메뉴 건너뛰기




Volumn 388, Issue 1, 2005, Pages 177-184

Interactions between Cdc42 and the scaffold protein Scd2: Requirement of SH3 domains for GTPase binding

Author keywords

Cell polarity; GTPase signalling; Phox homology domain (PX domain); Protein protein interaction; Src homology 3 domain (SH3 domain)

Indexed keywords

BINDING SITES; ISOTHERMAL TITRATION CALORIMETRY; NUCLEOTIDE-EXCHANGE FACTOR; PROTEIN-PROTEIN INTERACTIONS;

EID: 19544374273     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041838     Document Type: Article
Times cited : (17)

References (49)
  • 1
    • 0033007293 scopus 로고    scopus 로고
    • Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity
    • Johnson, D. I. (1999) Cdc42: an essential Rho-type GTPase controlling eukaryotic cell polarity. Microbiol. Mol. Biol. Rev. 63, 54-105
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 54-105
    • Johnson, D.I.1
  • 3
    • 2342432240 scopus 로고    scopus 로고
    • Cdc42 - The centre of polarity
    • Etienne-Manneville, S. (2004) Cdc42 - the centre of polarity. J. Cell Sci. 117, 1291-1300
    • (2004) J. Cell Sci. , vol.117 , pp. 1291-1300
    • Etienne-Manneville, S.1
  • 4
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M. S. and McCormick, F. (1993) Proteins regulating Ras and its relatives. Nature (London) 366, 643-654
    • (1993) Nature (London) , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 5
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang, S. R. (1997) G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 68, 639-678
    • (1997) Annu. Rev. Biochem. , vol.68 , pp. 639-678
    • Sprang, S.R.1
  • 6
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter, I. R. and Wittinghofer, A. (2001) The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 7
    • 0035195491 scopus 로고    scopus 로고
    • The Ste5p scaffold
    • Elion, E. A. (2001) The Ste5p scaffold. J. Cell Sci. 114, 3967-3978
    • (2001) J. Cell Sci. , vol.114 , pp. 3967-3978
    • Elion, E.A.1
  • 8
    • 0038554077 scopus 로고    scopus 로고
    • Biology of the p21-activated kinases
    • Bokoch, G. M. (2003) Biology of the p21-activated kinases. Annu. Rev. Biochem. 72, 743-781
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 743-781
    • Bokoch, G.M.1
  • 9
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T. and Nash, P. (2003) Assembly of cell regulatory systems through protein interaction domains. Science 300, 445-452
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 10
  • 11
    • 0042346345 scopus 로고    scopus 로고
    • Cell polarity: The ups and downs of the Par6/aPKC complex
    • Henrique, D. and Schweisguth, F. (2003) Cell polarity: the ups and downs of the Par6/aPKC complex. Curr. Opin. Genet. Dev. 13, 341-350
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 341-350
    • Henrique, D.1    Schweisguth, F.2
  • 12
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T. and Scott, J. D. (1997) Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075-2080
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 13
    • 0028052984 scopus 로고
    • Cdc42p GTPase is involved in controlling polarized cell growth in Schizosaccharomyces pombe
    • Miller, P. J. and Johnson, D. I. (1994) Cdc42p GTPase is involved in controlling polarized cell growth in Schizosaccharomyces pombe. Mol. Cell. Biol. 14, 1075-1083
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1075-1083
    • Miller, P.J.1    Johnson, D.I.2
  • 14
    • 0030474356 scopus 로고    scopus 로고
    • The highly conserved skb1 gene encodes a protein that interacts with Shk1, a fission yeast Ste20/PAK homolog
    • Gilbreth, M., Yang, P., Wang, D., Frost, J., Polverino, A., Cobb, M. H. and Marcus, S. (1996) The highly conserved skb1 gene encodes a protein that interacts with Shk1, a fission yeast Ste20/PAK homolog. Proc. Natl. Acad. Sci. U.S.A. 93, 13802-13807
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13802-13807
    • Gilbreth, M.1    Yang, P.2    Wang, D.3    Frost, J.4    Polverino, A.5    Cobb, M.H.6    Marcus, S.7
  • 15
    • 0033500151 scopus 로고    scopus 로고
    • Direct binding and in vivo regulation of the fission yeast p21-activated kinase shk1 by the SH3 domain protein scd2
    • Chang, E., Bartholomeusz, G., Pimental, R., Chen, J., Lai, H., Wang, L., Yang, P. and Marcus, S. (1999) Direct binding and in vivo regulation of the fission yeast p21-activated kinase shk1 by the SH3 domain protein scd2. Mol. Cell. Biol. 19, 8066-8074
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8066-8074
    • Chang, E.1    Bartholomeusz, G.2    Pimental, R.3    Chen, J.4    Lai, H.5    Wang, L.6    Yang, P.7    Marcus, S.8
  • 16
    • 0027937264 scopus 로고
    • Cooperative interaction of S. pombe proteins required for mating and morphogenesis
    • Chang, E. C., Barr, M., Wang, Y., Jung, V., Xu, H. P. and Wigler, M. H. (1994) Cooperative interaction of S. pombe proteins required for mating and morphogenesis. Cell 79, 131-141
    • (1994) Cell , vol.79 , pp. 131-141
    • Chang, E.C.1    Barr, M.2    Wang, Y.3    Jung, V.4    Xu, H.P.5    Wigler, M.H.6
  • 17
    • 0033579553 scopus 로고    scopus 로고
    • Direct activation of the fission yeast PAK Shk1 by the novel SH3 domain protein, Skb5
    • Yang, P., Pimental, R., Lai, H. and Marcus, S. (1999) Direct activation of the fission yeast PAK Shk1 by the novel SH3 domain protein, Skb5. J. Biol. Chem. 274, 36052-36057
    • (1999) J. Biol. Chem. , vol.274 , pp. 36052-36057
    • Yang, P.1    Pimental, R.2    Lai, H.3    Marcus, S.4
  • 18
    • 0035947081 scopus 로고    scopus 로고
    • Genetic and molecular characterization of Skb15, a highly conserved inhibitor of the fission yeast PAK
    • Kim, H. W., Yang, P., Qyang, Y., Lai, H., Du, H., Henkel, J. S., Kumar, K., Bao, S., Liu, M. and Marcus, S. (2001) Genetic and molecular characterization of Skb15, a highly conserved inhibitor of the fission yeast PAK, Shk1. Mol. Cell 7, 1095-1101
    • (2001) Shk1. Mol. Cell , vol.7 , pp. 1095-1101
    • Kim, H.W.1    Yang, P.2    Qyang, Y.3    Lai, H.4    Du, H.5    Henkel, J.S.6    Kumar, K.7    Bao, S.8    Liu, M.9    Marcus, S.10
  • 19
    • 0032907949 scopus 로고    scopus 로고
    • Genetic evidence for Pak1 autoinhibition and its release by Cdc42
    • Tu, H. and Wigler, M. (1999) Genetic evidence for Pak1 autoinhibition and its release by Cdc42. Mol. Cell. Biol. 19, 602-611
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 602-611
    • Tu, H.1    Wigler, M.2
  • 20
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • Lei, M., Lu, W., Meng, W., Parrini, M. C., Eck, M. J., Mayer, B. J. and Harrison, S. C. (2000) Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell 102, 387-397
    • (2000) Cell , vol.102 , pp. 387-397
    • Lei, M.1    Lu, W.2    Meng, W.3    Parrini, M.C.4    Eck, M.J.5    Mayer, B.J.6    Harrison, S.C.7
  • 21
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P. D., Drechsel, D. and Hall, A. (1995) A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270, 29071-29074
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 23
    • 0037428460 scopus 로고    scopus 로고
    • The Cdc42 binding and scaffolding activities of the fission yeast adaptor protein Scd2
    • Endo, M., Shirouzu, M. and Yokoyama, S. (2003) The Cdc42 binding and scaffolding activities of the fission yeast adaptor protein Scd2. J. Biol. Chem. 278, 843-852
    • (2003) J. Biol. Chem. , vol.278 , pp. 843-852
    • Endo, M.1    Shirouzu, M.2    Yokoyama, S.3
  • 24
    • 0035421216 scopus 로고    scopus 로고
    • Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions
    • Ito, T., Matsui, Y., Ago, T., Ota, K. and Sumimoto, H. (2001) Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions. EMBO J. 20, 3938-3946
    • (2001) EMBO J. , vol.20 , pp. 3938-3946
    • Ito, T.1    Matsui, Y.2    Ago, T.3    Ota, K.4    Sumimoto, H.5
  • 25
    • 0041625934 scopus 로고    scopus 로고
    • PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62
    • Wilson, M. I., Gill, D. J., Perisic, O., Quinn, M. T. and Williams, R. L. (2003) PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62. Mol. Cell 12, 39-50
    • (2003) Mol. Cell , vol.12 , pp. 39-50
    • Wilson, M.I.1    Gill, D.J.2    Perisic, O.3    Quinn, M.T.4    Williams, R.L.5
  • 26
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • Mayer, B. J. (2001) SH3 domains: complexity in moderation. J. Cell Sci. 114, 1253-1263
    • (2001) J. Cell Sci. , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 27
    • 0036420970 scopus 로고    scopus 로고
    • How SH3 domains recognize proline
    • Musacchio, A. (2002) How SH3 domains recognize proline. Adv. Protein Chem. 61, 211-268
    • (2002) Adv. Protein Chem. , vol.61 , pp. 211-268
    • Musacchio, A.1
  • 29
    • 0034944422 scopus 로고    scopus 로고
    • SNX3 regulates endosomal function through its PX-domain-mediated interaction with Ptdlns(3)P
    • Xu, Y., Hortsman, H., Seet, L., Wong, S. H. and Hong, W. (2001) SNX3 regulates endosomal function through its PX-domain-mediated interaction with Ptdlns(3)P. Nat. Cell Biol. 3, 658-666
    • (2001) Nat. Cell Biol. , vol.3 , pp. 658-666
    • Xu, Y.1    Hortsman, H.2    Seet, L.3    Wong, S.H.4    Hong, W.5
  • 31
    • 0034995037 scopus 로고    scopus 로고
    • Solution structure of the PX demain, a target of the SH3 domain
    • Hiroaki, H., Ago, T., Ito, T., Sumimoto, H. and Kohda, D. (2001) Solution structure of the PX demain, a target of the SH3 domain. Nat. Struct. Biol. 8, 526-530
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 526-530
    • Hiroaki, H.1    Ago, T.2    Ito, T.3    Sumimoto, H.4    Kohda, D.5
  • 33
    • 0037446850 scopus 로고    scopus 로고
    • Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation
    • Ago, T., Kuribayashi, F., Hiroaki, H., Takeya, R., Ito, T., Kohda, D. and Sumimoto, H. (2003) Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation. Proc. Natl. Acad. Sci. U.S.A. 100, 4474-4479
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4474-4479
    • Ago, T.1    Kuribayashi, F.2    Hiroaki, H.3    Takeya, R.4    Ito, T.5    Kohda, D.6    Sumimoto, H.7
  • 34
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping, Y., Lapouge, K., Smerdon, S. J. and Rittinger, K. (2003) Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell 113, 343-355
    • (2003) Cell , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, S.J.3    Rittinger, K.4
  • 35
    • 1842832382 scopus 로고    scopus 로고
    • Preparation of GTPases for structural and biophysical analysis
    • Smith, S. J. and Rittinger, K. (2002) Preparation of GTPases for structural and biophysical analysis. Methods Mol. Biol. 189, 13-24
    • (2002) Methods Mol. Biol. , vol.189 , pp. 13-24
    • Smith, S.J.1    Rittinger, K.2
  • 36
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J. F. and Lin, L. N. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131-137
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 37
    • 0034681424 scopus 로고    scopus 로고
    • R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras
    • Wang, B., Zou, J. X., Ek-Rylander, B. and Ruoslahti, E. (2000) R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras. J. Biol. Chem. 275, 5222-5227
    • (2000) J. Biol. Chem. , vol.275 , pp. 5222-5227
    • Wang, B.1    Zou, J.X.2    Ek-Rylander, B.3    Ruoslahti, E.4
  • 38
    • 0032572528 scopus 로고    scopus 로고
    • Regulation of sell polarity by microtubules in fission yeast
    • Sawin, K. E. and Nurse, P. (1998) Regulation of sell polarity by microtubules in fission yeast. J. Cell Biol. 142, 457-471
    • (1998) J. Cell Biol. , vol.142 , pp. 457-471
    • Sawin, K.E.1    Nurse, P.2
  • 40
    • 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
    • Liu Q., Berry, D., Nash, P., Pawson, T., McGlade, C. J. and Li, S. S. (2003) 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, 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
  • 46
    • 0344394312 scopus 로고    scopus 로고
    • Scaffold-mediated symmetry breaking by Cdc42p
    • Irazoqui, J. E., Gladfelter, A. S. and Lew, C. J. (2003) Scaffold-mediated symmetry breaking by Cdc42p. Nat. Cell Biol. 5, 1062-1070
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1062-1070
    • Irazoqui, J.E.1    Gladfelter, A.S.2    Lew, C.J.3
  • 47
    • 0037007225 scopus 로고    scopus 로고
    • A positive feedback loop stabilizes the guanine-nucleotide exchange factor Cdc24 at sites of polarization
    • Butty, A. C. Perrinjaquet, N., Petit, A., Jaquenoud, M., Segall, J. E., Hofmann, K., Zwahlen, C. and Peter, M. (2002) A positive feedback loop stabilizes the guanine-nucleotide exchange factor Cdc24 at sites of polarization. EMBO J. 21, 1565-1576
    • (2002) EMBO J. , vol.21 , pp. 1565-1576
    • Butty, A.C.1    Perrinjaquet, N.2    Petit, A.3    Jaquenoud, M.4    Segall, J.E.5    Hofmann, K.6    Zwahlen, C.7    Peter, M.8
  • 48
    • 0033635230 scopus 로고    scopus 로고
    • Phosphorylation of the Cdc42 exchange factor Cdc24 by the PAK-like kinase Cla4 may regulate polarized growth in yeast
    • Gulli, M. P., Jaquenoud, M., Shimada, Y., Niederhauser, G., Wiget, P. and Peter, M. (2000) Phosphorylation of the Cdc42 exchange factor Cdc24 by the PAK-like kinase Cla4 may regulate polarized growth in yeast. Mol. Cell 6, 1155-1167
    • (2000) Mol. Cell , vol.6 , pp. 1155-1167
    • Gulli, M.P.1    Jaquenoud, M.2    Shimada, Y.3    Niederhauser, G.4    Wiget, P.5    Peter, M.6
  • 49
    • 1842472163 scopus 로고    scopus 로고
    • The nucleotide exchange factor Cdc24p may be regulated by auto-inhibition
    • Shimada, Y., Wiget, P., Gulli, M. P., Bi, E. and Peter, M. (2004) The nucleotide exchange factor Cdc24p may be regulated by auto-inhibition. EMBO J. 23, 1051-1062
    • (2004) EMBO J. , vol.23 , pp. 1051-1062
    • Shimada, Y.1    Wiget, P.2    Gulli, M.P.3    Bi, E.4    Peter, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.