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Volumn 377, Issue 3, 2008, Pages 889-901

Recognition of Non-canonical Peptides by the Yeast Fus1p SH3 Domain: Elucidation of a Common Mechanism for Diverse SH3 Domain Specificities

Author keywords

Fus1p; non canonical peptide recognition; protein interaction module; SH3 domain; SH3 domain specificity

Indexed keywords

FUNGAL PROTEIN; PROTEIN FUS1P; PROTEIN SH3; UNCLASSIFIED DRUG;

EID: 40649118186     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.063     Document Type: Article
Times cited : (27)

References (43)
  • 1
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction
    • S.S. Li Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction Biochem. J. 390 2005 641 653
    • (2005) Biochem. J. , vol.390 , pp. 641-653
    • Li, S.S.1
  • 2
    • 0013033597 scopus 로고    scopus 로고
    • The structure and function of proline recognition domains
    • A. Zarrinpar R.P. Bhattacharyya W.A. Lim The structure and function of proline recognition domains Sci. STKE 2003 2003 RE8
    • (2003) Sci. STKE , vol.2003 , pp. RE8
    • Zarrinpar, A.1    Bhattacharyya, R.P.2    Lim, W.A.3
  • 3
    • 0034714554 scopus 로고    scopus 로고
    • Convergent evolution with combinatorial peptides
    • B.K. Kay J. Kasanov S. Knight A. Kurakin Convergent evolution with combinatorial peptides FEBS Lett. 480 2000 55 62
    • (2000) FEBS Lett. , vol.480 , pp. 55-62
    • Kay, B.K.1    Kasanov, J.2    Knight, S.3    Kurakin, A.4
  • 4
    • 0037059461 scopus 로고    scopus 로고
    • A combined experimental and computational strategy to define pro-tein interaction networks for peptide recognition modules
    • A.H. Tong B. Drees G. Nardelli G.D. Bader B. Brannetti L. Castagnoli A combined experimental and computational strategy to define pro-tein interaction networks for peptide recognition modules Science 295 2002 321 324
    • (2002) Science , vol.295 , pp. 321-324
    • Tong, A.H.1    Drees, B.2    Nardelli, G.3    Bader, G.D.4    Brannetti, B.5    Castagnoli, L.6
  • 5
    • 2942648435 scopus 로고    scopus 로고
    • Protein–protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast
    • J.A. Marles S. Dahesh J. Haynes B.J. Andrews A.R. Davidson Protein–protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast Mol. Cell 14 2004 813 823
    • (2004) Mol. Cell , vol.14 , pp. 813-823
    • Marles, J.A.1    Dahesh, S.2    Haynes, J.3    Andrews, B.J.4    Davidson, A.R.5
  • 6
    • 0346555269 scopus 로고    scopus 로고
    • Optimization of specificity in a cellular protein interaction network by negative selection
    • A. Zarrinpar S.H. Park W.A. Lim Optimization of specificity in a cellular protein interaction network by negative selection Nature 426 2003 676 680
    • (2003) Nature , vol.426 , pp. 676-680
    • Zarrinpar, A.1    Park, S.H.2    Lim, W.A.3
  • 7
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • T. Pawson Protein modules and signalling networks Nature 373 1995 573 580
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 8
    • 0034486070 scopus 로고    scopus 로고
    • The identification of conserved interactions within the SH3 domain by alignment of sequences and structures
    • S.M. Larson A.R. Davidson The identification of conserved interactions within the SH3 domain by alignment of sequences and structures Protein Sci. 9 2000 2170 2180
    • (2000) Protein Sci. , vol.9 , pp. 2170-2180
    • Larson, S.M.1    Davidson, A.R.2
  • 9
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • W.A. Lim F.M. Richards R.O. Fox Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains Nature 372 1994 375 379
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 10
    • 0036420970 scopus 로고    scopus 로고
    • How SH3 domains recognize proline
    • A. Musacchio How SH3 domains recognize proline Adv. Protein Chem. 61 2002 211 268
    • (2002) Adv. Protein Chem. , vol.61 , pp. 211-268
    • Musacchio, A.1
  • 11
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3–ligand interactions
    • S. Feng J.K. Chen H. Yu J.A. Simon S.L. Schreiber Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3–ligand interactions Science 266 1994 1241 1247
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 12
    • 25844525760 scopus 로고    scopus 로고
    • Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity
    • F. Bauer K. Schweimer H. Meiselbach S. Hoffmann P. Rosch H. Sticht Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity Protein Sci. 14 2005 2487 2498
    • (2005) Protein Sci. , vol.14 , pp. 2487-2498
    • Bauer, F.1    Schweimer, K.2    Meiselbach, H.3    Hoffmann, S.4    Rosch, P.5    Sticht, H.6
  • 13
    • 0347627529 scopus 로고    scopus 로고
    • The tryptophan switch: changing ligand-binding specificity from type I to type II in SH3 domains
    • G. Fernandez-Ballester C. Blanes-Mira L. Serrano The tryptophan switch: changing ligand-binding specificity from type I to type II in SH3 domains J. Mol. Biol. 335 2004 619 629
    • (2004) J. Mol. Biol. , vol.335 , pp. 619-629
    • Fernandez-Ballester, G.1    Blanes-Mira, C.2    Serrano, L.3
  • 14
    • 0029589911 scopus 로고
    • Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands
    • S. Feng C. Kasahara R.J. Rickles S.L. Schreiber Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands Proc. Natl Acad. Sci. USA 92 1995 12408 12415
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 12408-12415
    • Feng, S.1    Kasahara, C.2    Rickles, R.J.3    Schreiber, S.L.4
  • 16
    • 0029959928 scopus 로고    scopus 로고
    • Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2
    • A.B. Sparks J.E. Rider N.G. Hoffman D.M. Fowlkes L.A. Quillam B.K. Kay Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2 Proc. Natl Acad. Sci. USA 93 1996 1540 1544
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1540-1544
    • Sparks, A.B.1    Rider, J.E.2    Hoffman, N.G.3    Fowlkes, D.M.4    Quillam, L.A.5    Kay, B.K.6
  • 17
    • 0034753803 scopus 로고    scopus 로고
    • A novel, specific interaction involving the Csk SH3 domain and its natural ligand
    • R. Ghose A. Shekhtman M.J. Goger H. Ji D. Cowburn A novel, specific interaction involving the Csk SH3 domain and its natural ligand Nat. Struct. Biol. 8 2001 998 1004
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 998-1004
    • Ghose, R.1    Shekhtman, A.2    Goger, M.J.3    Ji, H.4    Cowburn, D.5
  • 18
    • 0037102138 scopus 로고    scopus 로고
    • Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p
    • K. Kami R. Takeya H. Sumimoto D. Kohda Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p EMBO J. 21 2002 4268 4276
    • (2002) EMBO J. , vol.21 , pp. 4268-4276
    • Kami, K.1    Takeya, R.2    Sumimoto, H.3    Kohda, D.4
  • 19
    • 33645641343 scopus 로고    scopus 로고
    • NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide
    • K. Ogura I. Nobuhisa S. Yuzawa R. Takeya S. Torikai K. Saikawa NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide J. Biol. Chem. 281 2006 3660 3668
    • (2006) J. Biol. Chem. , vol.281 , pp. 3660-3668
    • Ogura, K.1    Nobuhisa, I.2    Yuzawa, S.3    Takeya, R.4    Torikai, S.5    Saikawa, K.6
  • 21
    • 33646114301 scopus 로고    scopus 로고
    • Crystal structure of the SH3 domain of betaPIX in complex with a high affinity peptide from PAK2
    • A. Hoelz J.M. Janz S.D. Lawrie B. Corwin A. Lee T.P. Sakmar Crystal structure of the SH3 domain of betaPIX in complex with a high affinity peptide from PAK2 J. Mol. Biol. 358 2006 509 522
    • (2006) J. Mol. Biol. , vol.358 , pp. 509-522
    • Hoelz, A.1    Janz, J.M.2    Lawrie, S.D.3    Corwin, B.4    Lee, A.5    Sakmar, T.P.6
  • 22
    • 0346850829 scopus 로고    scopus 로고
    • Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain
    • T. Kaneko T. Kumasaka T. Ganbe T. Sato K. Miyazawa N. Kitamura N. Tanaka Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain J. Biol. Chem. 278 2003 48162 48168
    • (2003) J. Biol. Chem. , vol.278 , pp. 48162-48168
    • Kaneko, T.1    Kumasaka, T.2    Ganbe, T.3    Sato, T.4    Miyazawa, K.5    Kitamura, N.6    Tanaka, N.7
  • 23
    • 0034659759 scopus 로고    scopus 로고
    • SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55
    • H. Kang C. Freund J.S. Duke-Cohan A. Musacchio G. Wagner C.E. Rudd SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55 EMBO J. 19 2000 2889 2899
    • (2000) EMBO J. , vol.19 , pp. 2889-2899
    • Kang, H.1    Freund, C.2    Duke-Cohan, J.S.3    Musacchio, A.4    Wagner, G.5    Rudd, C.E.6
  • 24
    • 33846962112 scopus 로고    scopus 로고
    • Efficient T-cell receptor signaling requires a high-affinity interaction between the Gads C-SH3 domain and the SLP-76 RxxK motif
    • B.T. Seet D.M. Berry J.S. Maltzman J. Shabason M. Raina G.A. Koretzky Efficient T-cell receptor signaling requires a high-affinity interaction between the Gads C-SH3 domain and the SLP-76 RxxK motif EMBO J. 26 2007 678 689
    • (2007) EMBO J. , vol.26 , pp. 678-689
    • Seet, B.T.1    Berry, D.M.2    Maltzman, J.S.3    Shabason, J.4    Raina, M.5    Koretzky, G.A.6
  • 25
    • 0037291960 scopus 로고    scopus 로고
    • Structural basis for specific binding of the Gads SH3 domain to an RxxK motif-containing SLP-76 peptide: a novel mode of peptide recognition
    • Q. Liu D. Berry P. Nash T. Pawson C.J. McGlade S.S. Li Structural basis for specific binding of the Gads SH3 domain to an RxxK motif-containing SLP-76 peptide: a novel mode of peptide recognition Mol. Cell 11 2003 471 481
    • (2003) Mol. Cell , vol.11 , pp. 471-481
    • Liu, Q.1    Berry, D.2    Nash, P.3    Pawson, T.4    McGlade, C.J.5    Li, S.S.6
  • 27
    • 3142651452 scopus 로고    scopus 로고
    • Mona/Gads SH3C binding to hematopoietic progenitor kinase 1 (HPK1) combines an atypical SH3 binding motif, R/KXXK, with a classical PXXP motif embedded in a polyproline type II (PPII) helix
    • M. Lewitzky M. Harkiolaki M.C. Domart E.Y. Jones S.M. Feller Mona/Gads SH3C binding to hematopoietic progenitor kinase 1 (HPK1) combines an atypical SH3 binding motif, R/KXXK, with a classical PXXP motif embedded in a polyproline type II (PPII) helix J. Biol. Chem. 279 2004 28724 28732
    • (2004) J. Biol. Chem. , vol.279 , pp. 28724-28732
    • Lewitzky, M.1    Harkiolaki, M.2    Domart, M.C.3    Jones, E.Y.4    Feller, S.M.5
  • 29
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • S. Gorina N.P. Pavletich Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2 Science 274 1996 1001 1005
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 30
    • 1642268294 scopus 로고    scopus 로고
    • Fus1p interacts with components of the Hog1p mitogen-activated protein kinase and Cdc42p morphogenesis signaling pathways to control cell fusion during yeast mating
    • B. Nelson A.B. Parsons M. Evangelista K. Schaefer K. Kennedy S. Ritchie Fus1p interacts with components of the Hog1p mitogen-activated protein kinase and Cdc42p morphogenesis signaling pathways to control cell fusion during yeast mating Genetics 166 2004 67 77
    • (2004) Genetics , vol.166 , pp. 67-77
    • Nelson, B.1    Parsons, A.B.2    Evangelista, M.3    Schaefer, K.4    Kennedy, K.5    Ritchie, S.6
  • 31
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • A. Musacchio M. Saraste M. Wilmanns High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides Nat. Struct. Biol. 1 1994 546 551
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 33
    • 0031782969 scopus 로고    scopus 로고
    • Cell polarity and morphogenesis in budding yeast
    • K. Madden M. Snyder Cell polarity and morphogenesis in budding yeast Annu. Rev. Microbiol. 52 1998 687 744
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 687-744
    • Madden, K.1    Snyder, M.2
  • 34
    • 0038445654 scopus 로고    scopus 로고
    • Formins: signaling effectors for assembly and polarization of actin filaments
    • M. Evangelista S. Zigmond C. Boone Formins: signaling effectors for assembly and polarization of actin filaments J. Cell Sci. 116 2003 2603 2611
    • (2003) J. Cell Sci. , vol.116 , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 35
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • E.G. Hutchinson J.M. Thornton A revised set of potentials for beta-turn formation in proteins Protein Sci. 3 1994 2207 2216
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 36
    • 35349012607 scopus 로고    scopus 로고
    • A novel interaction between atrophin-interacting protein 4 and beta-p21-activated kinase-interactive exchange factor is mediated by an SH3 domain
    • J.M. Janz T.P. Sakmar K.C. Min A novel interaction between atrophin-interacting protein 4 and beta-p21-activated kinase-interactive exchange factor is mediated by an SH3 domain J. Biol. Chem. 282 2007 28893 28903
    • (2007) J. Biol. Chem. , vol.282 , pp. 28893-28903
    • Janz, J.M.1    Sakmar, T.P.2    Min, K.C.3
  • 37
    • 29344434301 scopus 로고    scopus 로고
    • Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain
    • A. Zarrine-Afsar A. Mittermaier L.E. Kay A.R. Davidson Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain Protein Sci. 15 2006 162 170
    • (2006) Protein Sci. , vol.15 , pp. 162-170
    • Zarrine-Afsar, A.1    Mittermaier, A.2    Kay, L.E.3    Davidson, A.R.4
  • 39
    • 0034383397 scopus 로고    scopus 로고
    • The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction
    • P. Barnett G. Bottger A.T. Klein H.F. Tabak B. Distel The peroxisomal membrane protein Pex13p shows a novel mode of SH3 interaction EMBO J. 19 2000 6382 6391
    • (2000) EMBO J. , vol.19 , pp. 6382-6391
    • Barnett, P.1    Bottger, G.2    Klein, A.T.3    Tabak, H.F.4    Distel, B.5
  • 40
    • 34548564106 scopus 로고    scopus 로고
    • Structural basis for ubiquitin recognition by SH3 domains
    • Y. He L. Hicke I. Radhakrishnan Structural basis for ubiquitin recognition by SH3 domains J. Mol. Biol. 373 2007 190 196
    • (2007) J. Mol. Biol. , vol.373 , pp. 190-196
    • He, Y.1    Hicke, L.2    Radhakrishnan, I.3
  • 41
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
    • C.H. Lee K. Saksela U.A. Mirza B.T. Chait J. Kuriyan Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain Cell 85 1996 931 942
    • (1996) Cell , vol.85 , pp. 931-942
    • Lee, C.H.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 42
    • 0032542018 scopus 로고    scopus 로고
    • Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects
    • K.L. Maxwell A.R. Davidson Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects Biochemistry 37 1998 16172 16182
    • (1998) Biochemistry , vol.37 , pp. 16172-16182
    • Maxwell, K.L.1    Davidson, A.R.2
  • 43
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • C.N. Pace F. Vajdos L. Fee G. Grimsley T. Gray How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4 1995 2411 2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5


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