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Volumn 422, Issue 5, 2012, Pages 697-704

The metavinculin tail domain directs constitutive interactions with raver1 and vinculin RNA

Author keywords

adherens junction; cardiomyopathy; focal adhesion; RNA binding; RRM domain

Indexed keywords

MEMBRANE PROTEIN; MESSENGER RNA; PHOSPHOLIPID; PROTEIN METAVINCULIN; PROTEIN RAVER1; RNA BINDING PROTEIN; UNCLASSIFIED DRUG; VINCULIN;

EID: 84865684426     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.06.015     Document Type: Article
Times cited : (6)

References (44)
  • 1
    • 0018692430 scopus 로고
    • A 130K protein from chicken gizzard: Its localization at the termini of microfilament bundles in cultured chicken cells
    • B. Geiger A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells Cell 18 1979 193 205
    • (1979) Cell , vol.18 , pp. 193-205
    • Geiger, B.1
  • 2
    • 0019568618 scopus 로고
    • Interaction of α-actinin and vinculin with actin: Opposite effects on filament network formation
    • B.M. Jockusch, and G. Isenberg Interaction of α-actinin and vinculin with actin: opposite effects on filament network formation Proc. Natl Acad. Sci. USA 78 1981 3005 3009
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 3005-3009
    • Jockusch, B.M.1    Isenberg, G.2
  • 3
    • 0020082249 scopus 로고
    • High-affinity interaction of vinculin with actin filaments in vitro
    • J.A. Wilkins, and S. Lin High-affinity interaction of vinculin with actin filaments in vitro Cell 28 1982 83 90
    • (1982) Cell , vol.28 , pp. 83-90
    • Wilkins, J.A.1    Lin, S.2
  • 4
    • 0010935732 scopus 로고
    • A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements (costameres) mark sites of attachment between myofibrils and sarcolemma
    • J.V. Pardo, J.D. Siliciano, and S.W. Craig A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements (costameres) mark sites of attachment between myofibrils and sarcolemma Proc. Natl Acad. Sci. USA 80 1983 1008 1012
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 1008-1012
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 5
    • 0023770986 scopus 로고
    • Immunolocalization of meta-vinculin in human smooth and cardiac muscles
    • A.M. Belkin, O.I. Ornatsky, M.A. Glukhova, and V.E. Koteliansky Immunolocalization of meta-vinculin in human smooth and cardiac muscles J. Cell Biol. 107 1988 545 553
    • (1988) J. Cell Biol. , vol.107 , pp. 545-553
    • Belkin, A.M.1    Ornatsky, O.I.2    Glukhova, M.A.3    Koteliansky, V.E.4
  • 6
    • 0024064403 scopus 로고
    • Porcine vinculin and metavinculin differ by a 68-residue insert located close to the carboxy-terminal part of the molecule
    • M. Gimona, J.V. Small, M. Moeremans, J. Van Damme, M. Puype, and J. Vandekerckhove Porcine vinculin and metavinculin differ by a 68-residue insert located close to the carboxy-terminal part of the molecule EMBO J. 7 1988 2329 2334
    • (1988) EMBO J. , vol.7 , pp. 2329-2334
    • Gimona, M.1    Small, J.V.2    Moeremans, M.3    Van Damme, J.4    Puype, M.5    Vandekerckhove, J.6
  • 7
    • 3843052495 scopus 로고    scopus 로고
    • Comparative biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites
    • S. Witt, A. Zieseniss, U. Fock, B.M. Jockusch, and S. Illenberger Comparative biochemical analysis suggests that vinculin and metavinculin cooperate in muscular adhesion sites J. Biol. Chem. 279 2004 31533 31543
    • (2004) J. Biol. Chem. , vol.279 , pp. 31533-31543
    • Witt, S.1    Zieseniss, A.2    Fock, U.3    Jockusch, B.M.4    Illenberger, S.5
  • 8
    • 0031034388 scopus 로고    scopus 로고
    • Dilated cardiomyopathy associated with deficiency of the cytoskeletal protein metavinculin
    • M. Maeda, E. Holder, B. Lowes, S. Valent, and R.D. Bies Dilated cardiomyopathy associated with deficiency of the cytoskeletal protein metavinculin Circulation 95 1997 17 20
    • (1997) Circulation , vol.95 , pp. 17-20
    • Maeda, M.1    Holder, E.2    Lowes, B.3    Valent, S.4    Bies, R.D.5
  • 10
    • 32044458438 scopus 로고    scopus 로고
    • Identification of a metavinculin missense mutation, R975W, associated with both hypertrophic and dilated cardiomyopathy
    • V.C. Vasile, M.L. Will, S.R. Ommen, W.D. Edwards, T.M. Olson, and M.J. Ackerman Identification of a metavinculin missense mutation, R975W, associated with both hypertrophic and dilated cardiomyopathy Mol. Genet. Metab. 87 2006 169 174
    • (2006) Mol. Genet. Metab. , vol.87 , pp. 169-174
    • Vasile, V.C.1    Will, M.L.2    Ommen, S.R.3    Edwards, W.D.4    Olson, T.M.5    Ackerman, M.J.6
  • 13
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • R.P. Johnson, and S.W. Craig An intramolecular association between the head and tail domains of vinculin modulates talin binding J. Biol. Chem. 269 1994 12611 12619
    • (1994) J. Biol. Chem. , vol.269 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 15
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • R.P. Johnson, and S.W. Craig F-actin binding site masked by the intramolecular association of vinculin head and tail domains Nature 373 1995 261 264
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 16
    • 0029761645 scopus 로고    scopus 로고
    • The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin
    • N.P. Brindle, M.R. Holt, J.E. Davies, C.J. Price, and D.R. Critchley The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin Biochem. J. 318 1996 753 757
    • (1996) Biochem. J. , vol.318 , pp. 753-757
    • Brindle, N.P.1    Holt, M.R.2    Davies, J.E.3    Price, C.J.4    Critchley, D.R.5
  • 17
    • 15644363085 scopus 로고    scopus 로고
    • α-Catenin-vinculin interaction functions to organize the apical junctional complex in epithelial cells
    • M. Watabe-Uchida, N. Uchida, Y. Imamura, A. Nagafuchi, K. Fujimoto, and T. Uemura α-Catenin-vinculin interaction functions to organize the apical junctional complex in epithelial cells J. Cell Biol. 142 1998 847 857
    • (1998) J. Cell Biol. , vol.142 , pp. 847-857
    • Watabe-Uchida, M.1    Uchida, N.2    Imamura, Y.3    Nagafuchi, A.4    Fujimoto, K.5    Uemura, T.6
  • 18
    • 0033545092 scopus 로고    scopus 로고
    • Vinexin: A novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organization
    • N. Kioka, S. Sakata, T. Kawauchi, T. Amachi, S.K. Akiyama, and K. Okazaki Vinexin: a novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organization J. Cell Biol. 144 1999 59 69
    • (1999) J. Cell Biol. , vol.144 , pp. 59-69
    • Kioka, N.1    Sakata, S.2    Kawauchi, T.3    Amachi, T.4    Akiyama, S.K.5    Okazaki, K.6
  • 19
    • 3042600016 scopus 로고    scopus 로고
    • Structural basis for amplifying vinculin activation by talin
    • T. Izard, and C. Vonrhein Structural basis for amplifying vinculin activation by talin J. Biol. Chem. 279 2004 27667 27678
    • (2004) J. Biol. Chem. , vol.279 , pp. 27667-27678
    • Izard, T.1    Vonrhein, C.2
  • 20
    • 21744441321 scopus 로고    scopus 로고
    • Structural dynamics of α-actinin-vinculin interactions
    • P.R. Bois, R.A. Borgon, C. Vonrhein, and T. Izard Structural dynamics of α-actinin-vinculin interactions Mol. Cell. Biol. 25 2005 6112 6122
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6112-6122
    • Bois, P.R.1    Borgon, R.A.2    Vonrhein, C.3    Izard, T.4
  • 21
    • 33646368402 scopus 로고    scopus 로고
    • The vinculin binding sites of talin and α-actinin are sufficient to activate vinculin
    • P.R. Bois, B.P. O'Hara, D. Nietlispach, J. Kirkpatrick, and T. Izard The vinculin binding sites of talin and α-actinin are sufficient to activate vinculin J. Biol. Chem. 281 2006 7228 7236
    • (2006) J. Biol. Chem. , vol.281 , pp. 7228-7236
    • Bois, P.R.1    O'Hara, B.P.2    Nietlispach, D.3    Kirkpatrick, J.4    Izard, T.5
  • 22
    • 33750716480 scopus 로고    scopus 로고
    • Shigella applies molecular mimicry to subvert vinculin and invade host cells
    • T. Izard, G. Tran Van Nhieu, and P.R. Bois Shigella applies molecular mimicry to subvert vinculin and invade host cells J. Cell Biol. 175 2006 465 475
    • (2006) J. Cell Biol. , vol.175 , pp. 465-475
    • Izard, T.1    Tran Van Nhieu, G.2    Bois, P.R.3
  • 23
    • 80053403384 scopus 로고    scopus 로고
    • The Rickettsia surface cell antigen 4 applies mimicry to bind to and activate vinculin
    • H. Park, J.H. Lee, P. Cossart, E. Gouin, and T. Izard The Rickettsia surface cell antigen 4 applies mimicry to bind to and activate vinculin J. Biol. Chem. 286 2011 35096 35103
    • (2011) J. Biol. Chem. , vol.286 , pp. 35096-35103
    • Park, H.1    Lee, J.H.2    Cossart, P.3    Gouin, E.4    Izard, T.5
  • 25
    • 79960687699 scopus 로고    scopus 로고
    • Intermolecular versus intramolecular interactions of the vinculin binding site 33 of talin
    • S.D. Yogesha, A. Sharff, G. Bricogne, and T. Izard Intermolecular versus intramolecular interactions of the vinculin binding site 33 of talin Protein Sci. 20 2011 1471 1476
    • (2011) Protein Sci. , vol.20 , pp. 1471-1476
    • Yogesha, S.D.1    Sharff, A.2    Bricogne, G.3    Izard, T.4
  • 26
    • 84858689928 scopus 로고    scopus 로고
    • Crystal structure of vinculin in complex with vinculin binding site 50 (VBS50), the integrin binding site 2 (IBS2) of talin
    • S.D. Yogesha, E.S. Rangarajan, C. Vonrhein, G. Bricogne, and T. Izard Crystal structure of vinculin in complex with vinculin binding site 50 (VBS50), the integrin binding site 2 (IBS2) of talin Protein Sci. 21 2012 583 588
    • (2012) Protein Sci. , vol.21 , pp. 583-588
    • Yogesha, S.D.1    Rangarajan, E.S.2    Vonrhein, C.3    Bricogne, G.4    Izard, T.5
  • 27
    • 0035956427 scopus 로고    scopus 로고
    • Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteins
    • S. Huttelmaier, S. Illenberger, I. Grosheva, M. Rudiger, R.H. Singer, and B.M. Jockusch Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteins J. Cell Biol. 155 2001 775 786
    • (2001) J. Cell Biol. , vol.155 , pp. 775-786
    • Huttelmaier, S.1    Illenberger, S.2    Grosheva, I.3    Rudiger, M.4    Singer, R.H.5    Jockusch, B.M.6
  • 28
    • 66349131836 scopus 로고    scopus 로고
    • Raver1 interactions with vinculin and RNA suggest a feed-forward pathway in directing mRNA to focal adhesions
    • J.H. Lee, E.S. Rangarajan, S.D. Yogesha, and T. Izard Raver1 interactions with vinculin and RNA suggest a feed-forward pathway in directing mRNA to focal adhesions Structure 17 2009 833 842
    • (2009) Structure , vol.17 , pp. 833-842
    • Lee, J.H.1    Rangarajan, E.S.2    Yogesha, S.D.3    Izard, T.4
  • 29
    • 0029009673 scopus 로고
    • The carboxy-terminal tail domain of vinculin contains a cryptic binding site for acidic phospholipids
    • R.P. Johnson, and S.W. Craig The carboxy-terminal tail domain of vinculin contains a cryptic binding site for acidic phospholipids Biochem. Biophys. Res. Commun. 210 1995 159 164
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 159-164
    • Johnson, R.P.1    Craig, S.W.2
  • 30
    • 65449131260 scopus 로고    scopus 로고
    • Lipid binding to the tail domain of vinculin: Specificity and the role of the N and C termini
    • S.M. Palmer, M.P. Playford, S.W. Craig, M.D. Schaller, and S.L. Campbell Lipid binding to the tail domain of vinculin: specificity and the role of the N and C termini J. Biol. Chem. 284 2009 7223 7231
    • (2009) J. Biol. Chem. , vol.284 , pp. 7223-7231
    • Palmer, S.M.1    Playford, M.P.2    Craig, S.W.3    Schaller, M.D.4    Campbell, S.L.5
  • 31
    • 77956289735 scopus 로고    scopus 로고
    • A helix replacement mechanism directs metavinculin functions
    • E.S. Rangarajan, J.H. Lee, S.D. Yogesha, and T. Izard A helix replacement mechanism directs metavinculin functions PLoS One 5 2010 e10679
    • (2010) PLoS One , vol.5 , pp. 10679
    • Rangarajan, E.S.1    Lee, J.H.2    Yogesha, S.D.3    Izard, T.4
  • 32
    • 0032503970 scopus 로고    scopus 로고
    • Differential actin organization by vinculin isoforms: Implications for cell type-specific microfilament anchorage
    • M. Rudiger, N. Korneeva, C. Schwienbacher, E.E. Weiss, and B.M. Jockusch Differential actin organization by vinculin isoforms: implications for cell type-specific microfilament anchorage FEBS Lett. 431 1998 49 54
    • (1998) FEBS Lett. , vol.431 , pp. 49-54
    • Rudiger, M.1    Korneeva, N.2    Schwienbacher, C.3    Weiss, E.E.4    Jockusch, B.M.5
  • 33
    • 66349107636 scopus 로고    scopus 로고
    • Adhesion dance with raver
    • T. Madl, and M. Sattler Adhesion dance with raver Structure 17 2009 781 783
    • (2009) Structure , vol.17 , pp. 781-783
    • Madl, T.1    Sattler, M.2
  • 36
    • 79960689515 scopus 로고    scopus 로고
    • Apo raver1 structure reveals distinct RRM domain orientations
    • E.S. Rangarajan, J.H. Lee, and T. Izard Apo raver1 structure reveals distinct RRM domain orientations Protein Sci. 20 2011 1464 1470
    • (2011) Protein Sci. , vol.20 , pp. 1464-1470
    • Rangarajan, E.S.1    Lee, J.H.2    Izard, T.3
  • 37
    • 0030805718 scopus 로고    scopus 로고
    • Characterization of two F-actin-binding and oligomerization sites in the cell-contact protein vinculin
    • S. Huttelmaier, P. Bubeck, M. Rudiger, and B.M. Jockusch Characterization of two F-actin-binding and oligomerization sites in the cell-contact protein vinculin Eur. J. Biochem. 247 1997 1136 1142
    • (1997) Eur. J. Biochem. , vol.247 , pp. 1136-1142
    • Huttelmaier, S.1    Bubeck, P.2    Rudiger, M.3    Jockusch, B.M.4
  • 38
    • 38949130021 scopus 로고    scopus 로고
    • Human α-synemin interacts directly with vinculin and metavinculin
    • N. Sun, D.R. Critchley, D. Paulin, Z. Li, and R.M. Robson Human α-synemin interacts directly with vinculin and metavinculin Biochem. J. 409 2008 657 667
    • (2008) Biochem. J. , vol.409 , pp. 657-667
    • Sun, N.1    Critchley, D.R.2    Paulin, D.3    Li, Z.4    Robson, R.M.5
  • 43
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • G. Langer, S.X. Cohen, V.S. Lamzin, and A. Perrakis Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7 Nat. Protoc. 3 2008 1171 1179
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.