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Volumn 34, Issue 15, 2014, Pages 2874-2889

PZR coordinates Shp2 Noonan and LEOPARD syndrome signaling in zebrafish and mice

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE SHP 2; PROTEIN ZERO RELATED PROTEIN; UNCLASSIFIED DRUG;

EID: 84904294127     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00135-14     Document Type: Article
Times cited : (29)

References (53)
  • 1
    • 84943235131 scopus 로고    scopus 로고
    • SH2 domain-containing protein tyrosine phosphatases
    • In Bradshaw RA, Dennis EA (ed), 2nd ed, Elsevier, San Diego, CA
    • Neel BG, Guo H, Pao L. 2009. SH2 domain-containing protein tyrosine phosphatases, p 707-728. In Bradshaw RA, Dennis EA (ed), Handbook in cell signaling, 2nd ed, vol 2. Elsevier, San Diego, CA.
    • (2009) Handbook in cell signaling , vol.2 , pp. 707-728
    • Neel, B.G.1    Guo, H.2    Pao, L.3
  • 2
    • 0032548830 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine phosphatase SHP-2
    • Hof P, Pluskey S, Dhe-Pagganon S, Eck MJ, Shoelson SE. 1998. Crystal structure of the tyrosine phosphatase SHP-2. Cell 92:441-450. http://dx .doi.org/10.1016/S0092-8674(00)80938-1.
    • (1998) Cell , vol.92 , pp. 441-450
    • Hof, P.1    Pluskey, S.2    Dhe-Pagganon, S.3    Eck, M.J.4    Shoelson, S.E.5
  • 4
    • 33846945811 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase function: the substrate perspective
    • Tiganis T, Bennett AM. 2007. Protein tyrosine phosphatase function: the substrate perspective. Biochem. J. 402:1-15. http://dx.doi.org/10.1042/BJ20061548.
    • (2007) Biochem. J. , vol.402 , pp. 1-15
    • Tiganis, T.1    Bennett, A.M.2
  • 5
    • 0030921502 scopus 로고    scopus 로고
    • Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2
    • Saxton TM, Henkemeyer M, Gasca S, Shen R, Rossi DJ, Shalaby F, Feng GS, Pawson T. 1997. Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2. EMBO J. 16:2352-2364. http://dx.doi.org/10.1093/emboj/16.9.2352.
    • (1997) EMBO J. , vol.16 , pp. 2352-2364
    • Saxton, T.M.1    Henkemeyer, M.2    Gasca, S.3    Shen, R.4    Rossi, D.J.5    Shalaby, F.6    Feng, G.S.7    Pawson, T.8
  • 6
    • 33644547703 scopus 로고    scopus 로고
    • A Shp2/SFK/Ras/Erk signaling pathway controls trophoblast stem cell survival
    • Yang W, Klaman LD, Chen B, Araki T, Harada H, Thomas SM, George EL, Neel BG. 2006. A Shp2/SFK/Ras/Erk signaling pathway controls trophoblast stem cell survival. Dev. Cell 10:317-327. http://dx.doi.org/10 .1016/j.devcel.2006.01.002.
    • (2006) Dev. Cell , vol.10 , pp. 317-327
    • Yang, W.1    Klaman, L.D.2    Chen, B.3    Araki, T.4    Harada, H.5    Thomas, S.M.6    George, E.L.7    Neel, B.G.8
  • 7
    • 0026630991 scopus 로고
    • corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso
    • Perkins LA, Larsen I, Perrimon N. 1992. corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso. Cell 70:225-236. http://dx .doi.org/10.1016/0092-8674(92)90098-W.
    • (1992) Cell , vol.70 , pp. 225-236
    • Perkins, L.A.1    Larsen, I.2    Perrimon, N.3
  • 8
    • 0038771965 scopus 로고    scopus 로고
    • The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
    • Neel BG, Gu H, Pao L. 2003. The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends Biochem. Sci. 28:284-293. http://dx.doi.org/10.1016/S0968-0004(03)00091-4.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 284-293
    • Neel, B.G.1    Gu, H.2    Pao, L.3
  • 10
    • 18444401014 scopus 로고    scopus 로고
    • Noonan syndrome and related disorders: genetics and pathogenesis
    • Tartaglia M, Gelb BD. 2005. Noonan syndrome and related disorders: genetics and pathogenesis. Annu. Rev. Genomics Hum. Genet. 6:45-68. http://dx.doi.org/10.1146/annurev.genom.6.080604.162305.
    • (2005) Annu. Rev. Genomics Hum. Genet. , vol.6 , pp. 45-68
    • Tartaglia, M.1    Gelb, B.D.2
  • 11
    • 37749041167 scopus 로고    scopus 로고
    • Shp2 knockdown and Noonan/LEOPARD mutant Shp2-induced gastrulation defects
    • Jopling C, van Geemen D, den Hertog J. 2007. Shp2 knockdown and Noonan/LEOPARD mutant Shp2-induced gastrulation defects. PLoS Genet. 3:e225. http://dx.doi.org/10.1371/journal.pgen.0030225.
    • (2007) PLoS Genet. , vol.3
    • Jopling, C.1    van Geemen, D.2    den Hertog, J.3
  • 13
    • 58149395502 scopus 로고    scopus 로고
    • Noonan, Costello and cardio-faciocutaneous syndromes: dysregulation of the Ras-MAPK pathway
    • Tidyman WE, Rauen KA. 2008. Noonan, Costello and cardio-faciocutaneous syndromes: dysregulation of the Ras-MAPK pathway. Expert Rev. Mol. Med. 10:e37. http://dx.doi.org/10.1017/S1462399408000902.
    • (2008) Expert Rev. Mol. Med. , vol.10
    • Tidyman, W.E.1    Rauen, K.A.2
  • 14
    • 79952225388 scopus 로고    scopus 로고
    • RAS signaling pathway mutations and hypertrophic cardiomyopathy: getting into and out of the thick of it
    • Gelb BD, Tartaglia M. 2011. RAS signaling pathway mutations and hypertrophic cardiomyopathy: getting into and out of the thick of it. J. Clin. Invest. 121:844-847. http://dx.doi.org/10.1172/JCI46399.
    • (2011) J. Clin. Invest. , vol.121 , pp. 844-847
    • Gelb, B.D.1    Tartaglia, M.2
  • 15
    • 33646096207 scopus 로고    scopus 로고
    • PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects
    • Kontaridis MI, Swanson KD, David FS, Barford D, Neel BG. 2006. PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects. J. Biol. Chem. 281:6785-6792. http://dx.doi .org/10.1074/jbc.M513068200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6785-6792
    • Kontaridis, M.I.1    Swanson, K.D.2    David, F.S.3    Barford, D.4    Neel, B.G.5
  • 17
    • 33646117025 scopus 로고    scopus 로고
    • Reduced phosphatase activity of SHP-2 in LEOPARD syndrome: consequences for PI3K binding on Gab1
    • Hanna N, Montagner A, Lee WH, Miteva M, Vidal M, Vidaud M, Parfait B, Raynal P. 2006. Reduced phosphatase activity of SHP-2 in LEOPARD syndrome: consequences for PI3K binding on Gab1. FEBS Lett. 580:2477-2482. http://dx.doi.org/10.1016/j.febslet.2006.03.088.
    • (2006) FEBS Lett. , vol.580 , pp. 2477-2482
    • Hanna, N.1    Montagner, A.2    Lee, W.H.3    Miteva, M.4    Vidal, M.5    Vidaud, M.6    Parfait, B.7    Raynal, P.8
  • 18
    • 33749003166 scopus 로고    scopus 로고
    • Noonan syndrome and related disorders: dysregulated RAS-mitogen activated protein kinase signal transduction
    • Gelb BD, Tartaglia M. 2006. Noonan syndrome and related disorders: dysregulated RAS-mitogen activated protein kinase signal transduction. Hum. Mol. Genet. 15(Suppl 2):R220-R226. http://dx.doi.org/10.1093/hmg/ddl197.
    • (2006) Hum. Mol. Genet. , vol.15 , Issue.SUPPL. 2
    • Gelb, B.D.1    Tartaglia, M.2
  • 19
  • 21
    • 0034052841 scopus 로고    scopus 로고
    • Dissecting the interaction of SHP-2 with PZR, an immunoglobulin family protein containing immunoreceptor tyrosinebased inhibitory motifs
    • Zhao R, Zhao ZJ. 2000. Dissecting the interaction of SHP-2 with PZR, an immunoglobulin family protein containing immunoreceptor tyrosinebased inhibitory motifs. J. Biol. Chem. 275:5453-5459. http://dx.doi.org/10.1074/jbc.275.8.5453.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5453-5459
    • Zhao, R.1    Zhao, Z.J.2
  • 22
    • 0037453249 scopus 로고    scopus 로고
    • Identification of a variant form of PZR lacking immunoreceptor tyrosine-based inhibitory motifs
    • Zhao R, Zhao ZJ. 2003. Identification of a variant form of PZR lacking immunoreceptor tyrosine-based inhibitory motifs. Biochem. Biophys. Res. Commun. 303:1028 -1033. http://dx.doi.org/10.1016/S0006-291X(03)00484-4.
    • (2003) Biochem. Biophys. Res. Commun. , vol.303
    • Zhao, R.1    Zhao, Z.J.2
  • 23
    • 15444348895 scopus 로고    scopus 로고
    • Purification and cloning of PZR, a binding protein and putative physiological substrate of tyrosine phosphatase SHP-2
    • Zhao ZJ, Zhao R. 1998. Purification and cloning of PZR, a binding protein and putative physiological substrate of tyrosine phosphatase SHP-2. J. Biol. Chem. 273:29367-29372. http://dx.doi.org/10.1074/jbc .273.45.29367.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29367-29372
    • Zhao, Z.J.1    Zhao, R.2
  • 24
    • 35648959797 scopus 로고    scopus 로고
    • The murine ortholog of the SHP-2 binding molecule, PZR accelerates cell migration on fibronectin and is expressed in early embryo formation
    • Roubelakis MG, Martin-Rendon E, Tsaknakis G, Stavropoulos A, Watt SM. 2007. The murine ortholog of the SHP-2 binding molecule, PZR accelerates cell migration on fibronectin and is expressed in early embryo formation. J. Cell. Biochem. 102:955-969. http://dx.doi.org/10.1002/jcb .21334.
    • (2007) J. Cell. Biochem. , vol.102 , pp. 955-969
    • Roubelakis, M.G.1    Martin-Rendon, E.2    Tsaknakis, G.3    Stavropoulos, A.4    Watt, S.M.5
  • 25
    • 47249118481 scopus 로고    scopus 로고
    • Noonan syndrome-associated SHP-2/ PTPN11 mutants enhance SIRPalpha and PZR tyrosyl phosphorylation and promote adhesion-mediated Erk activation
    • Eminaga S, Bennett AM. 2008. Noonan syndrome-associated SHP-2/ PTPN11 mutants enhance SIRPalpha and PZR tyrosyl phosphorylation and promote adhesion-mediated Erk activation. J. Biol. Chem. 283: 15328-15338. http://dx.doi.org/10.1074/jbc.M801382200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15328-15338
    • Eminaga, S.1    Bennett, A.M.2
  • 27
    • 0037561996 scopus 로고    scopus 로고
    • Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase alpha dimers
    • van der Wijk T, Blanchetot C, Overvoorde J, den Hertog J. 2003. Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase alpha dimers. J. Biol. Chem. 278:13968-13974. http://dx.doi.org/10.1074/jbc.M300632200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13968-13974
    • van der Wijk, T.1    Blanchetot, C.2    Overvoorde, J.3    den Hertog, J.4
  • 29
    • 33749577870 scopus 로고    scopus 로고
    • SHP-2 activates signaling of the nuclear factor of activated T cells to promote skeletal muscle growth
    • Fornaro M, Burch PM, Yang W, Zhang L, Hamilton CE, Kim JH, Neel BG, Bennett AM. 2006. SHP-2 activates signaling of the nuclear factor of activated T cells to promote skeletal muscle growth. J. Cell Biol. 175:87-97. http://dx.doi.org/10.1083/jcb.200602029.
    • (2006) J. Cell Biol. , vol.175 , pp. 87-97
    • Fornaro, M.1    Burch, P.M.2    Yang, W.3    Zhang, L.4    Hamilton, C.E.5    Kim, J.H.6    Neel, B.G.7    Bennett, A.M.8
  • 32
    • 0027453569 scopus 로고
    • Structure of the zebrafish snail1 gene and its expression in wild-type, spadetail and no tail mutant embryos
    • Thisse C, Thisse B, Schilling TF, Postlethwait JH. 1993. Structure of the zebrafish snail1 gene and its expression in wild-type, spadetail and no tail mutant embryos. Development 119:1203-1215.
    • (1993) Development , vol.119 , pp. 1203-1215
    • Thisse, C.1    Thisse, B.2    Schilling, T.F.3    Postlethwait, J.H.4
  • 33
    • 77951205715 scopus 로고    scopus 로고
    • RPTPalpha and PTPepsilon signaling via Fyn/Yes and RhoA is essential for zebrafish convergence and extension cell movements during gastrulation
    • van Eekelen M, Runtuwene V, Overvoorde J, den Hertog J. 2010. RPTPalpha and PTPepsilon signaling via Fyn/Yes and RhoA is essential for zebrafish convergence and extension cell movements during gastrulation. Dev. Biol. 340:626-639. http://dx.doi.org/10.1016/j.ydbio.2010.02.026.
    • (2010) Dev. Biol. , vol.340 , pp. 626-639
    • van Eekelen, M.1    Runtuwene, V.2    Overvoorde, J.3    den Hertog, J.4
  • 37
    • 84861161220 scopus 로고    scopus 로고
    • PTMScan direct: identification and quantification of peptides from critical signaling proteins by immunoaffinity enrichment coupled with LC-MS/MS
    • Stokes MP, Farnsworth CL, Moritz A, Silva JC, Jia X, Lee KA, Guo A, Polakiewicz RD, Comb MJ. 2012. PTMScan direct: identification and quantification of peptides from critical signaling proteins by immunoaffinity enrichment coupled with LC-MS/MS. Mol. Cell. Proteomics 11: 187-201. http://dx.doi.org/10.1074/mcp.M111.015883.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 187-201
    • Stokes, M.P.1    Farnsworth, C.L.2    Moritz, A.3    Silva, J.C.4    Jia, X.5    Lee, K.A.6    Guo, A.7    Polakiewicz, R.D.8    Comb, M.J.9
  • 38
    • 33749853607 scopus 로고    scopus 로고
    • A probabilitybased approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP. 2006. A probabilitybased approach for high-throughput protein phosphorylation analysis and site localization. Nat. Biotechnol. 24:1285-1292. http://dx.doi.org/10 .1038/nbt1240.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 39
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias JE, Gygi SP. 2007. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4:207-214. http://dx.doi.org/10.1038/nmeth1019.
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 41
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates JR, III, Eng JK, McCormack AL, Schieltz D. 1995. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem. 67:1426-1436. http://dx.doi .org/10.1021/ac00104a020.
    • (1995) Anal. Chem. , vol.67 , pp. 1426-1436
    • Yates III, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 42
    • 20044370091 scopus 로고    scopus 로고
    • Fyn/Yes and non-canonical Wnt signalling converge on RhoA in vertebrate gastrulation cell movements
    • Jopling C, den Hertog J. 2005. Fyn/Yes and non-canonical Wnt signalling converge on RhoA in vertebrate gastrulation cell movements. EMBO Rep. 6:426-431. http://dx.doi.org/10.1038/sj.embor.7400386.
    • (2005) EMBO Rep. , vol.6 , pp. 426-431
    • Jopling, C.1    den Hertog, J.2
  • 45
    • 0037040904 scopus 로고    scopus 로고
    • Cell surface glycoprotein PZR is a major mediator of concanavalin A-induced cell signaling
    • Zhao R, Guerrah A, Tang H, Zhao ZJ. 2002. Cell surface glycoprotein PZR is a major mediator of concanavalin A-induced cell signaling. J. Biol. Chem. 277:7882-7888. http://dx.doi.org/10.1074/jbc.M111914200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7882-7888
    • Zhao, R.1    Guerrah, A.2    Tang, H.3    Zhao, Z.J.4
  • 47
    • 45949088286 scopus 로고    scopus 로고
    • Phosphorylation and localization of protein-zero related (PZR) in cultured endothelial cells
    • Kusano K, Thomas TN, Fujiwara K. 2008. Phosphorylation and localization of protein-zero related (PZR) in cultured endothelial cells. Endothelium 15:127-136. http://dx.doi.org/10.1080/10623320802125250.
    • (2008) Endothelium , vol.15 , pp. 127-136
    • Kusano, K.1    Thomas, T.N.2    Fujiwara, K.3
  • 50
    • 33847046390 scopus 로고    scopus 로고
    • Structural and functional effects of disease-causing amino acid substitutions affecting residues Ala72 and Glu76 of the protein tyrosine phosphatase SHP-2
    • Bocchinfuso G, Stella L, Martinelli S, Flex E, Carta C, Pantaleoni F, Pispisa B, Venanzi M, Tartaglia M, Palleschi A. 2007. Structural and functional effects of disease-causing amino acid substitutions affecting residues Ala72 and Glu76 of the protein tyrosine phosphatase SHP-2. Proteins 66:963-974. http://dx.doi.org/10.1002/prot.21050.
    • (2007) Proteins , vol.66 , pp. 963-974
    • Bocchinfuso, G.1    Stella, L.2    Martinelli, S.3    Flex, E.4    Carta, C.5    Pantaleoni, F.6    Pispisa, B.7    Venanzi, M.8    Tartaglia, M.9    Palleschi, A.10
  • 51
    • 0033580431 scopus 로고    scopus 로고
    • The Shp-2 tyrosine phosphatase activates the Src tyrosine kinase by a non-enzymatic mechanism
    • Walter AO, Peng ZY, Cartwright CA. 1999. The Shp-2 tyrosine phosphatase activates the Src tyrosine kinase by a non-enzymatic mechanism. Oncogene 18:1911-1920. http://dx.doi.org/10.1038/sj.onc.1202513.
    • (1999) Oncogene , vol.18 , pp. 1911-1920
    • Walter, A.O.1    Peng, Z.Y.2    Cartwright, C.A.3
  • 52
    • 0028837693 scopus 로고
    • Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association
    • Peng Z-Y, Cartwright CA. 1995. Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association. Oncogene 11:1955-1962.
    • (1995) Oncogene , vol.11 , pp. 1955-1962
    • Peng, Z.-Y.1    Cartwright, C.A.2


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