메뉴 건너뛰기




Volumn 287, Issue 32, 2012, Pages 27066-27077

Counteracting effects operating on Src homology 2 domain-containing protein-tyrosine phosphatase 2 (SHP2) function drive selection of the recurrent Y62D and Y63C substitutions in Noonan syndrome

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC CONTROL; AMINO ACID SUBSTITUTION; BINDING PROPERTIES; BIOCHEMICAL DATA; DISRUPTIVE EFFECTS; DRIVING FORCES; MOLECULAR MECHANISM; PHOSPHOPEPTIDES; PROTEIN-TYROSINE PHOSPHATASE; SRC HOMOLOGY 2; STRUCTURAL REARRANGEMENT;

EID: 84864550789     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.350231     Document Type: Article
Times cited : (29)

References (48)
  • 5
    • 78650393745 scopus 로고    scopus 로고
    • Disorders of dysregulated signal traffic through the RAS-MAPK pathway: Phenotypic spectrum and molecular mechanisms
    • Tartaglia, M., and Gelb, B. D. (2010) Disorders of dysregulated signal traffic through the RAS-MAPK pathway: phenotypic spectrum and molecular mechanisms. Ann. N.Y. Acad. Sci. 1214, 99-121
    • (2010) Ann. N.Y. Acad. Sci. , vol.1214 , pp. 99-121
    • Tartaglia, M.1    Gelb, B.D.2
  • 6
    • 0038771965 scopus 로고    scopus 로고
    • The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
    • DOI 10.1016/S0968-0004(03)00091-4
    • Neel, B. G., Gu, H., and Pao, L. (2003) The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends Biochem. Sci. 28, 284-293 (Pubitemid 36776291)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.6 , pp. 284-293
    • Neel, B.G.1    Gu, H.2    Pao, L.3
  • 7
    • 0032548830 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine phosphatase SHP-2
    • DOI 10.1016/S0092-8674(00)80938-1
    • Hof, P., Pluskey, S., Dhe-Paganon, S., Eck, M. J., and Shoelson, S. E. (1998) Crystal structure of the tyrosine phosphatase SHP-2. Cell 92, 441-450 (Pubitemid 28101108)
    • (1998) Cell , vol.92 , Issue.4 , pp. 441-450
    • Hof, P.1    Pluskey, S.2    Dhe-Paganon, S.3    Eck, M.J.4    Shoelson, S.E.5
  • 10
    • 24744465207 scopus 로고    scopus 로고
    • Diverse biochemical properties of Shp2 mutants: Implications for disease phenotypes
    • DOI 10.1074/jbc.M504699200
    • Keilhack, H., David, F. S., McGregor, M., Cantley, L. C., and Neel, B. G. (2005) Diverse biochemical properties of Shp2 mutants: implications for disease phenotypes. J. Biol. Chem. 280, 30984-30993 (Pubitemid 41291831)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.35 , pp. 30984-30993
    • Keilhack, H.1    David, F.S.2    McGregor, M.3    Cantley, L.C.4    Neel, B.G.5
  • 13
    • 33646117025 scopus 로고    scopus 로고
    • Reduced phosphatase activity of SHP-2 in LEOPARDsyndrome: Consequences for PI3K binding on Gab1
    • Hanna, N., Montagner, A., Lee, W. H., Miteva, M., Vidal, M., Vidaud, M., Parfait, B., and Raynal, P. (2006) Reduced phosphatase activity of SHP-2 in LEOPARDsyndrome: consequences for PI3K binding on Gab1. FEBS Lett. 580, 2477-2482
    • (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
  • 14
    • 33646096207 scopus 로고    scopus 로고
    • PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects
    • DOI 10.1074/jbc.M513068200
    • Kontaridis, M. I., Swanson, K. D., David, F. S., Barford, D., and Neel, B. G. (2006) PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects. J. Biol. Chem. 281, 6785-6792 (Pubitemid 43847615)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.10 , pp. 6785-6792
    • Kontaridis, M.I.1    Swanson, K.D.2    David, F.S.3    Barford, D.4    Neel, B.G.5
  • 15
    • 0038278866 scopus 로고    scopus 로고
    • Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia
    • DOI 10.1038/ng1156
    • Tartaglia, M., Niemeyer, C. M., Fragale, A., Song, X., Buechner, J., Jung, A., Hählen, K., Hasle, H., Licht, J. D., and Gelb, B. D. (2003) Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes, and acute myeloid leukemia. Nat. Genet. 34, 148-150 (Pubitemid 36666923)
    • (2003) Nature Genetics , vol.34 , Issue.2 , pp. 148-150
    • Tartaglia, M.1    Niemeyer, C.M.2    Fragale, A.3    Song, X.4    Buechner, J.5    Jung, A.6    Hahlen, K.7    Hasle, H.8    Licht, J.D.9    Gelb, B.D.10
  • 18
    • 18244395853 scopus 로고    scopus 로고
    • Human somatic PTPN11 mutations induce hematopoietic-cell hypersensitivity to granulocyte-macrophage colony-stimulating factor
    • DOI 10.1182/blood-2004-10-4002
    • Chan, R. J., Leedy, M. B., Munugalavadla, V., Voorhorst, C. S., Li, Y., Yu, M., and Kapur, R. (2005) Human somatic PTPN11 mutations induce hematopoietic cell hypersensitivity to granulocyte-macrophage colony-stimulating factor. Blood 105, 3737-3742 (Pubitemid 40628224)
    • (2005) Blood , vol.105 , Issue.9 , pp. 3737-3742
    • Chan, R.J.1    Leedy, M.B.2    Munugalavadla, V.3    Voorhorst, C.S.4    Li, Y.5    Yu, M.6    Kapur, R.7
  • 19
    • 22044452124 scopus 로고    scopus 로고
    • Functional analysis of leukemia-associated PTPN11 mutations in primary hematopoietic cells
    • DOI 10.1182/blood-2004-11-4207
    • Schubbert, S., Lieuw, K., Rowe, S. L., Lee, C. M., Li, X., Loh, M. L., Clapp, D. W., and Shannon, K. M. (2005) Functional analysis of leukemia-associated PTPN11 mutations in primary hematopoietic cells. Blood 106, 311-317 (Pubitemid 40967207)
    • (2005) Blood , vol.106 , Issue.1 , pp. 311-317
    • Schubbert, S.1    Lieuw, K.2    Rowe, S.L.3    Lee, C.M.4    Li, X.5    Loh, M.L.6    Clapp, D.W.7    Shannon, K.M.8
  • 20
    • 1542619343 scopus 로고    scopus 로고
    • Noonan Syndrome-Associated SHP2/PTPN11 Mutants Cause EGF-Dependent Prolonged GAB1 Binding and Sustained ERK2/MAPK1 Activation
    • DOI 10.1002/humu.20005
    • Fragale, A., Tartaglia, M., Wu, J., and Gelb, B. D. (2004) Noonan syndrome-associated SHP2/PTPN11 mutants cause EGF-dependent prolonged GAB1 binding and sustained ERK2/MAPK1 activation. Hum. Mutat. 23, 267-277 (Pubitemid 38337891)
    • (2004) Human Mutation , vol.23 , Issue.3 , pp. 267-277
    • Fragale, A.1    Tartaglia, M.2    Wu, J.3    Gelb, B.D.4
  • 22
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., van der Spoel, D., and Lindahl, E. (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 24
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-Pdb-Viewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 25
    • 0002775934 scopus 로고
    • Interaction Models for Water in Relation to Protein Hydration
    • (Pullman, B., ed) . Reidel Publishing Company, Dordrecht, The Netherlands
    • Berendsen, H. J., Postma, J. P., van Gunsteren, W. F., and Hermans, J. (1981) Interaction Models for Water in Relation to Protein Hydration in Intermolecular Forces (Pullman, B., ed) pp. 331-342, Reidel Publishing Company, Dordrecht, The Netherlands
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.1    Postma, J.P.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 26
    • 84986440341 scopus 로고
    • Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • Miyamoto, S., and Kollman, P. A. (1992) Settle: an analytical version of the SHAKE and RATTLE algorithm for rigid water models. J. Comp. Chem. 13, 952-962
    • (1992) J. Comp. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 29
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55 (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 33
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • DOI 10.1006/jmbi.1999.3310
    • Blom, N., Gammeltoft, S., and Brunak, S. (1999) Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J. Mol. Biol. 294, 1351-1362 (Pubitemid 30008805)
    • (1999) Journal of Molecular Biology , vol.294 , Issue.5 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 34
    • 33745622868 scopus 로고    scopus 로고
    • Two Sample Logo: A graphical representation of the differences between two sets of sequence alignments
    • DOI 10.1093/bioinformatics/btl151
    • Vacic, V., Iakoucheva, L. M., and Radivojac, P. (2006) Two Sample Logo: a graphical representation of the differences between two sets of sequence alignments. Bioinformatics 22, 1536-1537 (Pubitemid 43985328)
    • (2006) Bioinformatics , vol.22 , Issue.12 , pp. 1536-1537
    • Vacic, V.1    Iakoucheva, L.M.2    Radivojac, P.3
  • 35
    • 34250721648 scopus 로고    scopus 로고
    • Peptide arrays on cellulose support: SPOT synthesis, a time and cost efficient method for synthesis of large numbers of peptides in a parallel and addressable fashion
    • DOI 10.1038/nprot.2007.160, PII NPROT.2007.160
    • Hilpert, K., Winkler, D. F., and Hancock, R. E. (2007) Peptide arrays on cellulose support: SPOT synthesis, a time- and cost-efficient method for synthesis of large numbers of peptides in a parallel and addressable fashion. Nat. Protoc. 2, 1333-1349 (Pubitemid 46952315)
    • (2007) Nature Protocols , vol.2 , Issue.6 , pp. 1333-1349
    • Hilpert, K.1    Winkler, D.F.H.2    Hancock, R.E.W.3
  • 36
    • 0033989423 scopus 로고    scopus 로고
    • Activated mutants of SHP-2 preferentially induce elongation of Xenopus animal caps
    • O'Reilly, A. M., Pluskey, S., Shoelson, S. E., and Neel, B. G. (2000) Activated mutants of SHP-2 preferentially induce elongation of Xenopus animal caps. Mol. Cell Biol. 20, 299-311 (Pubitemid 30002571)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.1 , pp. 299-311
    • O'Reilly, A.M.1    Pluskey, S.2    Shoelson, S.E.3    Neel, B.G.4
  • 39
    • 24644434907 scopus 로고    scopus 로고
    • Alternative mode of binding to phosphotyrosyl peptides by Src homology-2 domains
    • DOI 10.1021/bi050669o
    • Qin, C., Wavreille, A. S., and Pei, D. (2005) Alternative mode of binding to phosphotyrosyl peptides by Src homology-2 domains. Biochemistry 44, 12196-12202 (Pubitemid 41285718)
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 12196-12202
    • Qin, C.1    Wavreille, A.-S.2    Pei, D.3
  • 40
    • 24644500492 scopus 로고    scopus 로고
    • Decoding protein-protein interactions through combinatorial chemistry: Sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains
    • DOI 10.1021/bi051408h
    • Sweeney, M. C., Wavreille, A. S., Park, J., Butchar, J. P., Tridandapani, S., and Pei, D. (2005) Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains. Biochemistry 44, 14932-14947 (Pubitemid 41612272)
    • (2005) Biochemistry , vol.44 , Issue.45 , pp. 14932-14947
    • Sweeney, M.C.1    Wavreille, A.-S.2    Park, J.3    Butchar, J.P.4    Tridandapani, S.5    Pei, D.6
  • 41
    • 0028773467 scopus 로고
    • Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase
    • Lee, C. H., Kominos, D., Jacques, S., Margolis, B., Schlessinger, J., Shoelson, S. E., and Kuriyan, J. (1994) Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase. Structure 2, 423-438
    • (1994) Structure , vol.2 , pp. 423-438
    • Lee, C.H.1    Kominos, D.2    Jacques, S.3    Margolis, B.4    Schlessinger, J.5    Shoelson, S.E.6    Kuriyan, J.7
  • 42
    • 0030066325 scopus 로고    scopus 로고
    • Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2
    • Eck, M. J., Pluskey, S., Trüb, T., Harrison, S. C., and Shoelson, S. E. (1996) Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2. Nature 379, 277-280
    • (1996) Nature , vol.379 , pp. 277-280
    • Eck, M.J.1    Pluskey, S.2    Trüb, T.3    Harrison, S.C.4    Shoelson, S.E.5
  • 43
    • 0028021665 scopus 로고
    • Characterization of protein-tyrosine phosphatase SH-PTP2: Study of phosphopeptide substrates and possible regulatory role of SH2 domains
    • Dechert, U., Adam, M., Harder, K. W., Clark-Lewis, I., and Jirik, F. (1994) Characterization of protein-tyrosine phosphatase SH-PTP2: study of phosphopeptide substrates and possible regulatory role of SH2 domains. J. Biol. Chem. 269, 5602-5611
    • (1994) J. Biol. Chem. , vol.269 , pp. 5602-5611
    • Dechert, U.1    Adam, M.2    Harder, K.W.3    Clark-Lewis, I.4    Jirik, F.5
  • 44
    • 34047192313 scopus 로고    scopus 로고
    • 66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2 domain phosphotyrosine-peptide-binding cleft
    • 66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2 domain phosphotyrosine-peptide-binding cleft. BMC Struct. Biol. 7, 14
    • (2007) BMC Struct. Biol. , vol.7 , pp. 14
    • Guvench, O.1    Qu, C.K.2    MacKerell Jr., A.D.3
  • 47
    • 0030797548 scopus 로고    scopus 로고
    • A deletion mutation in the SH2-N domain of Shp-2 severely suppresses hematopoietic cell development
    • Qu, C. K., Shi, Z. Q., Shen, R., Tsai, F. Y., Orkin, S. H., and Feng, G. S. (1997) A deletion mutation in the SH2-N domain of Shp-2 severely suppresses hematopoietic cell development. Mol. Cell. Biol. 17, 5499-5507 (Pubitemid 27357646)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.9 , pp. 5499-5507
    • Qu, C.-K.1    Shi, Z.-Q.2    Shen, R.3    Tsai, F.-Y.4    Orkin, S.H.5    Feng, G.-S.6
  • 48
    • 0030921502 scopus 로고    scopus 로고
    • Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2
    • DOI 10.1093/emboj/16.9.2352
    • Saxton, T. M., Henkemeyer, M., Gasca, S., Shen, R., Rossi, D. J., Shalaby, F., Feng, G. S., and Pawson, T. (1997) Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2. EMBO J. 16, 2352-2364 (Pubitemid 27258636)
    • (1997) EMBO Journal , vol.16 , Issue.9 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.