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Volumn 4, Issue , 2013, Pages

Antagonism between binding site affinity and conformational dynamics tunes alternative cis-interactions within Shp2

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOTYROSINE; PLATELET DERIVED GROWTH FACTOR BETA RECEPTOR; PROTEIN TYROSINE PHOSPHATASE SHP 2; MUTANT PROTEIN; PEPTIDE; PROTEIN BINDING;

EID: 84891589105     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms3037     Document Type: Article
Times cited : (31)

References (44)
  • 1
    • 0036441510 scopus 로고    scopus 로고
    • Autoinhibitory domains: Modular effectors of cellular regulation
    • Pufall, M. A. & Graves, B. J. Autoinhibitory domains: modular effectors of cellular regulation. Annu. Rev. Cell. Dev. Biol. 18, 421-462 (2002).
    • (2002) Annu. Rev. Cell. Dev. Biol. , vol.18 , pp. 421-462
    • Pufall, M.A.1    Graves, B.J.2
  • 2
    • 33746363486 scopus 로고    scopus 로고
    • Domains, motifs, and scaffolds: The role of modular interactions in the evolution and wiring of cell signaling circuits
    • Bhattacharyya, R. P., Remenyi, A., Yeh, B. J. & Lim, W. A. Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Annu. Rev. Biochem. 75, 655-680 (2006).
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 655-680
    • Bhattacharyya, R.P.1    Remenyi, A.2    Yeh, B.J.3    Lim, W.A.4
  • 3
    • 0027393534 scopus 로고
    • Effects of a single base-pair deletion in the bacteriophage lambda PRM promoter. Repression of PRM by repressor bound at OR2 and by RNA polymerase bound at PR
    • Woody, S. T., Fong, R. S. & Gussin, G. N. Effects of a single base-pair deletion in the bacteriophage lambda PRM promoter. Repression of PRM by repressor bound at OR2 and by RNA polymerase bound at PR. J. Mol. Biol. 229, 37-51 (1993).
    • (1993) J. Mol. Biol. , vol.229 , pp. 37-51
    • Woody, S.T.1    Fong, R.S.2    Gussin, G.N.3
  • 4
    • 36249017917 scopus 로고    scopus 로고
    • Programming gene expression with combinatorial promoters
    • Cox, 3rd R. S., Surette, M. G. & Elowitz, M. B. Programming gene expression with combinatorial promoters. Mol. Syst. Biol. 3, 145 (2007).
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 145
    • Cox, R.S.1    Surette, M.G.2    Elowitz, M.B.3
  • 5
    • 34547925618 scopus 로고    scopus 로고
    • Combinatorial promoter design for engineering noisy gene expression
    • Murphy, K. F., Balazsi, G. & Collins, J. J. Combinatorial promoter design for engineering noisy gene expression. Proc. Natl Acad. Sci. USA 104, 12726-12731 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 12726-12731
    • Murphy, K.F.1    Balazsi, G.2    Collins, J.J.3
  • 6
    • 77649270851 scopus 로고    scopus 로고
    • Detecting the conformation of individual proteins in live cells
    • Sakon, J. J. & Weninger, K. R. Detecting the conformation of individual proteins in live cells. Nat. Methods 7, 203-205 (2010).
    • (2010) Nat. Methods , vol.7 , pp. 203-205
    • Sakon, J.J.1    Weninger, K.R.2
  • 7
    • 32944458874 scopus 로고    scopus 로고
    • Fluorescence (Forster) resonance energy transfer imaging of oncogene activity in living cells
    • Kiyokawa, E., Hara, S., Nakamura, T. & Matsuda, M. Fluorescence (Forster) resonance energy transfer imaging of oncogene activity in living cells. Cancer Sci. 97, 8-15 (2006).
    • (2006) Cancer Sci. , vol.97 , pp. 8-15
    • Kiyokawa, E.1    Hara, S.2    Nakamura, T.3    Matsuda, M.4
  • 8
    • 50249098131 scopus 로고    scopus 로고
    • Fluorescence proteins, live-cell imaging, and mechanobiology: Seeing is believing
    • Wang, Y., Shyy, J. Y. & Chien, S. Fluorescence proteins, live-cell imaging, and mechanobiology: seeing is believing. Annu. Rev. Biomed. Eng. 10, 1-38 (2008).
    • (2008) Annu. Rev. Biomed. Eng. , vol.10 , pp. 1-38
    • Wang, Y.1    Shyy, J.Y.2    Chien, S.3
  • 9
    • 70349124959 scopus 로고    scopus 로고
    • Fluorescent biosensors for real-time tracking of post-translational modification dynamics
    • Aye-Han, N. N., Ni, Q. & Zhang, J. Fluorescent biosensors for real-time tracking of post-translational modification dynamics. Curr. Opin. Chem. Biol. 13, 392-397 (2009).
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 392-397
    • Aye-Han, N.N.1    Ni, Q.2    Zhang, J.3
  • 10
    • 84867084476 scopus 로고    scopus 로고
    • Improving FRET dynamic range with bright green and red fluorescent proteins
    • Lam, A. J. et al. Improving FRET dynamic range with bright green and red fluorescent proteins. Nat. Methods 9, 1005-1012 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 1005-1012
    • Lam, A.J.1
  • 11
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: From genes, to function, to disease
    • Tonks, N. K. Protein tyrosine phosphatases: from genes, to function, to disease. Nat. Rev. Mol. Cell. Biol. 7, 833-846 (2006).
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 12
    • 79955979289 scopus 로고    scopus 로고
    • Ptpn11/Shp2 acts as a tumor suppressor in hepatocellular carcinogenesis
    • Bard-Chapeau, E. A. et al. Ptpn11/Shp2 acts as a tumor suppressor in hepatocellular carcinogenesis. Cancer Cell 19, 629-639 (2011).
    • (2011) Cancer Cell , vol.19 , pp. 629-639
    • Bard-Chapeau, E.A.1
  • 13
    • 43049093663 scopus 로고    scopus 로고
    • The tyrosine phosphatase Shp2 (PTPN11) in cancer
    • Chan, G., Kalaitzidis, D. & Neel, B. G. The tyrosine phosphatase Shp2 (PTPN11) in cancer. Cancer Metastasis. Rev. 27, 179-192 (2008).
    • (2008) Cancer Metastasis. Rev. , vol.27 , pp. 179-192
    • Chan, G.1    Kalaitzidis, D.2    Neel, B.G.3
  • 14
    • 18344385476 scopus 로고    scopus 로고
    • Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome
    • Tartaglia, M. et al. Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Nat. Genet. 29, 465-468 (2001).
    • (2001) Nat. Genet. , vol.29 , pp. 465-468
    • Tartaglia, M.1
  • 15
    • 18444401014 scopus 로고    scopus 로고
    • Noonan syndrome and related disorders: Genetics and pathogenesis
    • Tartaglia, M. & Gelb, B. D. Noonan syndrome and related disorders: genetics and pathogenesis. Annu. Rev. Genomics Hum. Genet. 6, 45-68 (2005).
    • (2005) Annu. Rev. Genomics Hum. Genet. , vol.6 , pp. 45-68
    • Tartaglia, M.1    Gelb, B.D.2
  • 16
    • 12144286410 scopus 로고    scopus 로고
    • Mutations in PTPN11 implicate the SHP-2 phosphatase in leukemogenesis
    • Loh, M. L. et al. Mutations in PTPN11 implicate the SHP-2 phosphatase in leukemogenesis. Blood 103, 2325-2331 (2004).
    • (2004) Blood , vol.103 , pp. 2325-2331
    • Loh, M.L.1
  • 17
    • 0038278866 scopus 로고    scopus 로고
    • Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia
    • Tartaglia, M. et al. Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia. Nat. Genet. 34, 148-150 (2003).
    • (2003) Nat. Genet. , vol.34 , pp. 148-150
    • Tartaglia, M.1
  • 18
    • 0038771965 scopus 로고    scopus 로고
    • The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
    • Neel, B. G., Gu, H. & Pao, L. The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends Biochem. Sci. 28, 284-293 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 284-293
    • Neel, B.G.1    Gu, H.2    Pao, L.3
  • 19
    • 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, P. A. 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).
    • (2001) Mol. Cell. , vol.8 , pp. 759-769
    • Lu, W.1    Gong, D.2    Bar-Sagi, D.3    Cole, P.A.4
  • 20
    • 55749093427 scopus 로고    scopus 로고
    • Determination of hierarchical relationship of Src and Rac at subcellular locations with FRET biosensors
    • Ouyang, M., Sun, J., Chien, S. & Wang, Y. Determination of hierarchical relationship of Src and Rac at subcellular locations with FRET biosensors. Proc. Natl Acad. Sci. USA 105, 14353-14358 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 14353-14358
    • Ouyang, M.1    Sun, J.2    Chien, S.3    Wang, Y.4
  • 21
    • 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., Trub, T., Harrison, S. C. & Shoelson, S. E. Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2. Nature 379, 277-280 (1996).
    • (1996) Nature , vol.379 , pp. 277-280
    • Eck, M.J.1    Pluskey, S.2    Trub, T.3    Harrison, S.C.4    Shoelson, S.E.5
  • 22
    • 0142211311 scopus 로고    scopus 로고
    • Tyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factors
    • Araki, T., Nawa, H. & Neel, B. G. Tyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factors. J. Biol. Chem. 278, 41677-41684 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 41677-41684
    • Araki, T.1    Nawa, H.2    Neel, B.G.3
  • 23
    • 0028123457 scopus 로고
    • A new function for a phosphotyrosine phosphatase: Linking GRB2-Sos to a receptor tyrosine kinase
    • Li, W. et al. A new function for a phosphotyrosine phosphatase: linking GRB2-Sos to a receptor tyrosine kinase. Mol. Cell. Biol. 14, 509-517 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 509-517
    • Li, W.1
  • 24
    • 0029966854 scopus 로고    scopus 로고
    • The TEL/platelet-derived growth factor beta receptor (PDGF beta R) fusion in chronic myelomonocytic leukemia is a transforming protein that self-associates and activates PDGF beta R kinase-dependent signaling pathways
    • Carroll, M., Tomasson, M. H., Barker, G. F., Golub, T. R. & Gilliland, D. G. The TEL/platelet-derived growth factor beta receptor (PDGF beta R) fusion in chronic myelomonocytic leukemia is a transforming protein that self-associates and activates PDGF beta R kinase-dependent signaling pathways. Proc. Natl Acad. Sci. USA 93, 14845-14850 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14845-14850
    • Carroll, M.1    Tomasson, M.H.2    Barker, G.F.3    Golub, T.R.4    Gilliland, D.G.5
  • 25
    • 38049151008 scopus 로고    scopus 로고
    • Regulation of platelet-derived growth factor receptor activation by afadin through SHP-2: Implications for cellular morphology
    • Nakata, S. et al. Regulation of platelet-derived growth factor receptor activation by afadin through SHP-2: implications for cellular morphology. J. Biol. Chem. 282, 37815-37825 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 37815-37825
    • Nakata, S.1
  • 26
    • 0030961779 scopus 로고    scopus 로고
    • How Src exercises self-restraint
    • Nguyen, J. T. & Lim, W. A. How Src exercises self-restraint. Nat. Struct. Biol. 4, 256-260 (1997).
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 256-260
    • Nguyen, J.T.1    Lim, W.A.2
  • 27
    • 0037819447 scopus 로고    scopus 로고
    • Transcription regulation and animal diversity
    • Levine, M. & Tjian, R. Transcription regulation and animal diversity. Nature 424, 147-151 (2003).
    • (2003) Nature , vol.424 , pp. 147-151
    • Levine, M.1    Tjian, R.2
  • 28
    • 77952944052 scopus 로고    scopus 로고
    • Designing customized cell signalling circuits
    • Lim, W. A. Designing customized cell signalling circuits. Nat. Rev. Mol. Cell. Biol. 11, 393-403 (2010).
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 393-403
    • Lim, W.A.1
  • 29
    • 71849110893 scopus 로고    scopus 로고
    • Next-generation synthetic gene networks
    • Lu, T. K., Khalil, A. S. & Collins, J. J. Next-generation synthetic gene networks. Nat. Biotechnol. 27, 1139-1150 (2009).
    • (2009) Nat. Biotechnol , vol.27 , pp. 1139-1150
    • Lu, T.K.1    Khalil, A.S.2    Collins, J.J.3
  • 30
    • 40849100220 scopus 로고    scopus 로고
    • Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics
    • Bashor, C. J., Helman, N. C., Yan, S. & Lim, W. A. Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics. Science 319, 1539-1543 (2008).
    • (2008) Science , vol.319 , pp. 1539-1543
    • Bashor, C.J.1    Helman, N.C.2    Yan, S.3    Lim, W.A.4
  • 31
    • 79955770162 scopus 로고    scopus 로고
    • Scaffold proteins: Hubs for controlling the flow of cellular information
    • Good, M. C., Zalatan, J. G. & Lim, W. A. Scaffold proteins: hubs for controlling the flow of cellular information. Science 332, 680-686 (2011).
    • (2011) Science , vol.332 , pp. 680-686
    • Good, M.C.1    Zalatan, J.G.2    Lim, W.A.3
  • 32
    • 77956141521 scopus 로고    scopus 로고
    • Phosphotyrosine signaling: Evolving a new cellular communication system
    • Lim, W. A. & Pawson, T. Phosphotyrosine signaling: evolving a new cellular communication system. Cell 142, 661-667 (2011).
    • (2011) Cell , vol.142 , pp. 661-667
    • Lim, W.A.1    Pawson, T.2
  • 33
    • 79954624505 scopus 로고    scopus 로고
    • Structural mechanism associated with domain opening in gain-of-function mutations in SHP2 phosphatase
    • Darian, E., Guvench, O., Yu, B., Qu, C. K. & MacKerell, Jr A. D. Structural mechanism associated with domain opening in gain-of-function mutations in SHP2 phosphatase. Proteins 79, 1573-1588 (2011).
    • (2011) Proteins , vol.79 , pp. 1573-1588
    • Darian, E.1    Guvench, O.2    Yu, B.3    Qu, C.K.4    MacKerell, A.D.5
  • 34
    • 34047192313 scopus 로고    scopus 로고
    • Tyr66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2-domain phosphotyrosine-peptide binding cleft
    • Guvench, O., Qu, C. K. & MacKerell, Jr A. D. Tyr66 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).
    • (2007) BMC Struct. Biol. , vol.7 , pp. 14
    • Guvench, O.1    Qu, C.K.2    MacKerell, A.D.3
  • 35
    • 0028282967 scopus 로고
    • Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1
    • Sugimoto, S., Wandless, T. J., Shoelson, S. E., Neel, B. G. & Walsh, C. T. Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1. J. Biol. Chem. 269, 13614-13622 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 13614-13622
    • Sugimoto, S.1    Wandless, T.J.2    Shoelson, S.E.3    Neel, B.G.4    Walsh, C.T.5
  • 36
    • 0032548830 scopus 로고    scopus 로고
    • Crystal structure of the tyrosine phosphatase SHP-2
    • Hof, P., Pluskey, S., Dhe-Paganon, S., Eck, M. J. & Shoelson, S. E. Crystal structure of the tyrosine phosphatase SHP-2. Cell 92, 441-450 (1998).
    • (1998) Cell , vol.92 , pp. 441-450
    • Hof, P.1    Pluskey, S.2    Dhe-Paganon, S.3    Eck, M.J.4    Shoelson, S.E.5
  • 37
    • 0027910431 scopus 로고
    • Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • Egan, S. E. et al. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature 363, 45-51 (1993).
    • (1993) Nature , vol.363 , pp. 45-51
    • Egan, S.E.1
  • 38
    • 38349004658 scopus 로고    scopus 로고
    • The molecular functions of Shp2 in the Ras/Mitogen-activated protein kinase (ERK1/2) pathway
    • Dance, M., Montagner, A., Salles, J. P., Yart, A. & Raynal, P. The molecular functions of Shp2 in the Ras/Mitogen-activated protein kinase (ERK1/2) pathway. Cell Signal. 20, 453-459 (2008).
    • (2008) Cell Signal , vol.20 , pp. 453-459
    • Dance, M.1    Montagner, A.2    Salles, J.P.3    Yart, A.4    Raynal, P.5
  • 39
    • 33847355217 scopus 로고    scopus 로고
    • Growth factor-induced MAPK network topology shapes Erk response determining PC-12 cell fate
    • Santos, S. D., Verveer, P. J. & Bastiaens, P. I. Growth factor-induced MAPK network topology shapes Erk response determining PC-12 cell fate. Nat. Cell. Biol. 9, 324-330 (2007).
    • (2007) Nat. Cell. Biol. , vol.9 , pp. 324-330
    • Santos, S.D.1    Verveer, P.J.2    Bastiaens, P.I.3
  • 40
    • 70349451178 scopus 로고    scopus 로고
    • The phosphatase SHP2 regulates the spacing effect for long-term memory induction
    • Pagani, M. R., Oishi, K., Gelb, B. D. & Zhong, Y. The phosphatase SHP2 regulates the spacing effect for long-term memory induction. Cell 139, 186-198 (2009).
    • (2009) Cell , vol.139 , pp. 186-198
    • Pagani, M.R.1    Oishi, K.2    Gelb, B.D.3    Zhong, Y.4
  • 41
    • 0035575586 scopus 로고    scopus 로고
    • SH2 domains, interaction modules and cellular wiring
    • Pawson, T., Gish, G. D. & Nash, P. SH2 domains, interaction modules and cellular wiring. Trends Cell Biol. 11, 504-511 (2001).
    • (2001) Trends Cell Biol. , vol.11 , pp. 504-511
    • Pawson, T.1    Gish, G.D.2    Nash, P.3
  • 42
    • 7944223078 scopus 로고    scopus 로고
    • Structure and regulation of Src family kinases
    • Boggon, T. J. & Eck, M. J. Structure and regulation of Src family kinases. Oncogene 23, 7918-7927 (2004).
    • (2004) Oncogene , vol.23 , pp. 7918-7927
    • Boggon, T.J.1    Eck, M.J.2
  • 43
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown, M. T. & Cooper, J. A. Regulation, substrates and functions of src. Biochim. Biophys. Acta. 1287, 121-149 (1996).
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 44


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