메뉴 건너뛰기




Volumn 356, Issue 1, 2006, Pages 142-154

Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction

Author keywords

MAPKKK; Nuclear magnetic resonance; Sterile alpha motif

Indexed keywords

AMINO ACID; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; MUTANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 30344433269     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.11.012     Document Type: Article
Times cited : (30)

References (34)
  • 1
    • 0029999863 scopus 로고    scopus 로고
    • Ste50p sustains mating pheromone-induced signal transduction in the yeast Saccharomyces cerevisiae
    • G. Xu, G. Jansen, D.Y. Thomas, C.P. Hollenberg, and M. Ramezani Rad Ste50p sustains mating pheromone-induced signal transduction in the yeast Saccharomyces cerevisiae Mol. Microbiol. 20 1996 773 783
    • (1996) Mol. Microbiol. , vol.20 , pp. 773-783
    • Xu, G.1    Jansen, G.2    Thomas, D.Y.3    Hollenberg, C.P.4    Ramezani Rad, M.5
  • 2
    • 0031658234 scopus 로고    scopus 로고
    • Requirement of STE50 for osmostress-induced activation of the STE11 mitogen-activated protein kinase kinase kinase in the high-osmolarity glycerol response pathway
    • F. Posas, E.A. Witten, and H. Saito Requirement of STE50 for osmostress-induced activation of the STE11 mitogen-activated protein kinase kinase kinase in the high-osmolarity glycerol response pathway Mol. Cell. Biol. 18 1998 5788 5796
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5788-5796
    • Posas, F.1    Witten, E.A.2    Saito, H.3
  • 3
    • 0031683956 scopus 로고    scopus 로고
    • Ste50p is involved in regulating filamentous growth in the yeast Saccharomyces cerevisiae and associates with Ste11p
    • M. Ramezani Rad, G. Jansen, F. Buhring, and C.P. Hollenberg Ste50p is involved in regulating filamentous growth in the yeast Saccharomyces cerevisiae and associates with Ste11p Mol. Gen. Genet. 259 1998 29 38
    • (1998) Mol. Gen. Genet. , vol.259 , pp. 29-38
    • Ramezani Rad, M.1    Jansen, G.2    Buhring, F.3    Hollenberg, C.P.4
  • 4
    • 0026619906 scopus 로고
    • STE50, a novel gene required for activation of conjugation at an early step in mating in Saccharomyces cerevisiae
    • M.R. Ramezani Rad, G. Xu, and C.P. Hollenberg STE50, a novel gene required for activation of conjugation at an early step in mating in Saccharomyces cerevisiae Mol. Gen. Genet. 236 1992 145 154
    • (1992) Mol. Gen. Genet. , vol.236 , pp. 145-154
    • Ramezani Rad, M.R.1    Xu, G.2    Hollenberg, C.P.3
  • 5
    • 0038112138 scopus 로고    scopus 로고
    • The role of adaptor protein Ste50-dependent regulation of the MAPKKK Ste11 in multiple signalling pathways of yeast
    • M. Ramezani Rad The role of adaptor protein Ste50-dependent regulation of the MAPKKK Ste11 in multiple signalling pathways of yeast Curr. Genet. 43 2003 161 170
    • (2003) Curr. Genet. , vol.43 , pp. 161-170
    • Ramezani Rad, M.1
  • 6
    • 0032837521 scopus 로고    scopus 로고
    • Functional characterization of the interaction of Ste50p with Ste11p MAPKKK in Saccharomyces cerevisiae
    • C. Wu, E. Leberer, D.Y. Thomas, and M. Whiteway Functional characterization of the interaction of Ste50p with Ste11p MAPKKK in Saccharomyces cerevisiae Mol. Biol. Cell 10 1999 2425 2440
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2425-2440
    • Wu, C.1    Leberer, E.2    Thomas, D.Y.3    Whiteway, M.4
  • 7
    • 0033647489 scopus 로고    scopus 로고
    • Pheromone response, mating and cell biology
    • E.A. Elion Pheromone response, mating and cell biology Curr. Opin. Microbiol. 3 2000 573 581
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 573-581
    • Elion, E.A.1
  • 8
    • 0035089150 scopus 로고    scopus 로고
    • Mutations in the SAM domain of STE50 differentially influence the MAPK-mediated pathways for mating, filamentous growth and osmotolerance in Saccharomyces cerevisiae
    • G. Jansen, F. Buhring, C.P. Hollenberg, and M. Ramezani Rad Mutations in the SAM domain of STE50 differentially influence the MAPK-mediated pathways for mating, filamentous growth and osmotolerance in Saccharomyces cerevisiae Mol. Genet. Genomics 265 2001 102 117
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 102-117
    • Jansen, G.1    Buhring, F.2    Hollenberg, C.P.3    Ramezani Rad, M.4
  • 9
    • 0029091904 scopus 로고
    • SAM: A novel motif in yeast sterile and Drosophila polyhomeotic proteins
    • C.P. Ponting SAM: a novel motif in yeast sterile and Drosophila polyhomeotic proteins Protein Sci. 4 1995 1928 1930
    • (1995) Protein Sci. , vol.4 , pp. 1928-1930
    • Ponting, C.P.1
  • 10
    • 0345306620 scopus 로고    scopus 로고
    • Binding of the C-terminal sterile alpha motif (SAM) domain of human p73 to lipid membranes
    • F.N. Barrera, J.A. Poveda, J.M. Gonzalez-Ros, and J.L. Neira Binding of the C-terminal sterile alpha motif (SAM) domain of human p73 to lipid membranes J. Biol. Chem. 278 2003 46878 46885
    • (2003) J. Biol. Chem. , vol.278 , pp. 46878-46885
    • Barrera, F.N.1    Poveda, J.A.2    Gonzalez-Ros, J.M.3    Neira, J.L.4
  • 11
    • 0042490664 scopus 로고    scopus 로고
    • The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators
    • T. Aviv, Z. Lin, S. Lau, L.M. Rendl, F. Sicheri, and C.A. Smibert The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators Nature Struct. Biol. 10 2003 614 621
    • (2003) Nature Struct. Biol. , vol.10 , pp. 614-621
    • Aviv, T.1    Lin, Z.2    Lau, S.3    Rendl, L.M.4    Sicheri, F.5    Smibert, C.A.6
  • 13
    • 30344442873 scopus 로고    scopus 로고
    • The many faces of SAM
    • F. Qiao, and J.U. Bowie The many faces of SAM Sci. STKE 2005 2005 1 7
    • (2005) Sci. STKE , vol.2005 , pp. 1-7
    • Qiao, F.1    Bowie, J.U.2
  • 14
    • 4344631456 scopus 로고    scopus 로고
    • The solution structure of the S. cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50
    • J.J. Kwan, N. Warner, T. Pawson, and L.W. Donaldson The solution structure of the S. cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50 J. Mol. Biol. 342 2004 681 693
    • (2004) J. Mol. Biol. , vol.342 , pp. 681-693
    • Kwan, J.J.1    Warner, N.2    Pawson, T.3    Donaldson, L.W.4
  • 15
    • 0347087434 scopus 로고    scopus 로고
    • Structure of the SAM domain of the S. cerevisiae MAPK pathway modulating protein STE50 and analysis of its interaction with STE11 SAM
    • S.J. Grimshaw, H.R. Mott, K.M. Stott, P.R. Nielson, K.A. Evetts, and L.J. Hopkins Structure of the SAM domain of the S. cerevisiae MAPK pathway modulating protein STE50 and analysis of its interaction with STE11 SAM J. Biol. Chem. 279 2004 2192 2201
    • (2004) J. Biol. Chem. , vol.279 , pp. 2192-2201
    • Grimshaw, S.J.1    Mott, H.R.2    Stott, K.M.3    Nielson, P.R.4    Evetts, K.A.5    Hopkins, L.J.6
  • 18
    • 3242688256 scopus 로고    scopus 로고
    • Derepression by depolymerization; Structural insights into the regulation of Yan by Mae
    • F. Qiao, H. Song, C.A. Kim, M.R. Sawaya, J.B. Hunter, and M. Gingery Derepression by depolymerization; structural insights into the regulation of Yan by Mae Cell 118 2004 163 173
    • (2004) Cell , vol.118 , pp. 163-173
    • Qiao, F.1    Song, H.2    Kim, C.A.3    Sawaya, M.R.4    Hunter, J.B.5    Gingery, M.6
  • 19
    • 23044476138 scopus 로고    scopus 로고
    • Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer
    • C.A. Kim, M.R. Sawaya, D. Cascio, W. Kim, and J.U. Bowie Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer J. Biol. Chem. 280 2005 27769 27775
    • (2005) J. Biol. Chem. , vol.280 , pp. 27769-27775
    • Kim, C.A.1    Sawaya, M.R.2    Cascio, D.3    Kim, W.4    Bowie, J.U.5
  • 20
    • 0035421962 scopus 로고    scopus 로고
    • Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression
    • C.A. Kim, M.L. Phillips, W. Kim, M. Gingery, H.H. Tran, and M.A. Robinson Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression EMBO J. 20 2001 4173 4182
    • (2001) EMBO J. , vol.20 , pp. 4173-4182
    • Kim, C.A.1    Phillips, M.L.2    Kim, W.3    Gingery, M.4    Tran, H.H.5    Robinson, M.A.6
  • 21
    • 14144255403 scopus 로고    scopus 로고
    • Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast: Implications for efficient signaling through the MAPK cascades
    • S. Bhattacharjya, P. Xu, M. Chakrapani, L. Johnston, and F. Ni Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast: implications for efficient signaling through the MAPK cascades Protein Sci. 14 2005 828 835
    • (2005) Protein Sci. , vol.14 , pp. 828-835
    • Bhattacharjya, S.1    Xu, P.2    Chakrapani, M.3    Johnston, L.4    Ni, F.5
  • 22
    • 8544271634 scopus 로고    scopus 로고
    • Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: Implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex
    • S. Bhattacharjya, P. Xu, R. Gingras, R. Shaykhutdinov, C. Wu, M. Whiteway, and F. Ni Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex J. Mol. Biol. 344 2004 1071 1087
    • (2004) J. Mol. Biol. , vol.344 , pp. 1071-1087
    • Bhattacharjya, S.1    Xu, P.2    Gingras, R.3    Shaykhutdinov, R.4    Wu, C.5    Whiteway, M.6    Ni, F.7
  • 23
    • 0032473427 scopus 로고    scopus 로고
    • Activation of the yeast SSK2 MAP kinase kinase kinase by the SSK1 two-component response regulator
    • F. Posas, and H. Saito Activation of the yeast SSK2 MAP kinase kinase kinase by the SSK1 two-component response regulator EMBO J. 17 1998 1385 1394
    • (1998) EMBO J. , vol.17 , pp. 1385-1394
    • Posas, F.1    Saito, H.2
  • 24
    • 0030595378 scopus 로고    scopus 로고
    • Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor
    • F. Posas, S.M. Wurgler-Murphy, T. Maeda, E.A. Witten, T.C. Thai, and H. Saito Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor Cell 86 1996 865 875
    • (1996) Cell , vol.86 , pp. 865-875
    • Posas, F.1    Wurgler-Murphy, S.M.2    Maeda, T.3    Witten, E.A.4    Thai, T.C.5    Saito, H.6
  • 25
    • 23744450036 scopus 로고    scopus 로고
    • Antagonistic regulation of Yan nuclear export by Mae and Crm1 may increase the stringency of the Ras response
    • H. Song, M. Nie, F. Qiao, J.U. Bowie, and A.J. Courey Antagonistic regulation of Yan nuclear export by Mae and Crm1 may increase the stringency of the Ras response Genes Dev. 19 2005 1767 1772
    • (2005) Genes Dev. , vol.19 , pp. 1767-1772
    • Song, H.1    Nie, M.2    Qiao, F.3    Bowie, J.U.4    Courey, A.J.5
  • 27
    • 0033199801 scopus 로고    scopus 로고
    • The best yeast?
    • S.L. Forsburg The best yeast? Trends Genet. 15 1999 340 344
    • (1999) Trends Genet. , vol.15 , pp. 340-344
    • Forsburg, S.L.1
  • 29
    • 34249765651 scopus 로고
    • NMRVIEW: A computer program for the visualization and analysis of NMR data
    • B.A. Johnson, and R.A. Blevins NMRVIEW: a computer program for the visualization and analysis of NMR data J. Biomol. NMR 4 1994 603 614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 30
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 31
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • P. Guntert Automated NMR structure calculation with CYANA Methods Mol. Biol. 278 2004 353 378
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Guntert, P.1
  • 33
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • T. Schwede, J. Kopp, N. Guex, and M.C. Peitsch SWISS-MODEL: an automated protein homology-modeling server Nucl. Acids Res. 31 2003 3381 3385
    • (2003) Nucl. Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 34
    • 8844265931 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of highly heterogeneous systems
    • B. Demeler, and K.E. van Holde Sedimentation velocity analysis of highly heterogeneous systems Anal. Biochem. 335 2004 279 288
    • (2004) Anal. Biochem. , vol.335 , pp. 279-288
    • Demeler, B.1    Van Holde, K.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.