Okochi N, Yoshiki Y, Nannya Y, et al. 2011. Evi1 represses PTEN expression and activates PI3K/AKT/mTOR via interactions with polycomb proteins. Blood 117:3617-28
    • (2011) Blood , vol.117 , pp. 3617-3628
    • Yoshimi, A.1    Goyama, S.2    Watanabe-Okochi, N.3    Yoshiki, Y.4    Nannya, Y.5
  • 177
    • 79251589918 scopus 로고    scopus 로고
    • Bmi-1 promotes invasion and metastasis, and its elevated expression is correlated with an advanced stage of breast cancer
    • Guo BH, Feng Y, Zhang R, Xu LH, Li MZ, et al. 2011. Bmi-1 promotes invasion and metastasis, and its elevated expression is correlated with an advanced stage of breast cancer. Mol. Cancer 10:10
    • (2011) Mol. Cancer , vol.10 , pp. 10
    • Guo, B.H.1    Feng, Y.2    Zhang, R.3    Xu, L.H.4    Li, M.Z.5
  • 179
    • 33846621883 scopus 로고    scopus 로고
    • CBF-1 (RBP-J?) binds to the PTEN promoter and regulates PTEN gene expression
    • Whelan JT, Forbes SL, Bertrand FE. 2007. CBF-1 (RBP-J?) binds to the PTEN promoter and regulates PTEN gene expression. Cell Cycle 6:80-84
    • (2007) Cell Cycle , vol.6 , pp. 80-84
    • Whelan, J.T.1    Forbes, S.L.2    Bertrand, F.E.3
  • 180
  • 182
    • 38349030742 scopus 로고    scopus 로고
    • New insights into PTEN
    • Tamguney T, Stokoe D. 2007. New insights into PTEN. J. Cell Sci. 120:4071-79
    • (2007) J. Cell Sci , vol.120 , pp. 4071-4079
    • Tamguney, T.1    Stokoe, D.2
  • 183
    • 77955644289 scopus 로고    scopus 로고
    • Mammalian microRNAs predominantly act to decrease target mRNA levels
    • Guo H, Ingolia NT, Weissman JS, Bartel DP. 2010. Mammalian microRNAs predominantly act to decrease target mRNA levels. Nature 466:835-40
    • (2010) Nature , vol.466 , pp. 835-840
    • Guo, H.1    Ingolia, N.T.2    Weissman, J.S.3    Bartel, D.P.4
  • 184
    • 84883310620 scopus 로고    scopus 로고
    • MicroRNA-17-92 plays a causative role in lymphomagenesis by coordinating multiple oncogenic pathways
    • Jin HY, Oda H, Lai M, Skalsky RL, Bethel K, et al. 2013. MicroRNA-17?92 plays a causative role in lymphomagenesis by coordinating multiple oncogenic pathways. EMBO J. 32:2377-91
    • (2013) EMBO J , vol.32 , pp. 2377-2391
    • Jin, H.Y.1    Oda, H.2    Lai, M.3    Skalsky, R.L.4    Bethel, K.5
  • 185
    • 78449293102 scopus 로고    scopus 로고
    • The miR-17-92 cluster of microRNAs confers tumorigenicity by inhibiting oncogene-induced senescence
    • Hong L, Lai M, Chen M, Xie C, Liao R, et al. 2010. The miR-17-92 cluster of microRNAs confers tumorigenicity by inhibiting oncogene-induced senescence. Cancer Res. 70:8547-57
    • (2010) Cancer Res , vol.70 , pp. 8547-8557
    • Hong, L.1    Lai, M.2    Chen, M.3    Xie, C.4    Liao, R.5
  • 186
  • 187
    • 84857079737 scopus 로고    scopus 로고
    • The microcosmos of cancer
    • Lujambio A, Lowe SW. 2012. The microcosmos of cancer. Nature 482:347-55
    • (2012) Nature , vol.482 , pp. 347-355
    • Lujambio, A.1    Lowe, S.W.2
  • 188
    • 84883478160 scopus 로고    scopus 로고
    • MiR-205 targets PTEN and PHLPP2 to augment AKT signaling and drive malignant phenotypes in non-small cell lung cancer
    • Cai J, Fang L, Huang Y, Li R, Yuan J, et al. 2013. miR-205 targets PTEN and PHLPP2 to augment AKT signaling and drive malignant phenotypes in non-small cell lung cancer. Cancer Res. 73:5402-15
    • (2013) Cancer Res , vol.73 , pp. 5402-5415
    • Cai, J.1    Fang, L.2    Huang, Y.3    Li, R.4    Yuan, J.5
  • 189
    • 84876177255 scopus 로고    scopus 로고
    • A pseudogene long-noncoding-RNA network regulates PTEN transcription and translation in human cells
    • Johnsson P, Ackley A, Vidarsdottir L, Lui WO, CorcoranM, et al. 2013. A pseudogene long-noncoding-RNA network regulates PTEN transcription and translation in human cells. Nat. Struct. Mol. Biol. 20:440-46
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 440-446
    • Johnsson, P.1    Ackley, A.2    Vidarsdottir, L.3    Lui, W.O.4    Corcoran, M.5
  • 190
    • 77953957633 scopus 로고    scopus 로고
    • A coding-independent function of gene and pseudogene mRNAs regulates tumour biology
    • Poliseno L, Salmena L, Zhang J, Carver B, Haveman WJ, Pandolfi PP. 2010. A coding-independent function of gene and pseudogene mRNAs regulates tumour biology. Nature 465:1033-38
    • (2010) Nature , vol.465 , pp. 1033-1038
    • Poliseno, L.1    Salmena, L.2    Zhang, J.3    Carver, B.4    Haveman, W.J.5    Pandolfi, P.P.6
  • 192
    • 84866543760 scopus 로고    scopus 로고
    • Pseudogenes: Newly discovered players in human cancer
    • Poliseno L. 2012. Pseudogenes: newly discovered players in human cancer. Sci. Signal. 5:re5
    • (2012) Sci. Signal , vol.5
    • Poliseno, L.1
  • 194
    • 4143138570 scopus 로고    scopus 로고
    • Promoter methylation of the PTEN gene is a common molecular change in breast cancer
    • Garc JM, Silva J, Pen∼a C, Garcia V, Rodr?́uez R, et al. 2004. Promoter methylation of the PTEN gene is a common molecular change in breast cancer. Genes Chromosomes Cancer 41:117-24
    • (2004) Genes Chromosomes Cancer , vol.41 , pp. 117-124
    • Garc, J.M.1    Silva, J.2    Pena, C.3    Garcia, V.4    Rodŕuez, R.5
  • 195
    • 58149503967 scopus 로고    scopus 로고
    • PTEN promotermethylation andLOHof 10q22-23 locus in PTEN expression of ovarian clear cell adenocarcinomas
    • Ho CM, Lin MC,Huang SH,Huang CJ, Lai HC, et al. 2009. PTEN promotermethylation andLOHof 10q22-23 locus in PTEN expression of ovarian clear cell adenocarcinomas. Gynecol. Oncol. 112:307-13
    • (2009) Gynecol. Oncol , vol.112 , pp. 307-313
    • Ho, C.M.1    Lin, M.C.2    Huang, S.H.3    Huang, C.J.4    Lai, H.C.5
  • 196
    • 84867505054 scopus 로고    scopus 로고
    • PTEN promoter methylation and activation of the PI3K/Akt/mTOR pathway in pediatric gliomas and influence on clinical outcome
    • Mueller S, Phillips J, Onar-Thomas A, Romero E, Zheng S, et al. 2012. PTEN promoter methylation and activation of the PI3K/Akt/mTOR pathway in pediatric gliomas and influence on clinical outcome. Neuro-Oncology 14:1146-52
    • (2012) Neuro-Oncology , vol.14 , pp. 1146-1152
    • Mueller, S.1    Phillips, J.2    Onar-Thomas, A.3    Romero, E.4    Zheng, S.5
  • 197
    • 85027932610 scopus 로고    scopus 로고
    • Association of sporadic breast cancer with PTEN/MMAC1/ TEP1 promoter hypermethylation
    • Sadeq V, Isar N, Manoochehr T. 2011. Association of sporadic breast cancer with PTEN/MMAC1/ TEP1 promoter hypermethylation. Med. Oncol. 28:420-23
    • (2011) Med. Oncol , vol.28 , pp. 420-423
    • Sadeq, V.1    Isar, N.2    Manoochehr, T.3
  • 198
    • 34247277178 scopus 로고    scopus 로고
    • Epigenetic and genetic alterations of PTEN in hepatocellular carcinoma
    • Wang L, Wang WL, Zhang Y, Guo SP, Zhang J, Li QL. 2007. Epigenetic and genetic alterations of PTEN in hepatocellular carcinoma. Hepatol. Res. 37:389-96
    • (2007) Hepatol. Res , vol.37 , pp. 389-396
    • Wang, L.1    Wang, W.L.2    Zhang, Y.3    Guo, S.P.4    Zhang, J.5    Li, Q.L.6
  • 199
    • 79953038262 scopus 로고    scopus 로고
    • PTEN loss in the continuum of common cancers, rare syndromes and mouse models
    • Hollander MC, Blumenthal GM, Dennis PA. 2011. PTEN loss in the continuum of common cancers, rare syndromes and mouse models. Nat. Rev. Cancer 11:289-301
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 289-301
    • Hollander, M.C.1    Blumenthal, G.M.2    Dennis, P.A.3
  • 200
    • 78650503110 scopus 로고    scopus 로고
    • Germline epigenetic regulation ofKILLIN inCowden and Cowdenlike syndrome
    • Bennett KL,Mester J,Eng C. 2010. Germline epigenetic regulation ofKILLIN inCowden and Cowdenlike syndrome. J. Am. Med. Assoc. 304:2724-31
    • (2010) J. Am. Med. Assoc , vol.304 , pp. 2724-2731
    • Bennett, K.L.1    Mester, J.2    Eng, C.3
  • 201
    • 44449130834 scopus 로고    scopus 로고
    • Killin is a p53-regulated nuclear inhibitor of DNA synthesis
    • Cho YJ, Liang P. 2008. Killin is a p53-regulated nuclear inhibitor of DNA synthesis. Proc. Natl. Acad. Sci. USA 105:5396-401
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5396-5401
    • Cho, Y.J.1    Liang, P.2
  • 203
    • 79958071323 scopus 로고    scopus 로고
    • Germline and somatic DNA methylation and epigenetic regulation of KILLIN in renal cell carcinoma
    • Bennett KL, Campbell R, Ganapathi S, Zhou M, Rini B, et al. 2011. Germline and somatic DNA methylation and epigenetic regulation of KILLIN in renal cell carcinoma. Genes Chromosomes Cancer 50:654-61
    • (2011) Genes Chromosomes Cancer , vol.50 , pp. 654-661
    • Bennett, K.L.1    Campbell, R.2    Ganapathi, S.3    Zhou, M.4    Rini, B.5
  • 204
    • 84868198811 scopus 로고    scopus 로고
    • PTENsignaling in autism spectrum disorders
    • Zhou J, Parada LF. 2012.PTENsignaling in autism spectrum disorders. Curr. Opin.Neurobiol. 22:873-79
    • (2012) Curr. Opin.Neurobiol , vol.22 , pp. 873-879
    • Zhou, J.1    Parada, L.F.2
  • 207
    • 79551542888 scopus 로고    scopus 로고
    • PTEN level in tumor suppression:How much is too little?
    • Carracedo A, Alimonti A, Pandolfi PP. 2011. PTEN level in tumor suppression:How much is too little? Cancer Res. 71:629-33
    • (2011) Cancer Res , vol.71 , pp. 629-633
    • Carracedo, A.1    Alimonti, A.2    Pandolfi, P.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.