메뉴 건너뛰기




Volumn 355, Issue 4, 2006, Pages 651-663

Structural basis of syndecan-4 phosphorylation as a molecular switch to regulate signaling

Author keywords

NMR; Phosphatidylinositol 4, 5 bisphosphate; Phosphorylation; Solution structure; Syndecan 4

Indexed keywords

CARBON; DIMER; OLIGOMER; SERINE; SYNDECAN 4;

EID: 29144435969     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.09.087     Document Type: Article
Times cited : (65)

References (43)
  • 2
    • 0030660196 scopus 로고    scopus 로고
    • Syndecans: Multifunctional cell-surface co-receptors
    • D.J. Carey Syndecans: multifunctional cell-surface co-receptors Biochem. J. 327 1997 1 16
    • (1997) Biochem. J. , vol.327 , pp. 1-16
    • Carey, D.J.1
  • 3
    • 0032746544 scopus 로고    scopus 로고
    • Syndecan-4 and integrins: Combinatorial signaling in cell adhesion
    • J.R. Couchman, and A. Woods Syndecan-4 and integrins: combinatorial signaling in cell adhesion J. Cell Sci. 112 1999 3415 3420
    • (1999) J. Cell Sci. , vol.112 , pp. 3415-3420
    • Couchman, J.R.1    Woods, A.2
  • 4
    • 0028213641 scopus 로고
    • Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component
    • A. Woods, and J.R. Couchman Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component Mol. Biol. Cell 5 1994 183 192
    • (1994) Mol. Biol. Cell , vol.5 , pp. 183-192
    • Woods, A.1    Couchman, J.R.2
  • 5
    • 0027315260 scopus 로고
    • A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation
    • A. Woods, J.B. McCarthy, L.T. Furcht, and J.R. Couchman A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation Mol. Biol. Cell 4 1993 605 613
    • (1993) Mol. Biol. Cell , vol.4 , pp. 605-613
    • Woods, A.1    McCarthy, J.B.2    Furcht, L.T.3    Couchman, J.R.4
  • 6
    • 0033017955 scopus 로고    scopus 로고
    • Syndecan-4 signals cooperatively with integrins in a Rho-dependent manner in the assembly of focal adhesions and actin stress fibers
    • S. Saoncella, F. Echtermeyer, F. Denhez, J.K. Nowlen, D.F. Mosher, and S.D. Robinson Syndecan-4 signals cooperatively with integrins in a Rho-dependent manner in the assembly of focal adhesions and actin stress fibers Proc. Natl Acad. Sci. USA 96 1999 2805 2810
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2805-2810
    • Saoncella, S.1    Echtermeyer, F.2    Denhez, F.3    Nowlen, J.K.4    Mosher, D.F.5    Robinson, S.D.6
  • 8
    • 0032514263 scopus 로고    scopus 로고
    • Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    • Y.P. Hsueh, F.C. Yang, V. Kharazia, S. Naisbitt, A.R. Cohen, R.J. Weinberg, and M. Sheng Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses J. Cell Biol. 142 1998 139 151
    • (1998) J. Cell Biol. , vol.142 , pp. 139-151
    • Hsueh, Y.P.1    Yang, F.C.2    Kharazia, V.3    Naisbitt, S.4    Cohen, A.R.5    Weinberg, R.J.6    Sheng, M.7
  • 9
    • 0033869852 scopus 로고    scopus 로고
    • Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration
    • Y. Gao, M. Li, W. Chen, and M. Simons Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration J. Cell Physiol. 184 2000 373 379
    • (2000) J. Cell Physiol. , vol.184 , pp. 373-379
    • Gao, Y.1    Li, M.2    Chen, W.3    Simons, M.4
  • 10
    • 0034733733 scopus 로고    scopus 로고
    • Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin
    • J.J. Grootjans, G. Reekmans, H. Ceulemans, and G. David Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin J. Biol. Chem. 275 2000 19933 19941
    • (2000) J. Biol. Chem. , vol.275 , pp. 19933-19941
    • Grootjans, J.J.1    Reekmans, G.2    Ceulemans, H.3    David, G.4
  • 11
    • 0035157574 scopus 로고    scopus 로고
    • Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments
    • P. Zimmerman, D. Tomatis, M. Rosas, J. Grootjans, I. Leenarts, and G. Degeest Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments Mol. Biol. Cell 12 2001 339 350
    • (2001) Mol. Biol. Cell , vol.12 , pp. 339-350
    • Zimmerman, P.1    Tomatis, D.2    Rosas, M.3    Grootjans, J.4    Leenarts, I.5    Degeest, G.6
  • 12
    • 0030889054 scopus 로고    scopus 로고
    • Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C
    • E.S. Oh, A. Woods, and J.R. Couchman Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C J. Biol. Chem. 272 1997 8133 8136
    • (1997) J. Biol. Chem. , vol.272 , pp. 8133-8136
    • Oh, E.S.1    Woods, A.2    Couchman, J.R.3
  • 13
    • 0032562706 scopus 로고    scopus 로고
    • Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity
    • E.S. Oh, A. Woods, S.T. Lim, A. Theibert, and J.R. Couchman Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity J. Biol. Chem. 273 1998 10624 10629
    • (1998) J. Biol. Chem. , vol.273 , pp. 10624-10629
    • Oh, E.S.1    Woods, A.2    Lim, S.T.3    Theibert, A.4    Couchman, J.R.5
  • 14
    • 0032557438 scopus 로고    scopus 로고
    • Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate
    • D. Lee, E.S. Oh, A. Woods, J.R. Couchman, and W. Lee Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate J. Biol. Chem. 273 1998 13022 13029
    • (1998) J. Biol. Chem. , vol.273 , pp. 13022-13029
    • Lee, D.1    Oh, E.S.2    Woods, A.3    Couchman, J.R.4    Lee, W.5
  • 15
    • 0037147206 scopus 로고    scopus 로고
    • Regulation of inositol phospholipid binding and signaling through syndecan-4
    • J.R. Couchman, S. Vogt, S.-T. Lim, Y. Lim, E.-S. Oh, and G.D. Prestwich Regulation of inositol phospholipid binding and signaling through syndecan-4 J. Biol. Chem. 277 2002 49296 49303
    • (2002) J. Biol. Chem. , vol.277 , pp. 49296-49303
    • Couchman, J.R.1    Vogt, S.2    Lim, S.-T.3    Lim, Y.4    Oh, E.-S.5    Prestwich, G.D.6
  • 16
    • 0037515626 scopus 로고    scopus 로고
    • Direct binding of syndecan-4 cytoplasmic domain to the catalytic domain of protein kinase C alpha (PKC alpha) increases focal adhesion localization of PKC alpha
    • S.T. Lim, R.L. Langley, J.R. Couchman, and A. Woods Direct binding of syndecan-4 cytoplasmic domain to the catalytic domain of protein kinase C alpha (PKC alpha) increases focal adhesion localization of PKC alpha J. Biol. Chem. 278 2003 13795 13802
    • (2003) J. Biol. Chem. , vol.278 , pp. 13795-13802
    • Lim, S.T.1    Langley, R.L.2    Couchman, J.R.3    Woods, A.4
  • 17
    • 0028880289 scopus 로고
    • Protein kinase C regulates the recruitment of syndecan-4 into focal contacts
    • P.C. Baciu, and P.F. Goetinck Protein kinase C regulates the recruitment of syndecan-4 into focal contacts Mol. Biol. Cell 6 1995 1503 1513
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1503-1513
    • Baciu, P.C.1    Goetinck, P.F.2
  • 18
    • 0026603414 scopus 로고
    • Protein kinase C involvement in focal adhesion formation
    • A. Woods, and J.R. Couchman Protein kinase C involvement in focal adhesion formation J. Cell Sci. 101 1992 277 290
    • (1992) J. Cell Sci. , vol.101 , pp. 277-290
    • Woods, A.1    Couchman, J.R.2
  • 20
  • 21
    • 0030911243 scopus 로고    scopus 로고
    • Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C
    • E.S. Oh, A. Woods, and J.R. Couchman Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C J. Biol. Chem. 272 1997 11805 11811
    • (1997) J. Biol. Chem. , vol.272 , pp. 11805-11811
    • Oh, E.S.1    Woods, A.2    Couchman, J.R.3
  • 22
    • 0028842497 scopus 로고
    • Self-association of N-syndecan (Syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region
    • V.K. Asundi, and D.J. Carey Self-association of N-syndecan (Syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region J. Biol. Chem. 270 1995 26404 26410
    • (1995) J. Biol. Chem. , vol.270 , pp. 26404-26410
    • Asundi, V.K.1    Carey, D.J.2
  • 23
    • 0026742962 scopus 로고
    • Molecular cloning of the major cell surface heparan sulfate proteoglycan from rat liver
    • A. Pierce, M. Lyon, I.N. Hampson, G.J. Cowling, and J. Gallagher Molecular cloning of the major cell surface heparan sulfate proteoglycan from rat liver J. Biol. Chem. 267 1992 3894 3900
    • (1992) J. Biol. Chem. , vol.267 , pp. 3894-3900
    • Pierce, A.1    Lyon, M.2    Hampson, I.N.3    Cowling, G.J.4    Gallagher, J.5
  • 24
    • 0035942994 scopus 로고    scopus 로고
    • Solution structure of the dimeric cytoplasmic domain of syndecan-4
    • J. Shin, W. Lee, D. Lee, B.K. Koo, Y. Lim, and A. Woods Solution structure of the dimeric cytoplasmic domain of syndecan-4 Biochemistry 40 2001 8471 8478
    • (2001) Biochemistry , vol.40 , pp. 8471-8478
    • Shin, J.1    Lee, W.2    Lee, D.3    Koo, B.K.4    Lim, Y.5    Woods, A.6
  • 25
    • 0032080332 scopus 로고    scopus 로고
    • Regulation of syndecan-4 phosphorylation in vivo
    • A. Horowitz, and M. Simons Regulation of syndecan-4 phosphorylation in vivo J. Biol. Chem. 273 1998 10914 10918
    • (1998) J. Biol. Chem. , vol.273 , pp. 10914-10918
    • Horowitz, A.1    Simons, M.2
  • 26
    • 0032475975 scopus 로고    scopus 로고
    • Phosphorylation of the cytoplasmic tail of syndecan-4 regulates activation of protein kinase Cα
    • A. Horowitz, and M. Simons Phosphorylation of the cytoplasmic tail of syndecan-4 regulates activation of protein kinase Cα J. Biol. Chem. 273 1998 25548 25551
    • (1998) J. Biol. Chem. , vol.273 , pp. 25548-25551
    • Horowitz, A.1    Simons, M.2
  • 28
    • 0023268552 scopus 로고
    • A proton and carbon 13 nuclear magnetic resonance study of neomycin B and its interactions with phosphatidylinositol 4,5-bisphosphate
    • D.G. Reid, and K. Gajjar A proton and carbon 13 nuclear magnetic resonance study of neomycin B and its interactions with phosphatidylinositol 4,5-bisphosphate J. Biol. Chem. 262 1987 7967 7972
    • (1987) J. Biol. Chem. , vol.262 , pp. 7967-7972
    • Reid, D.G.1    Gajjar, K.2
  • 30
    • 0033619730 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-bisphosphate mediates the interaction of syndecan-4 with protein kinase C
    • A. Horowitz, M. Murakami, Y. Gao, and M. Simons Phosphatidylinositol-4,5- bisphosphate mediates the interaction of syndecan-4 with protein kinase C Biochemistry 38 1999 15871 15877
    • (1999) Biochemistry , vol.38 , pp. 15871-15877
    • Horowitz, A.1    Murakami, M.2    Gao, Y.3    Simons, M.4
  • 31
    • 0037113167 scopus 로고    scopus 로고
    • Cytoplasmic interactions of syndecan-4 orchestrate adhesion receptor and growth factor receptor signalling
    • M.D. Bass, and M.J. Humphries Cytoplasmic interactions of syndecan-4 orchestrate adhesion receptor and growth factor receptor signalling Biochem. J. 368 2002 1 15
    • (2002) Biochem. J. , vol.368 , pp. 1-15
    • Bass, M.D.1    Humphries, M.J.2
  • 32
    • 0031452282 scopus 로고    scopus 로고
    • Lack of coupling between secondary structure formation and collapse in a model polypeptide that mimics early folding intermediates, the F(2) fragment of the Escherichia coli tryptophan-synthase {beta} chain
    • K. Gast, A.F. Chaffotte, D. Zirwer, Y. Guillou, M. Mueller-Frohne, and C. Cadieux Lack of coupling between secondary structure formation and collapse in a model polypeptide that mimics early folding intermediates, the F(2) fragment of the Escherichia coli tryptophan-synthase {beta} chain Protein Sci. 6 1997 2578 2588
    • (1997) Protein Sci. , vol.6 , pp. 2578-2588
    • Gast, K.1    Chaffotte, A.F.2    Zirwer, D.3    Guillou, Y.4    Mueller-Frohne, M.5    Cadieux, C.6
  • 34
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • A. Bax, and D.G. Davis MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy J. Magn. Reson. 65 1985 355 360
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 35
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance
    • K. Wuthrich, M. Billeter, and W. Braun Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance J. Mol. Biol. 169 1983 949 961
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wuthrich, K.1    Billeter, M.2    Braun, W.3
  • 36
    • 46149136737 scopus 로고
    • Origin of t1 and t2 ridges in 2D NMR spectra and procedures for suppression
    • G. Otting, H. Widmer, G. Wagner, and K. Wuthrich Origin of t1 and t2 ridges in 2D NMR spectra and procedures for suppression J. Magn. Reson. 66 1986 187 193
    • (1986) J. Magn. Reson. , vol.66 , pp. 187-193
    • Otting, G.1    Widmer, H.2    Wagner, G.3    Wuthrich, K.4
  • 38
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations
    • M. Nilges, G.M. Clore, and A.M. Gronenborn Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations FEBS Letters 229 1988 317 324
    • (1988) FEBS Letters , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 39
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms circumventing problems associated with folding
    • M. Nilges, G.M. Clore, and A.M. Gronenborn Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms circumventing problems associated with folding FEBS Letters 239 1988 129 136
    • (1988) FEBS Letters , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 40
    • 0023998438 scopus 로고
    • Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2
    • M. Nilges, A.M. Gronenborn, A.T. Brunger, and G.M. Clore Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2 Protein Eng. 2 1988 27 38
    • (1988) Protein Eng. , vol.2 , pp. 27-38
    • Nilges, M.1    Gronenborn, A.M.2    Brunger, A.T.3    Clore, G.M.4
  • 41
    • 0027383637 scopus 로고
    • A calculation strategy for the structure determination of symmetric dimers by 1H NMR
    • M. Nilges A calculation strategy for the structure determination of symmetric dimers by 1H NMR Proteins: Struct. Funct. Genet. 17 1993 297 309
    • (1993) Proteins: Struct. Funct. Genet. , vol.17 , pp. 297-309
    • Nilges, M.1
  • 43
    • 0024595937 scopus 로고
    • Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • P.C. Driscoll, A.M. Gronenborn, L. Beress, and G.M. Clore Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing Biochemistry 28 1989 2188 2198
    • (1989) Biochemistry , vol.28 , pp. 2188-2198
    • Driscoll, P.C.1    Gronenborn, A.M.2    Beress, L.3    Clore, G.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.