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Volumn 8, Issue 5, 2013, Pages

Src-Mediated Phosphorylation of the Tyrosine Phosphatase PRL-3 Is Required for PRL-3 Promotion of Rho Activation, Motility and Invasion

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; PLATELET DERIVED GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PRL 3 PROTEIN; PROTEIN KINASE FYN; PROTEIN KINASE YES; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHO KINASE; RHOC GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; COLLAGEN; DRUG COMBINATION; IMMEDIATE EARLY PROTEIN; LAMININ; MATRIGEL; PROTEOGLYCAN; PTP4A3 PROTEIN, MOUSE; RAS PROTEIN; RHOC PROTEIN, MOUSE; SMALL INTERFERING RNA;

EID: 84877848617     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0064309     Document Type: Article
Times cited : (33)

References (58)
  • 1
    • 78649878760 scopus 로고    scopus 로고
    • PRL-3 phosphatase and cancer metastasis
    • Al-Aidaroos AQ, Zeng Q, (2010) PRL-3 phosphatase and cancer metastasis. J Cell Biochem 111: 1087-1098.
    • (2010) J Cell Biochem , vol.111 , pp. 1087-1098
    • Al-Aidaroos, A.Q.1    Zeng, Q.2
  • 2
    • 43049131055 scopus 로고    scopus 로고
    • PRL PTPs: mediators and markers of cancer progression
    • Bessette DC, Qiu D, Pallen CJ, (2008) PRL PTPs: mediators and markers of cancer progression. Cancer Metastasis Rev 27: 231-252.
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 231-252
    • Bessette, D.C.1    Qiu, D.2    Pallen, C.J.3
  • 3
    • 84872781756 scopus 로고    scopus 로고
    • Molecular mechanisms of the PRL phosphatases
    • Rios P, Li X, Kohn M, (2013) Molecular mechanisms of the PRL phosphatases. The FEBS journal 280: 505-524.
    • (2013) The FEBS Journal , vol.280 , pp. 505-524
    • Rios, P.1    Li, X.2    Kohn, M.3
  • 4
    • 33645516549 scopus 로고    scopus 로고
    • PRL tyrosine phosphatases regulate rho family GTPases to promote invasion and motility
    • Fiordalisi JJ, Keller PJ, Cox AD, (2006) PRL tyrosine phosphatases regulate rho family GTPases to promote invasion and motility. Cancer Res 66: 3153-3161.
    • (2006) Cancer Res , vol.66 , pp. 3153-3161
    • Fiordalisi, J.J.1    Keller, P.J.2    Cox, A.D.3
  • 5
    • 16844373567 scopus 로고    scopus 로고
    • Catalytic domain of PRL-3 plays an essential role in tumor metastasis: formation of PRL-3 tumors inside the blood vessels
    • Guo K, Li J, Tang JP, Koh V, Gan BQ, et al. (2004) Catalytic domain of PRL-3 plays an essential role in tumor metastasis: formation of PRL-3 tumors inside the blood vessels. Cancer Biol Ther 3: 945-951.
    • (2004) Cancer Biol Ther , vol.3 , pp. 945-951
    • Guo, K.1    Li, J.2    Tang, J.P.3    Koh, V.4    Gan, B.Q.5
  • 6
    • 0034801443 scopus 로고    scopus 로고
    • Role of PRL-3, a human muscle-specific tyrosine phosphatase, in angiotensin-II signaling
    • Matter WF, Estridge T, Zhang C, Belagaje R, Stancato L, et al. (2001) Role of PRL-3, a human muscle-specific tyrosine phosphatase, in angiotensin-II signaling. Biochem Biophys Res Commun 283: 1061-1068.
    • (2001) Biochem Biophys Res Commun , vol.283 , pp. 1061-1068
    • Matter, W.F.1    Estridge, T.2    Zhang, C.3    Belagaje, R.4    Stancato, L.5
  • 7
    • 80052245816 scopus 로고    scopus 로고
    • The metastasis-promoting phosphatase PRL-3 shows activity toward phosphoinositides
    • McParland V, Varsano G, Li X, Thornton J, Baby J, et al. (2011) The metastasis-promoting phosphatase PRL-3 shows activity toward phosphoinositides. Biochemistry 50: 7579-7590.
    • (2011) Biochemistry , vol.50 , pp. 7579-7590
    • McParland, V.1    Varsano, G.2    Li, X.3    Thornton, J.4    Baby, J.5
  • 8
    • 2442655501 scopus 로고    scopus 로고
    • Phosphatase of regenerating liver-3 promotes motility and metastasis of mouse melanoma cells
    • Wu X, Zeng H, Zhang X, Zhao Y, Sha H, et al. (2004) Phosphatase of regenerating liver-3 promotes motility and metastasis of mouse melanoma cells. Am J Pathol 164: 2039-2054.
    • (2004) Am J Pathol , vol.164 , pp. 2039-2054
    • Wu, X.1    Zeng, H.2    Zhang, X.3    Zhao, Y.4    Sha, H.5
  • 9
    • 42949121716 scopus 로고    scopus 로고
    • The metastasis-associated gene Prl-3 Is a p53 target involved in cell-cycle regulation
    • Basak S, Jacobs SB, Krieg AJ, Pathak N, Zeng Q, et al. (2008) The metastasis-associated gene Prl-3 Is a p53 target involved in cell-cycle regulation. Mol Cell 30: 303-314.
    • (2008) Mol Cell , vol.30 , pp. 303-314
    • Basak, S.1    Jacobs, S.B.2    Krieg, A.J.3    Pathak, N.4    Zeng, Q.5
  • 11
    • 80355136508 scopus 로고    scopus 로고
    • VEGF promotes the transcription of the human PRL-3 gene in HUVEC through transcription factor MEF2C
    • Xu J, Cao S, Wang L, Xu R, Chen G, et al. (2011) VEGF promotes the transcription of the human PRL-3 gene in HUVEC through transcription factor MEF2C. PloS one 6: e27165.
    • (2011) PloS One , vol.6
    • Xu, J.1    Cao, S.2    Wang, L.3    Xu, R.4    Chen, G.5
  • 12
    • 77954288770 scopus 로고    scopus 로고
    • PCBP1 suppresses the translation of metastasis-associated PRL-3 phosphatase
    • Wang H, Vardy LA, Tan CP, Loo JM, Guo K, et al. (2010) PCBP1 suppresses the translation of metastasis-associated PRL-3 phosphatase. Cancer cell 18: 52-62.
    • (2010) Cancer Cell , vol.18 , pp. 52-62
    • Wang, H.1    Vardy, L.A.2    Tan, C.P.3    Loo, J.M.4    Guo, K.5
  • 14
    • 0032484109 scopus 로고    scopus 로고
    • Low molecular weight protein-tyrosine phosphatase tyrosine phosphorylation by c-Src during platelet-derived growth factor-induced mitogenesis correlates with its subcellular targeting
    • Cirri P, Chiarugi P, Taddei L, Raugei G, Camici G, et al. (1998) Low molecular weight protein-tyrosine phosphatase tyrosine phosphorylation by c-Src during platelet-derived growth factor-induced mitogenesis correlates with its subcellular targeting. J Biol Chem 273: 32522-32527.
    • (1998) J Biol Chem , vol.273 , pp. 32522-32527
    • Cirri, P.1    Chiarugi, P.2    Taddei, L.3    Raugei, G.4    Camici, G.5
  • 15
    • 0031048053 scopus 로고    scopus 로고
    • Regulation of the low molecular weight phosphotyrosine phosphatase by phosphorylation at tyrosines 131 and 132
    • Tailor P, Gilman J, Williams S, Couture C, Mustelin T, (1997) Regulation of the low molecular weight phosphotyrosine phosphatase by phosphorylation at tyrosines 131 and 132. J Biol Chem 272: 5371-5374.
    • (1997) J Biol Chem , vol.272 , pp. 5371-5374
    • Tailor, P.1    Gilman, J.2    Williams, S.3    Couture, C.4    Mustelin, T.5
  • 16
    • 0038119084 scopus 로고    scopus 로고
    • The EphA8 receptor phosphorylates and activates low molecular weight phosphotyrosine protein phosphatase in vitro
    • Park S, (2003) The EphA8 receptor phosphorylates and activates low molecular weight phosphotyrosine protein phosphatase in vitro. J Biochem Mol Biol 36: 288-293.
    • (2003) J Biochem Mol Biol , vol.36 , pp. 288-293
    • Park, S.1
  • 17
    • 0032587198 scopus 로고    scopus 로고
    • The low Mr phosphotyrosine protein phosphatase behaves differently when phosphorylated at Tyr131 or Tyr132 by Src kinase
    • Bucciantini M, Chiarugi P, Cirri P, Taddei L, Stefani M, et al. (1999) The low Mr phosphotyrosine protein phosphatase behaves differently when phosphorylated at Tyr131 or Tyr132 by Src kinase. FEBS Lett 456: 73-78.
    • (1999) FEBS Lett , vol.456 , pp. 73-78
    • Bucciantini, M.1    Chiarugi, P.2    Cirri, P.3    Taddei, L.4    Stefani, M.5
  • 18
    • 33645473597 scopus 로고    scopus 로고
    • Negative regulation of a protein tyrosine phosphatase by tyrosine phosphorylation
    • Schwarzer D, Zhang Z, Zheng W, Cole PA, (2006) Negative regulation of a protein tyrosine phosphatase by tyrosine phosphorylation. J Am Chem Soc 128: 4192-4193.
    • (2006) J Am Chem Soc , vol.128 , pp. 4192-4193
    • Schwarzer, D.1    Zhang, Z.2    Zheng, W.3    Cole, P.A.4
  • 19
    • 0035346317 scopus 로고    scopus 로고
    • Phosphorylation and activation of protein tyrosine phosphatase (PTP) 1B by insulin receptor
    • Dadke S, Kusari A, Kusari J, (2001) Phosphorylation and activation of protein tyrosine phosphatase (PTP) 1B by insulin receptor. Mol Cell Biochem 221: 147-154.
    • (2001) Mol Cell Biochem , vol.221 , pp. 147-154
    • Dadke, S.1    Kusari, A.2    Kusari, J.3
  • 20
    • 0035800846 scopus 로고    scopus 로고
    • Insulin stimulates tyrosine phosphorylation and inactivation of protein-tyrosine phosphatase 1B in vivo
    • Tao J, Malbon CC, Wang HY, (2001) Insulin stimulates tyrosine phosphorylation and inactivation of protein-tyrosine phosphatase 1B in vivo. J Biol Chem 276: 29520-29525.
    • (2001) J Biol Chem , vol.276 , pp. 29520-29525
    • Tao, J.1    Malbon, C.C.2    Wang, H.Y.3
  • 21
    • 48249148368 scopus 로고    scopus 로고
    • Association of protein tyrosine phosphatases (PTPs)-1B with c-Met receptor and modulation of corneal epithelial wound healing
    • Kakazu A, Sharma G, Bazan HE, (2008) Association of protein tyrosine phosphatases (PTPs)-1B with c-Met receptor and modulation of corneal epithelial wound healing. Invest Ophthalmol Vis Sci 49: 2927-2935.
    • (2008) Invest Ophthalmol Vis Sci , vol.49 , pp. 2927-2935
    • Kakazu, A.1    Sharma, G.2    Bazan, H.E.3
  • 22
    • 0037737741 scopus 로고    scopus 로고
    • The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation
    • Zhang Z, Shen K, Lu W, Cole PA, (2003) The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation. J Biol Chem 278: 4668-4674.
    • (2003) J Biol Chem , vol.278 , pp. 4668-4674
    • Zhang, Z.1    Shen, K.2    Lu, W.3    Cole, P.A.4
  • 23
    • 0034758469 scopus 로고    scopus 로고
    • Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling
    • Lu W, Gong D, Bar-Sagi D, Cole PA, (2001) Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling. Mol Cell 8: 759-769.
    • (2001) Mol Cell , vol.8 , pp. 759-769
    • Lu, W.1    Gong, D.2    Bar-Sagi, D.3    Cole, P.A.4
  • 24
    • 56349103300 scopus 로고    scopus 로고
    • SHP-2 is a novel target of Abl kinases during cell proliferation
    • Mitra S, Beach C, Feng GS, Plattner R, (2008) SHP-2 is a novel target of Abl kinases during cell proliferation. J Cell Sci 121: 3335-3346.
    • (2008) J Cell Sci , vol.121 , pp. 3335-3346
    • Mitra, S.1    Beach, C.2    Feng, G.S.3    Plattner, R.4
  • 25
    • 0028359370 scopus 로고
    • PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth
    • Diamond RH, Cressman DE, Laz TM, Abrams CS, Taub R, (1994) PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth. Mol Cell Biol 14: 3752-3762.
    • (1994) Mol Cell Biol , vol.14 , pp. 3752-3762
    • Diamond, R.H.1    Cressman, D.E.2    Laz, T.M.3    Abrams, C.S.4    Taub, R.5
  • 26
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer RA, Sachsenmaier C, Cooper JA, Soriano P, (1999) Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J 18: 2459-2471.
    • (1999) EMBO J , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 27
    • 0036168355 scopus 로고    scopus 로고
    • Characterization of RhoC expression in benign and malignant breast disease: a potential new marker for small breast carcinomas with metastatic ability
    • Kleer CG, van Golen KL, Zhang Y, Wu ZF, Rubin MA, et al. (2002) Characterization of RhoC expression in benign and malignant breast disease: a potential new marker for small breast carcinomas with metastatic ability. Am J Pathol 160: 579-584.
    • (2002) Am J Pathol , vol.160 , pp. 579-584
    • Kleer, C.G.1    van Golen, K.L.2    Zhang, Y.3    Wu, Z.F.4    Rubin, M.A.5
  • 28
    • 69249156944 scopus 로고    scopus 로고
    • miR-200 regulates PDGF-D-mediated epithelial-mesenchymal transition, adhesion, and invasion of prostate cancer cells
    • Kong D, Li Y, Wang Z, Banerjee S, Ahmad A, et al. (2009) miR-200 regulates PDGF-D-mediated epithelial-mesenchymal transition, adhesion, and invasion of prostate cancer cells. Stem Cells 27: 1712-1721.
    • (2009) Stem Cells , vol.27 , pp. 1712-1721
    • Kong, D.1    Li, Y.2    Wang, Z.3    Banerjee, S.4    Ahmad, A.5
  • 30
    • 77953725367 scopus 로고    scopus 로고
    • Emerging roles of PDGF-D signaling pathway in tumor development and progression
    • Wang Z, Ahmad A, Li Y, Kong D, Azmi AS, et al. (2010) Emerging roles of PDGF-D signaling pathway in tumor development and progression. Biochim Biophys Acta 1806: 122-130.
    • (2010) Biochim Biophys Acta , vol.1806 , pp. 122-130
    • Wang, Z.1    Ahmad, A.2    Li, Y.3    Kong, D.4    Azmi, A.S.5
  • 31
    • 77956042544 scopus 로고    scopus 로고
    • SRC: A Century of Science Brought to the Clinic
    • Aleshin A, Finn RS, (2010) SRC: A Century of Science Brought to the Clinic. Neoplasia 12: 599-607.
    • (2010) Neoplasia , vol.12 , pp. 599-607
    • Aleshin, A.1    Finn, R.S.2
  • 32
    • 70349305426 scopus 로고    scopus 로고
    • Specific induction of migration and invasion of pancreatic carcinoma cells by RhoC, which differs from RhoA in its localisation and activity
    • Dietrich KA, Schwarz R, Liska M, Grass S, Menke A, et al. (2009) Specific induction of migration and invasion of pancreatic carcinoma cells by RhoC, which differs from RhoA in its localisation and activity. Biol Chem 390: 1063-1077.
    • (2009) Biol Chem , vol.390 , pp. 1063-1077
    • Dietrich, K.A.1    Schwarz, R.2    Liska, M.3    Grass, S.4    Menke, A.5
  • 33
    • 68549122708 scopus 로고    scopus 로고
    • Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion
    • Narumiya S, Tanji M, Ishizaki T, (2009) Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion. Cancer Metastasis Rev 28: 65-76.
    • (2009) Cancer Metastasis Rev , vol.28 , pp. 65-76
    • Narumiya, S.1    Tanji, M.2    Ishizaki, T.3
  • 35
    • 79953019177 scopus 로고    scopus 로고
    • PRL-3, an emerging marker of carcinogenesis, is strongly associated with poor prognosis
    • Guzinska-Ustymowicz K, Pryczynicz A, (2011) PRL-3, an emerging marker of carcinogenesis, is strongly associated with poor prognosis. Anti-cancer agents in medicinal chemistry 11: 99-108.
    • (2011) Anti-Cancer Agents in Medicinal Chemistry , vol.11 , pp. 99-108
    • Guzinska-Ustymowicz, K.1    Pryczynicz, A.2
  • 36
    • 0035834386 scopus 로고    scopus 로고
    • A phosphatase associated with metastasis of colorectal cancer
    • Saha S, Bardelli A, Buckhaults P, Velculescu VE, Rago C, et al. (2001) A phosphatase associated with metastasis of colorectal cancer. Science 294: 1343-1346.
    • (2001) Science , vol.294 , pp. 1343-1346
    • Saha, S.1    Bardelli, A.2    Buckhaults, P.3    Velculescu, V.E.4    Rago, C.5
  • 37
    • 82555175354 scopus 로고    scopus 로고
    • Correlation between Liver Metastases and the Level of PRL-3 mRNA Expression in Patients with Primary Colorectal Cancer
    • Kim NW, Chu CW, Ahn TS, Kim CJ, Jung DJ, et al. (2011) Correlation between Liver Metastases and the Level of PRL-3 mRNA Expression in Patients with Primary Colorectal Cancer. J Korean Soc Coloproctol 27: 231-236.
    • (2011) J Korean Soc Coloproctol , vol.27 , pp. 231-236
    • Kim, N.W.1    Chu, C.W.2    Ahn, T.S.3    Kim, C.J.4    Jung, D.J.5
  • 38
    • 84871818179 scopus 로고    scopus 로고
    • Upregulation of Protein Tyrosine Phosphatase Type IVA Member 3 (PTP4A3/PRL-3) is Associated with Tumor Differentiation and a Poor Prognosis in Human Hepatocellular Carcinoma
    • Mayinuer A, Yasen M, Mogushi K, Obulhasim G, Xieraili M, et al. (2013) Upregulation of Protein Tyrosine Phosphatase Type IVA Member 3 (PTP4A3/PRL-3) is Associated with Tumor Differentiation and a Poor Prognosis in Human Hepatocellular Carcinoma. Ann Surg Oncol 20: 305-317.
    • (2013) Ann Surg Oncol , vol.20 , pp. 305-317
    • Mayinuer, A.1    Yasen, M.2    Mogushi, K.3    Obulhasim, G.4    Xieraili, M.5
  • 39
    • 84872069314 scopus 로고    scopus 로고
    • The Expression of the Phosphatase Regenerating Liver 3 Gene is Associated with Outcome in Patients with Colorectal Cancer
    • Tamagawa H, Oshima T, Yoshihara K, Watanabe T, Numata M, et al. (2012) The Expression of the Phosphatase Regenerating Liver 3 Gene is Associated with Outcome in Patients with Colorectal Cancer. Hepatogastroenterology 59.
    • (2012) Hepatogastroenterology , vol.59
    • Tamagawa, H.1    Oshima, T.2    Yoshihara, K.3    Watanabe, T.4    Numata, M.5
  • 41
    • 84867073227 scopus 로고    scopus 로고
    • Downregulating PRL-3 inhibit migration and invasion of lung cancer cell via RhoA and mDia1
    • Jian M, Nan L, Guocheng J, Qingfu Z, Xueshan Q, et al. (2012) Downregulating PRL-3 inhibit migration and invasion of lung cancer cell via RhoA and mDia1. Tumori 98: 370-376.
    • (2012) Tumori , vol.98 , pp. 370-376
    • Jian, M.1    Nan, L.2    Guocheng, J.3    Qingfu, Z.4    Xueshan, Q.5
  • 42
    • 84869104386 scopus 로고    scopus 로고
    • The phosphatase of regenerating liver 3 (PRL-3) promotes cell migration through Arf-activity-dependent stimulation of integrin alpha5 recycling
    • Krndija D, Munzberg C, Maass U, Hafner M, Adler G, et al. (2012) The phosphatase of regenerating liver 3 (PRL-3) promotes cell migration through Arf-activity-dependent stimulation of integrin alpha5 recycling. J Cell Sci 125: 3883-3892.
    • (2012) J Cell Sci , vol.125 , pp. 3883-3892
    • Krndija, D.1    Munzberg, C.2    Maass, U.3    Hafner, M.4    Adler, G.5
  • 43
    • 34247119239 scopus 로고    scopus 로고
    • PRL3 promotes cell invasion and proliferation by down-regulation of Csk leading to Src activation
    • Liang F, Liang J, Wang WQ, Sun JP, Udho E, et al. (2007) PRL3 promotes cell invasion and proliferation by down-regulation of Csk leading to Src activation. J Biol Chem 282: 5413-5419.
    • (2007) J Biol Chem , vol.282 , pp. 5413-5419
    • Liang, F.1    Liang, J.2    Wang, W.Q.3    Sun, J.P.4    Udho, E.5
  • 44
    • 72549094086 scopus 로고    scopus 로고
    • PRL-3 promotes the motility, invasion, and metastasis of LoVo colon cancer cells through PRL-3-integrin beta1-ERK1/2 and-MMP2 signaling
    • Peng L, Xing X, Li W, Qu L, Meng L, et al. (2009) PRL-3 promotes the motility, invasion, and metastasis of LoVo colon cancer cells through PRL-3-integrin beta1-ERK1/2 and-MMP2 signaling. Mol Cancer 8: 110.
    • (2009) Mol Cancer , vol.8 , pp. 110
    • Peng, L.1    Xing, X.2    Li, W.3    Qu, L.4    Meng, L.5
  • 45
    • 0038615996 scopus 로고    scopus 로고
    • PRL-3 and PRL-1 promote cell migration, invasion, and metastasis
    • Zeng Q, Dong JM, Guo K, Li J, Tan HX, et al. (2003) PRL-3 and PRL-1 promote cell migration, invasion, and metastasis. Cancer Res 63: 2716-2722.
    • (2003) Cancer Res , vol.63 , pp. 2716-2722
    • Zeng, Q.1    Dong, J.M.2    Guo, K.3    Li, J.4    Tan, H.X.5
  • 46
    • 34250677652 scopus 로고    scopus 로고
    • PRL-3 siRNA inhibits the metastasis of B16-BL6 mouse melanoma cells in vitro and in vivo
    • Qian F, Li YP, Sheng X, Zhang ZC, Song R, et al. (2007) PRL-3 siRNA inhibits the metastasis of B16-BL6 mouse melanoma cells in vitro and in vivo. Mol Med 13: 151-159.
    • (2007) Mol Med , vol.13 , pp. 151-159
    • Qian, F.1    Li, Y.P.2    Sheng, X.3    Zhang, Z.C.4    Song, R.5
  • 47
    • 84875506390 scopus 로고    scopus 로고
    • Targeted Deletion of the Metastasis-Associated Phosphatase Ptp4a3 (PRL-3) Suppresses Murine Colon Cancer
    • Zimmerman MW, Homanics GE, Lazo JS, (2013) Targeted Deletion of the Metastasis-Associated Phosphatase Ptp4a3 (PRL-3) Suppresses Murine Colon Cancer. PloS one 8: e58300.
    • (2013) PloS One , vol.8
    • Zimmerman, M.W.1    Homanics, G.E.2    Lazo, J.S.3
  • 48
    • 1642482862 scopus 로고    scopus 로고
    • Structural insights into molecular function of the metastasis-associated phosphatase PRL-3
    • Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, et al. (2004) Structural insights into molecular function of the metastasis-associated phosphatase PRL-3. J Biol Chem 279: 11882-11889.
    • (2004) J Biol Chem , vol.279 , pp. 11882-11889
    • Kozlov, G.1    Cheng, J.2    Ziomek, E.3    Banville, D.4    Gehring, K.5
  • 49
    • 9644295701 scopus 로고    scopus 로고
    • Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms
    • Jeong DG, Kim SJ, Kim JH, Son JH, Park MR, et al. (2005) Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms. J Mol Biol 345: 401-413.
    • (2005) J Mol Biol , vol.345 , pp. 401-413
    • Jeong, D.G.1    Kim, S.J.2    Kim, J.H.3    Son, J.H.4    Park, M.R.5
  • 50
    • 24644519820 scopus 로고    scopus 로고
    • Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion
    • Sun JP, Wang WQ, Yang H, Liu S, Liang F, et al. (2005) Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion. Biochemistry 44: 12009-12021.
    • (2005) Biochemistry , vol.44 , pp. 12009-12021
    • Sun, J.P.1    Wang, W.Q.2    Yang, H.3    Liu, S.4    Liang, F.5
  • 51
    • 54249137797 scopus 로고    scopus 로고
    • Feedback loops shape cellular signals in space and time
    • Brandman O, Meyer T, (2008) Feedback loops shape cellular signals in space and time. Science 322: 390-395.
    • (2008) Science , vol.322 , pp. 390-395
    • Brandman, O.1    Meyer, T.2
  • 52
    • 62749096589 scopus 로고    scopus 로고
    • Mammalian target of rapamycin complex 1: signalling inputs, substrates and feedback mechanisms
    • Dunlop EA, Tee AR, (2009) Mammalian target of rapamycin complex 1: signalling inputs, substrates and feedback mechanisms. Cell Signal 21: 827-835.
    • (2009) Cell Signal , vol.21 , pp. 827-835
    • Dunlop, E.A.1    Tee, A.R.2
  • 53
    • 63149194964 scopus 로고    scopus 로고
    • (V600E)BRAF is associated with disabled feedback inhibition of RAF-MEK signaling and elevated transcriptional output of the pathway
    • Pratilas CA, Taylor BS, Ye Q, Viale A, Sander C, et al. (2009) (V600E)BRAF is associated with disabled feedback inhibition of RAF-MEK signaling and elevated transcriptional output of the pathway. Proc Natl Acad Sci U S A 106: 4519-4524.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 4519-4524
    • Pratilas, C.A.1    Taylor, B.S.2    Ye, Q.3    Viale, A.4    Sander, C.5
  • 54
    • 34248591612 scopus 로고    scopus 로고
    • Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer
    • Roberts PJ, Der CJ, (2007) Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer. Oncogene 26: 3291-3310.
    • (2007) Oncogene , vol.26 , pp. 3291-3310
    • Roberts, P.J.1    Der, C.J.2
  • 55
    • 33846675914 scopus 로고    scopus 로고
    • PRL-1 tyrosine phosphatase regulates c-Src levels, adherence, and invasion in human lung cancer cells
    • Achiwa H, Lazo JS, (2007) PRL-1 tyrosine phosphatase regulates c-Src levels, adherence, and invasion in human lung cancer cells. Cancer Res 67: 643-650.
    • (2007) Cancer Res , vol.67 , pp. 643-650
    • Achiwa, H.1    Lazo, J.S.2
  • 56
    • 0027469402 scopus 로고
    • Increase in activity and level of pp60c-src in progressive stages of human colorectal cancer
    • Talamonti MS, Roh MS, Curley SA, Gallick GE, (1993) Increase in activity and level of pp60c-src in progressive stages of human colorectal cancer. J Clin Invest 91: 53-60.
    • (1993) J Clin Invest , vol.91 , pp. 53-60
    • Talamonti, M.S.1    Roh, M.S.2    Curley, S.A.3    Gallick, G.E.4
  • 58
    • 84857916018 scopus 로고    scopus 로고
    • Targeting Src family kinases in anti-cancer therapies: turning promise into triumph
    • Zhang S, Yu D, (2012) Targeting Src family kinases in anti-cancer therapies: turning promise into triumph. Trends in pharmacological sciences 33: 122-128.
    • (2012) Trends in Pharmacological Sciences , vol.33 , pp. 122-128
    • Zhang, S.1    Yu, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.