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Volumn 20, Issue 8, 2011, Pages 1464-1470

Apo raver1 structure reveals distinct RRM domain orientations

Author keywords

Actin cytoskeleton; Crystallography; Focal adhesion; RNA binding; RNP motif; Vinculin

Indexed keywords

ARGININE; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; PHOSPHATE; PROTEIN RAVER1; RNA; SULFATE; UNCLASSIFIED DRUG; VINCULIN;

EID: 79960689515     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.664     Document Type: Article
Times cited : (3)

References (34)
  • 1
  • 4
    • 0025761656 scopus 로고
    • RNA recognition: Towards identifiying determinants of specificity
    • Kenan DJ, Query CC, Keene JD (1991) RNA recognition: towards identifying determinants of specificity. Trends Biochem Sci 16:214-220. (Pubitemid 121004438)
    • (1991) Trends in Biochemical Sciences , vol.16 , Issue.1 , pp. 214-220
    • Kenan, D.J.1    Query, C.C.2    Keene, J.D.3
  • 5
    • 18544377013 scopus 로고    scopus 로고
    • The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression
    • DOI 10.1111/j.1742-4658.2005.04653.x
    • Maris C, Dominguez C, Allain FH (2005) The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression. FEBS J 272:2118-2131. (Pubitemid 40655326)
    • (2005) FEBS Journal , vol.272 , Issue.9 , pp. 2118-2131
    • Maris, C.1    Dominguez, C.2    Allain, F.H.-T.3
  • 6
  • 7
    • 0026660025 scopus 로고
    • HnRNP I, the polypyrimidine tract-binding protein: Distinct nuclear localization and association with hnRNAs
    • Ghetti A, Pinol-Roma S, Michael WM, Morandi C, Dreyfuss G (1992) hnRNP I, the polypyrimidine tract-binding protein: distinct nuclear localization and association with hnRNAs. Nucleic Acids Res 20:3671-3678.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3671-3678
    • Ghetti, A.1    Pinol-Roma, S.2    Michael, W.M.3    Morandi, C.4    Dreyfuss, G.5
  • 8
    • 0022004694 scopus 로고
    • Molecular shape and self-association of vinculin and metavinculin
    • DOI 10.1002/jcb.240290104
    • Molony L, Burridge K (1985) Molecular shape and self-association of vinculin and metavinculin. J Cell Biochem 29:31-36. (Pubitemid 15235686)
    • (1985) Journal of Cellular Biochemistry , vol.29 , Issue.1 , pp. 31-36
    • Molony, L.1    Burridge, K.2
  • 10
    • 0020082249 scopus 로고
    • High-affinity interaction of vinculin with actin filaments in vitro
    • Wilkins JA, Lin S (1982) High-affinity interaction of vinculin with actin filaments in vitro. Cell 28:83-90. (Pubitemid 12223310)
    • (1982) Cell , vol.28 , Issue.1 , pp. 83-90
    • Wilkins, J.A.1    Lin, S.2
  • 11
    • 0019568618 scopus 로고
    • Interaction of alpha-actinin and vinculin with actin: Opposite effects on filament network formation
    • Jockusch BM, Isenberg G (1981) Interaction of alpha-actinin and vinculin with actin: opposite effects on filament network formation. Proc Natl Acad Sci USA 78:3005-3009.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3005-3009
    • Jockusch, B.M.1    Isenberg, G.2
  • 12
    • 0021214312 scopus 로고
    • An interaction between vinculin and talin
    • Burridge K, Mangeat P (1984) An interaction between vinculin and talin. Nature 308:744-746. (Pubitemid 14127674)
    • (1984) Nature , vol.308 , Issue.5961 , pp. 744-746
    • Burridge, K.1    Mangeat, P.2
  • 14
    • 0347717894 scopus 로고    scopus 로고
    • Vinculin activation by talin through helical bundle conversion
    • DOI 10.1038/nature02281
    • Izard T, Evans G, Borgon RA, Rush CL, Bricogne G, Bois PR (2004) Vinculin activation by talin through helical bundle conversion. Nature 427:171-175. (Pubitemid 38094959)
    • (2004) Nature , vol.427 , Issue.6970 , pp. 171-175
    • Izard, T.1    Evans, G.2    Borgon, R.A.3    Rush, C.L.4    Bricogne, G.5    Bois, P.R.J.6
  • 15
    • 77956289735 scopus 로고    scopus 로고
    • A helix replacement mechanism directs metavinculin functions
    • Rangarajan ES, Lee JH, Yogesha SD, Izard T (2010) A helix replacement mechanism directs metavinculin functions. PLoS ONE 5:e10679.
    • (2010) PLoS ONE , vol.5
    • Rangarajan, E.S.1    Lee, J.H.2    Yogesha, S.D.3    Izard, T.4
  • 16
    • 0033695362 scopus 로고    scopus 로고
    • Structure of the dimerization and beta-catenin-binding region of alpha-catenin
    • Pokutta S, Weis WI (2000) Structure of the dimerization and beta-catenin-binding region of alpha-catenin. Mol Cell 5:533-543.
    • (2000) Mol Cell , vol.5 , pp. 533-543
    • Pokutta, S.1    Weis, W.I.2
  • 17
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson RP, Craig SW (1994) An intramolecular association between the head and tail domains of vinculin modulates talin binding. J Biol Chem 269:12611-12619. (Pubitemid 24202049)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.17 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 18
    • 3042600016 scopus 로고    scopus 로고
    • Structural basis for amplifying vinculin activation by talin
    • DOI 10.1074/jbc.M403076200
    • Izard T, Vonrhein C (2004) Structural basis for amplifying vinculin activation by talin. J Biol Chem 279:27667-27678. (Pubitemid 38812608)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27667-27678
    • Izard, T.1    Vonrhein, C.2
  • 19
    • 21744441321 scopus 로고    scopus 로고
    • Structural dynamics of alpha-actinin-vinculin interactions
    • Bois PR, Borgon RA, Vonrhein C, Izard T (2005) Structural dynamics of alpha-actinin-vinculin interactions. Mol Cell Biol 25:6112-6122.
    • (2005) Mol Cell Biol , vol.25 , pp. 6112-6122
    • Bois, P.R.1    Borgon, R.A.2    Vonrhein, C.3    Izard, T.4
  • 20
    • 33646368402 scopus 로고    scopus 로고
    • The vinculin binding sites of talin and alpha-actinin are sufficient to activate vinculin
    • DOI 10.1074/jbc.M510397200
    • Bois PR, O'Hara BP, Nietlispach D, Kirkpatrick J, Izard T (2006) The vinculin binding sites of talin and alpha-actinin are sufficient to activate vinculin. J Biol Chem 281:7228-7236. (Pubitemid 43847490)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.11 , pp. 7228-7236
    • Bois, P.R.J.1    O'Hara, B.P.2    Nietlispach, D.3    Kirkpatrick, J.4    Izard, T.5
  • 21
    • 33750716480 scopus 로고    scopus 로고
    • Shigella applies molecular mimicry to subvert vinculin and invade host cells
    • Izard T, Tran Van Nhieu G, Bois PR (2006) Shigella applies molecular mimicry to subvert vinculin and invade host cells. J Cell Biol 175:465-475.
    • (2006) J Cell Biol , vol.175 , pp. 465-475
    • Izard, T.1    Van Tran Nhieu, G.2    Bois, P.R.3
  • 22
    • 35649016759 scopus 로고    scopus 로고
    • Vinculin binding in its closed conformation by a helix addition mechanism
    • DOI 10.1038/sj.emboj.7601863, PII 7601863
    • Tran Van Nhieu G, Izard T (2007) Vinculin binding in its closed conformation by a helix addition mechanism. EMBO J 26:4588-4596. (Pubitemid 350036624)
    • (2007) EMBO Journal , vol.26 , Issue.21 , pp. 4588-4596
    • Tran, V.N.G.1    Izard, T.2
  • 23
    • 66349131836 scopus 로고    scopus 로고
    • Raver1 interactions with vinculin and RNA suggest a feed-forward pathway in directing mRNA to focal adhesions
    • Lee JH, Rangarajan ES, Yogesha SD, Izard T (2009) Raver1 interactions with vinculin and RNA suggest a feed-forward pathway in directing mRNA to focal adhesions. Structure 17:833-842.
    • (2009) Structure , vol.17 , pp. 833-842
    • Lee, J.H.1    Rangarajan, E.S.2    Yogesha, S.D.3    Izard, T.4
  • 24
    • 66349107636 scopus 로고    scopus 로고
    • Adhesion dance with raver
    • Madl T, Sattler M (2009) Adhesion dance with raver. Structure 17:781-783.
    • (2009) Structure , vol.17 , pp. 781-783
    • Madl, T.1    Sattler, M.2
  • 25
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • DOI 10.1002/(SICI)1097-0134(19980201)30:2<144::AID-PROT4>3.0.CO;2-N
    • Hayward S, Berendsen HJ (1998) Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins 30:144-154. (Pubitemid 28080149)
    • (1998) Proteins: Structure, Function and Genetics , vol.30 , Issue.2 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.C.2
  • 27
    • 78650145379 scopus 로고    scopus 로고
    • AutoPROC - A framework for automated data processing
    • Vonrhein C, Bricogne G (2008) AutoPROC - a framework for automated data processing. Acta Crystallogr A 64:C78.
    • (2008) Acta Crystallogr A , vol.64
    • Vonrhein, C.1    Bricogne, G.2
  • 29
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin A, Teplyakov A (1997) MOLREP: an automated program for molecular replacement. J Appl Crystallogr 30:1022-1025. (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 30
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • DOI 10.1038/8263
    • Perrakis A, Morris R, Lamzin VS (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6:458-463. (Pubitemid 29218016)
    • (1999) Nature Structural Biology , vol.6 , Issue.5 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.