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Volumn 278, Issue 17, 2011, Pages 2980-2996

DYNLL/LC8: A light chain subunit of the dynein motor complex and beyond

Author keywords

dynein; hub protein; intracellular transport; linear motif; protein protein interactions

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; DYNEIN LIGHT CHAIN; HUB PROTEIN; MOLECULAR MOTOR; PROTEIN SUBUNIT; REGULATOR PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84860389388     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08254.x     Document Type: Review
Times cited : (109)

References (135)
  • 2
    • 35948979262 scopus 로고    scopus 로고
    • Dyneins across eukaryotes: A comparative genomic analysis
    • DOI 10.1111/j.1600-0854.2007.00646.x
    • Wickstead B, &, Gull K, (2007) Dyneins across eukaryotes: a comparative genomic analysis. Traffic 8, 1708-1721. (Pubitemid 350066684)
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1708-1721
    • Wickstead, B.1    Gull, K.2
  • 3
    • 84860390085 scopus 로고    scopus 로고
    • Molecular organization and force-generating mechanism of dynein
    • Sakakibara H, &, Oiwa K, (2011) Molecular organization and force-generating mechanism of dynein. FEBS J 278, 2964-2979.
    • (2011) FEBS J , vol.278 , pp. 2964-2979
    • Sakakibara, H.1    Oiwa, K.2
  • 4
    • 0020309907 scopus 로고
    • Purification and polypeptide composition of dynein ATPases from chlamydomonas flagella
    • Pfister KK, Fay RB, &, Witman GB, (1982) Purification and polypeptide composition of dynein ATPases from Chlamydomonas flagella. Cell Motil 2, 525-547. (Pubitemid 13088596)
    • (1982) Cell Motility , vol.2 , Issue.6 , pp. 525-547
    • Pfister, K.K.1    Fay, R.B.2    Witman, G.B.3
  • 5
    • 0029977560 scopus 로고    scopus 로고
    • Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster
    • Dick T, Ray K, Salz HK, &, Chia W, (1996) Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster. Mol Cell Biol 16, 1966-1977. (Pubitemid 26123717)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.5 , pp. 1966-1977
    • Dick, T.1    Ray, K.2    Salz, H.K.3    Chia, W.4
  • 8
    • 0035830488 scopus 로고    scopus 로고
    • Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain
    • DOI 10.1006/jmbi.2000.4374
    • Fan J, Zhang Q, Tochio H, Li M, &, Zhang M, (2001) Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain. J Mol Biol 306, 97-108. (Pubitemid 33027735)
    • (2001) Journal of Molecular Biology , vol.306 , Issue.1 , pp. 97-108
    • Fan, J.-S.1    Zhang, Q.2    Tochio, H.3    Li, M.4    Zhang, M.5
  • 9
    • 33748940071 scopus 로고    scopus 로고
    • Dazl can bind to dynein motor complex and may play a role in transport of specific mRNAs
    • DOI 10.1038/sj.emboj.7601304, PII 7601304
    • Lee KH, Lee S, Kim B, Chang S, Kim SW, Paick JS, &, Rhee K, (2006) Dazl can bind to dynein motor complex and may play a role in transport of specific mRNAs. EMBO J 25, 4263-4270. (Pubitemid 44435224)
    • (2006) EMBO Journal , vol.25 , Issue.18 , pp. 4263-4270
    • Lee, K.H.1    Lee, S.2    Kim, B.3    Chang, S.4    Kim, S.W.5    Paick, J.-S.6    Rhee, K.7
  • 10
    • 14844333111 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation
    • DOI 10.1074/jbc.M411408200
    • Lo KW, Kan HM, Chan LN, Xu WG, Wang KP, Wu Z, Sheng M, &, Zhang M, (2005) The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation. J Biol Chem 280, 8172-8179. (Pubitemid 40349718)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 8172-8179
    • Lo, K.W.-H.1    Kan, H.-M.2    Chan, L.-N.3    Xu, W.-G.4    Wang, K.-P.5    Wu, Z.6    Sheng, M.7    Zhang, M.8
  • 11
    • 2342549289 scopus 로고    scopus 로고
    • Egalitarian binds dynein light chain to establish oocyte polarity and maintain oocyte fate
    • DOI 10.1038/ncb1122
    • Navarro C, Puthalakath H, Adams JM, Strasser A, &, Lehmann R, (2004) Egalitarian binds dynein light chain to establish oocyte polarity and maintain oocyte fate. Nat Cell Biol 6, 427-435. (Pubitemid 38607503)
    • (2004) Nature Cell Biology , vol.6 , Issue.5 , pp. 427-435
    • Navarro, C.1    Puthalakath, H.2    Adams, J.M.3    Strasser, A.4    Lehmann, R.5
  • 12
    • 0035903004 scopus 로고    scopus 로고
    • Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique
    • DOI 10.1016/S0014-5793(01)02718-1, PII S0014579301027181
    • Rodriguez-Crespo I, Yelamos B, Roncal F, Albar JP, Ortiz de Montellano PR, &, Gavilanes F, (2001) Identification of novel cellular proteins that bind to the LC8 dynein light chain using a pepscan technique. FEBS Lett 503, 135-141. (Pubitemid 32763193)
    • (2001) FEBS Letters , vol.503 , Issue.2-3 , pp. 135-141
    • Rodriguez-Crespo, I.1    Yelamos, B.2    Roncal, F.3    Albar, J.P.4    Ortiz De Montellano, P.R.5    Gavilanes, F.6
  • 13
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • DOI 10.1016/S1097-2765(00)80456-6
    • Puthalakath H, Huang DC, O'Reilly LA, King SM, &, Strasser A, (1999) The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell 3, 287-296. (Pubitemid 29290669)
    • (1999) Molecular Cell , vol.3 , Issue.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.S.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 14
    • 34447277680 scopus 로고    scopus 로고
    • Structure and Dynamics of LC8 Complexes with KXTQT-Motif Peptides: Swallow and Dynein Intermediate Chain Compete for a Common Site
    • DOI 10.1016/j.jmb.2007.05.046, PII S0022283607006821
    • Benison G, Karplus PA, &, Barbar E, (2007) Structure and dynamics of LC8 complexes with KXTQT-motif peptides: swallow and dynein intermediate chain compete for a common site. J Mol Biol 371, 457-468. (Pubitemid 47048273)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.2 , pp. 457-468
    • Benison, G.1    Karplus, P.A.2    Barbar, E.3
  • 16
    • 56249116551 scopus 로고    scopus 로고
    • Differences in dynamic structure of LC8 monomer, dimer, and dimer-peptide complexes
    • Hall J, Hall A, Pursifull N, &, Barbar E, (2008) Differences in dynamic structure of LC8 monomer, dimer, and dimer-peptide complexes. Biochemistry 47, 11940-11952.
    • (2008) Biochemistry , vol.47 , pp. 11940-11952
    • Hall, J.1    Hall, A.2    Pursifull, N.3    Barbar, E.4
  • 17
    • 13844275995 scopus 로고    scopus 로고
    • Solution structure of the Tctex1 dimer reveals a mechanism for dynein-cargo interactions
    • DOI 10.1016/j.str.2004.11.013
    • Wu H, Maciejewski MW, Takebe S, &, King SM, (2005) Solution structure of the Tctex1 dimer reveals a mechanism for dynein-cargo interactions. Structure 13, 213-223. (Pubitemid 40253525)
    • (2005) Structure , vol.13 , Issue.2 , pp. 213-223
    • Wu, H.1    Maciejewski, M.W.2    Takebe, S.3    King, S.M.4
  • 18
    • 38849199178 scopus 로고    scopus 로고
    • Dynein light chain LC8 is a dimerization hub essential in diverse protein networks
    • DOI 10.1021/bi701995m
    • Barbar E, (2008) Dynein light chain LC8 is a dimerization hub essential in diverse protein networks. Biochemistry 47, 503-508. (Pubitemid 351195422)
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 503-508
    • Barbar, E.1
  • 20
    • 56249132454 scopus 로고    scopus 로고
    • The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8
    • Benison G, Karplus PA, &, Barbar E, (2008) The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8. J Mol Biol 384, 954-966.
    • (2008) J Mol Biol , vol.384 , pp. 954-966
    • Benison, G.1    Karplus, P.A.2    Barbar, E.3
  • 24
    • 73149105738 scopus 로고    scopus 로고
    • Structural, thermodynamic, and kinetic effects of a phosphomimetic mutation in dynein light chain LC8
    • Benison G, Chiodo M, Karplus PA, &, Barbar E, (2009) Structural, thermodynamic, and kinetic effects of a phosphomimetic mutation in dynein light chain LC8. Biochemistry 48, 11381-11389.
    • (2009) Biochemistry , vol.48 , pp. 11381-11389
    • Benison, G.1    Chiodo, M.2    Karplus, P.A.3    Barbar, E.4
  • 26
    • 79955142468 scopus 로고    scopus 로고
    • Directed evolution reveals the binding motif preference of the LC8/DYNLL hub protein and predicts large numbers of novel binders in the human proteome
    • Rapali P, Radnai L, Suveges D, Harmat V, Tolgyesi F, Wahlgren WY, Katona G, Nyitray L, &, Pal G, (2011) Directed evolution reveals the binding motif preference of the LC8/DYNLL hub protein and predicts large numbers of novel binders in the human proteome. PLoS ONE 6, e18818.
    • (2011) PLoS ONE , vol.6
    • Rapali, P.1    Radnai, L.2    Suveges, D.3    Harmat, V.4    Tolgyesi, F.5    Wahlgren, W.Y.6    Katona, G.7    Nyitray, L.8    Pal, G.9
  • 27
    • 77951708885 scopus 로고    scopus 로고
    • Structural basis for the interaction between dynein light chain 1 and the glutamate channel homolog GRINL1A
    • Garcia-Mayoral MF, Martinez-Moreno M, Albar JP, Rodriguez-Crespo I, &, Bruix M, (2010) Structural basis for the interaction between dynein light chain 1 and the glutamate channel homolog GRINL1A. FEBS J 277, 2340-2350.
    • (2010) FEBS J , vol.277 , pp. 2340-2350
    • Garcia-Mayoral, M.F.1    Martinez-Moreno, M.2    Albar, J.P.3    Rodriguez-Crespo, I.4    Bruix, M.5
  • 28
    • 78650888642 scopus 로고    scopus 로고
    • Structural models of DYNLL1 with interacting partners: African swine fever virus protein p54 and postsynaptic scaffolding protein gephyrin
    • Garcia-Mayoral MF, Rodriguez-Crespo I, &, Bruix M, (2010) Structural models of DYNLL1 with interacting partners: African swine fever virus protein p54 and postsynaptic scaffolding protein gephyrin. FEBS Lett 585, 53-57.
    • (2010) FEBS Lett , vol.585 , pp. 53-57
    • Garcia-Mayoral, M.F.1    Rodriguez-Crespo, I.2    Bruix, M.3
  • 29
    • 70450235060 scopus 로고    scopus 로고
    • Multivalency in the assembly of intrinsically disordered dynein intermediate chain
    • Hall J, Karplus PA, &, Barbar E, (2009) Multivalency in the assembly of intrinsically disordered dynein intermediate chain. J Biol Chem 284, 33115-33121.
    • (2009) J Biol Chem , vol.284 , pp. 33115-33121
    • Hall, J.1    Karplus, P.A.2    Barbar, E.3
  • 30
    • 20444488809 scopus 로고    scopus 로고
    • Crystal structure of dynein light chain TcTex-1
    • DOI 10.1074/jbc.M414643200
    • Williams JC, Xie H, &, Hendrickson WA, (2005) Crystal structure of dynein light chain TcTex-1. J Biol Chem 280, 21981-21986. (Pubitemid 40827851)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.23 , pp. 21981-21986
    • Williams, J.C.1    Xie, H.2    Hendrickson, W.A.3
  • 31
    • 0035958082 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif
    • Lo KW, Naisbitt S, Fan JS, Sheng M, &, Zhang M, (2001) The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif. J Biol Chem 276, 14059-14066.
    • (2001) J Biol Chem , vol.276 , pp. 14059-14066
    • Lo, K.W.1    Naisbitt, S.2    Fan, J.S.3    Sheng, M.4    Zhang, M.5
  • 32
    • 33750054653 scopus 로고    scopus 로고
    • Alternatively spliced exon B of myosin Va is essential for binding the tail-associated light chain shared by dynein
    • DOI 10.1021/bi060991e
    • Hodi Z, Nemeth AL, Radnai L, Hetenyi C, Schlett K, Bodor A, Perczel A, &, Nyitray L, (2006) Alternatively spliced exon B of myosin Va is essential for binding the tail-associated light chain shared by dynein. Biochemistry 45, 12582-12595. (Pubitemid 44583700)
    • (2006) Biochemistry , vol.45 , Issue.41 , pp. 12582-12595
    • Hodi, Z.1    Nemeth, A.L.2    Radnai, L.3    Hetenyi, C.4    Schlett, K.5    Bodor, A.6    Perczel, A.7    Nyitray, L.8
  • 33
    • 33749012287 scopus 로고    scopus 로고
    • The binding of DYNLL2 to myosin Va requires alternatively spliced exon B and stabilizes a portion of the myosin's coiled-coil domain
    • DOI 10.1021/bi061142u
    • Wagner W, Fodor E, Ginsburg A, &, Hammer JA III, (2006) The binding of DYNLL2 to myosin Va requires alternatively spliced exon B and stabilizes a portion of the myosin's coiled-coil domain. Biochemistry 45, 11564-11577. (Pubitemid 44454004)
    • (2006) Biochemistry , vol.45 , Issue.38 , pp. 11564-11577
    • Wagner, W.1    Fodor, E.2    Ginsburg, A.3    Hammer III, J.A.4
  • 34
    • 61849123674 scopus 로고    scopus 로고
    • NMR analysis of dynein light chain dimerization and interactions with diverse ligands
    • Benison G, &, Barbar E, (2009) NMR analysis of dynein light chain dimerization and interactions with diverse ligands. Methods Enzymol 455, 237-258.
    • (2009) Methods Enzymol , vol.455 , pp. 237-258
    • Benison, G.1    Barbar, E.2
  • 35
    • 0035996716 scopus 로고    scopus 로고
    • Backbone dynamics of the 8 kDa dynein light chain dimer reveals molecular basis of the protein's functional diversity
    • DOI 10.1023/A:1016332918178
    • Fan JS, Zhang Q, Tochio H, &, Zhang M, (2002) Backbone dynamics of the 8 kDa dynein light chain dimer reveals molecular basis of the protein's functional diversity. J Biomol NMR 23, 103-114. (Pubitemid 34778163)
    • (2002) Journal of Biomolecular NMR , vol.23 , Issue.2 , pp. 103-114
    • Fan, J.-S.1    Zhang, Q.2    Tochio, H.3    Zhang, M.4
  • 37
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen M, Choi SK, &, Whitesides GM, (1998) Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. Angew Chem Int Ed 37, 2754-2794. (Pubitemid 29008561)
    • (1998) Angewandte Chemie - International Edition , vol.37 , Issue.20 , pp. 2754-2794
    • Mammen, M.1    Choi, S.-K.2    Whitesides, G.M.3
  • 38
    • 0035852805 scopus 로고    scopus 로고
    • Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein
    • DOI 10.1021/bi002278+
    • Barbar E, Kleinman B, Imhoff D, Li M, Hays TS, &, Hare M, (2001) Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein. Biochemistry 40, 1596-1605. (Pubitemid 32144028)
    • (2001) Biochemistry , vol.40 , Issue.6 , pp. 1596-1605
    • Barbar, E.1    Kleinman, B.2    Imhoff, D.3    Li, M.4    Hays, T.S.5    Hare, M.6
  • 39
    • 1342331844 scopus 로고    scopus 로고
    • The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila
    • DOI 10.1110/ps.03462204
    • Makokha M, Huang YJ, Montelione G, Edison AS, &, Barbar E, (2004) The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila. Protein Sci 13, 727-734. (Pubitemid 38252570)
    • (2004) Protein Science , vol.13 , Issue.3 , pp. 727-734
    • Makokha, M.1    Huang, Y.J.2    Montelione, G.3    Edison, A.S.4    Barbar, E.5
  • 40
    • 27444442808 scopus 로고    scopus 로고
    • Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation
    • DOI 10.1021/bi0512694
    • Nyarko A, Cochrun L, Norwood S, Pursifull N, Voth A, &, Barbar E, (2005) Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation. Biochemistry 44, 14248-14255. (Pubitemid 41533049)
    • (2005) Biochemistry , vol.44 , Issue.43 , pp. 14248-14255
    • Nyarko, A.1    Cochrun, L.2    Norwood, S.3    Pursifull, N.4    Voth, A.5    Barbar, E.6
  • 41
    • 0142039800 scopus 로고    scopus 로고
    • Structure of the Monomeric 8-kDa Dynein Light Chain and Mechanism of the Domain-swapped Dimer Assembly
    • DOI 10.1074/jbc.M307118200
    • Wang W, Lo KW, Kan HM, Fan JS, &, Zhang M, (2003) Structure of the monomeric 8-kDa dynein light chain and mechanism of the domain-swapped dimer assembly. J Biol Chem 278, 41491-41499. (Pubitemid 37280978)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.42 , pp. 41491-41499
    • Wang, W.1    Lo, K.W.-H.2    Kan, H.-M.3    Fan, J.-S.4    Zhang, M.5
  • 42
    • 42949104734 scopus 로고    scopus 로고
    • Serine 88 phosphorylation of the 8-kDa dynein light chain 1 is a molecular switch for its dimerization status and functions
    • Song C, Wen W, Rayala SK, Chen M, Ma J, Zhang M, &, Kumar R, (2008) Serine 88 phosphorylation of the 8-kDa dynein light chain 1 is a molecular switch for its dimerization status and functions. J Biol Chem 283, 4004-4013.
    • (2008) J Biol Chem , vol.283 , pp. 4004-4013
    • Song, C.1    Wen, W.2    Rayala, S.K.3    Chen, M.4    Ma, J.5    Zhang, M.6    Kumar, R.7
  • 43
    • 34447127515 scopus 로고    scopus 로고
    • Potential role for phosphorylation in differential regulation of the assembly of jdynein light chains
    • DOI 10.1074/jbc.M610445200
    • Song Y, Benison G, Nyarko A, Hays TS, &, Barbar E, (2007) Potential role for phosphorylation in differential regulation of the assembly of dynein light chains. J Biol Chem 282, 17272-17279. (Pubitemid 47093205)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.23 , pp. 17272-17279
    • Song, Y.1    Benison, G.2    Nyarko, A.3    Hays, T.S.4    Barbar, E.5
  • 44
    • 2942603255 scopus 로고    scopus 로고
    • Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes
    • DOI 10.1016/j.ccr.2004.05.022, PII S1535610804001473
    • Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, &, Kumar R, (2004) Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes. Cancer Cell 5, 575-585. (Pubitemid 38748919)
    • (2004) Cancer Cell , vol.5 , Issue.6 , pp. 575-585
    • Vadlamudi, R.K.1    Bagheri-Yarmand, R.2    Yang, Z.3    Balasenthil, S.4    Nguyen, D.5    Sahin, A.A.6    Den Hollander, P.7    Kumar, R.8
  • 45
    • 12844272185 scopus 로고    scopus 로고
    • Dynein light chain 1 phosphorylation controls macropinocytosis
    • DOI 10.1074/jbc.M408486200
    • Yang Z, Vadlamudi RK, &, Kumar R, (2005) Dynein light chain 1 phosphorylation controls macropinocytosis. J Biol Chem 280, 654-659. (Pubitemid 40165032)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.1 , pp. 654-659
    • Yang, Z.1    Vadlamudi, R.K.2    Kumar, R.3
  • 46
    • 67649464367 scopus 로고    scopus 로고
    • Interaction with LC8 is required for Pak1 nuclear import and is indispensable for zebrafish development
    • Lightcap CM, Kari G, Arias-Romero LE, Chernoff J, Rodeck U, &, Williams JC, (2009) Interaction with LC8 is required for Pak1 nuclear import and is indispensable for zebrafish development. PLoS ONE 4, e6025.
    • (2009) PLoS ONE , vol.4
    • Lightcap, C.M.1    Kari, G.2    Arias-Romero, L.E.3    Chernoff, J.4    Rodeck, U.5    Williams, J.C.6
  • 49
    • 68049135457 scopus 로고    scopus 로고
    • Dynein light chain LC8 regulates syntaphilin-mediated mitochondrial docking in axons
    • Chen YM, Gerwin C, &, Sheng ZH, (2009) Dynein light chain LC8 regulates syntaphilin-mediated mitochondrial docking in axons. J Neurosci 29, 9429-9438.
    • (2009) J Neurosci , vol.29 , pp. 9429-9438
    • Chen, Y.M.1    Gerwin, C.2    Sheng, Z.H.3
  • 50
    • 0037006969 scopus 로고    scopus 로고
    • Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74
    • DOI 10.1021/bi011970h
    • Makokha M, Hare M, Li M, Hays T, &, Barbar E, (2002) Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74. Biochemistry 41, 4302-4311. (Pubitemid 34259873)
    • (2002) Biochemistry , vol.41 , Issue.13 , pp. 4302-4311
    • Makokha, M.1    Hare, M.2    Li, M.3    Hays, T.4    Barbar, E.5
  • 51
    • 10644253619 scopus 로고    scopus 로고
    • The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8
    • DOI 10.1021/bi048451+
    • Nyarko A, Hare M, Hays TS, &, Barbar E, (2004) The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8. Biochemistry 43, 15595-15603. (Pubitemid 39647485)
    • (2004) Biochemistry , vol.43 , Issue.49 , pp. 15595-15603
    • Nyarko, A.1    Hare, M.2    Hays, T.S.3    Barbar, E.4
  • 52
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • DOI 10.1016/j.febslet.2005.03.072, PII S0014579305004242
    • Tompa P, (2005) The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 579, 3346-3354. (Pubitemid 40804685)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3346-3354
    • Tompa, P.1
  • 54
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • DOI 10.1093/bioinformatics/btm035
    • Fuxreiter M, Tompa P, &, Simon I, (2007) Local structural disorder imparts plasticity on linear motifs. Bioinformatics 23, 950-956. (Pubitemid 47050581)
    • (2007) Bioinformatics , vol.23 , Issue.8 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3
  • 55
    • 33748460073 scopus 로고    scopus 로고
    • Heteronuclear NMR Identifies a Nascent Helix in Intrinsically Disordered Dynein Intermediate Chain: Implications for Folding and Dimerization
    • DOI 10.1016/j.jmb.2006.08.006, PII S0022283606009946
    • Benison G, Nyarko A, &, Barbar E, (2006) Heteronuclear NMR identifies a nascent helix in intrinsically disordered dynein intermediate chain: implications for folding and dimerization. J Mol Biol 362, 1082-1093. (Pubitemid 44353526)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.5 , pp. 1082-1093
    • Benison, G.1    Nyarko, A.2    Barbar, E.3
  • 56
    • 33845486323 scopus 로고    scopus 로고
    • Bim, Bad and Bmf: Intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets
    • DOI 10.1038/sj.cdd.4401934, PII 4401934
    • Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, &, Day CL, (2007) Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. Cell Death Differ 14, 128-136. (Pubitemid 44911900)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.1 , pp. 128-136
    • Hinds, M.G.1    Smits, C.2    Fredericks-Short, R.3    Risk, J.M.4    Bailey, M.5    Huang, D.C.S.6    Day, C.L.7
  • 58
    • 4043144340 scopus 로고    scopus 로고
    • Cellulose membrane supported peptide arrays for deciphering protein-protein interaction sites: The case of PIN, a protein with multiple natural partners
    • DOI 10.1023/B:MODI.0000036242.01129.27
    • Lajoix AD, Gross R, Aknin C, Dietz S, Granier C, &, Laune D, (2004) Cellulose membrane supported peptide arrays for deciphering protein-protein interaction sites: the case of PIN, a protein with multiple natural partners. Mol Divers 8, 281-290. (Pubitemid 39061576)
    • (2004) Molecular Diversity , vol.8 , Issue.3 , pp. 281-290
    • Lajoix, A.-D.1    Gross, R.2    Aknin, C.3    Dietz, S.4    Granier, C.5    Laune, D.6
  • 59
    • 49749117432 scopus 로고    scopus 로고
    • Contextual specificity in peptide-mediated protein interactions
    • Stein A, &, Aloy P, (2008) Contextual specificity in peptide-mediated protein interactions. PLoS ONE 3, e2524.
    • (2008) PLoS ONE , vol.3
    • Stein, A.1    Aloy, P.2
  • 63
    • 0033603631 scopus 로고    scopus 로고
    • High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70
    • DOI 10.1006/jmbi.1999.2776
    • Morshauser RC, Hu W, Wang H, Pang Y, Flynn GC, &, Zuiderweg ER, (1999) High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70. J Mol Biol 289, 1387-1403. (Pubitemid 29296712)
    • (1999) Journal of Molecular Biology , vol.289 , Issue.5 , pp. 1387-1403
    • Morshauser, R.C.1    Hu, W.2    Wang, H.3    Pang, Y.4    Flynn, G.C.5    Zuiderweg, E.R.P.6
  • 65
    • 0036892923 scopus 로고    scopus 로고
    • The RACK1 scaffold protein: A dynamic cog in cell response mechanisms
    • DOI 10.1124/mol.62.6.1261
    • McCahill A, Warwicker J, Bolger GB, Houslay MD, &, Yarwood SJ, (2002) The RACK1 scaffold protein: a dynamic cog in cell response mechanisms. Mol Pharmacol 62, 1261-1273. (Pubitemid 35403822)
    • (2002) Molecular Pharmacology , vol.62 , Issue.6 , pp. 1261-1273
    • McCahill, A.1    Warwicker, J.2    Bolger, G.B.3    Houslay, M.D.4    Yarwood, S.J.5
  • 66
    • 34548603504 scopus 로고    scopus 로고
    • Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation
    • DOI 10.1038/nature06146, PII NATURE06146
    • Jia D, Jurkowska RZ, Zhang X, Jeltsch A, &, Cheng X, (2007) Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation. Nature 449, 248-251. (Pubitemid 47402375)
    • (2007) Nature , vol.449 , Issue.7159 , pp. 248-251
    • Jia, D.1    Jurkowska, R.Z.2    Zhang, X.3    Jeltsch, A.4    Cheng, X.5
  • 67
    • 0033787039 scopus 로고    scopus 로고
    • The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes
    • Schnorrer F, Bohmann K, &, Nusslein-Volhard C, (2000) The molecular motor dynein is involved in targeting swallow and bicoid RNA to the anterior pole of Drosophila oocytes. Nat Cell Biol 2, 185-190.
    • (2000) Nat Cell Biol , vol.2 , pp. 185-190
    • Schnorrer, F.1    Bohmann, K.2    Nusslein-Volhard, C.3
  • 68
    • 10644221806 scopus 로고    scopus 로고
    • Dynein Light Chain LC8 Promotes Assembly of the Coiled-Coil Domain of Swallow Protein
    • DOI 10.1021/bi036328x
    • Wang L, Hare M, Hays TS, &, Barbar E, (2004) Dynein light chain LC8 promotes assembly of the coiled-coil domain of swallow protein. Biochemistry 43, 4611-4620. (Pubitemid 38500590)
    • (2004) Biochemistry , vol.43 , Issue.15 , pp. 4611-4620
    • Wang, L.1    Hare, M.2    Hays, T.S.3    Barbar, E.4
  • 71
    • 34347383511 scopus 로고    scopus 로고
    • Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex
    • DOI 10.1038/ncb1604, PII NCB1604
    • Stelter P, Kunze R, Flemming D, Hopfner D, Diepholz M, Philippsen P, Bottcher B, &, Hurt E, (2007) Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex. Nat Cell Biol 9, 788-796. (Pubitemid 47019465)
    • (2007) Nature Cell Biology , vol.9 , Issue.7 , pp. 788-796
    • Stelter, P.1    Kunze, R.2    Flemming, D.3    Hopfner, D.4    Diepholz, M.5    Philippsen, P.6    Bottcher, B.7    Hurt, E.8
  • 72
    • 33745235514 scopus 로고    scopus 로고
    • Dynein light chain 1 contributes to cell cycle progression by increasing cyclin-dependent kinase 2 activity in estrogen-stimulated cells
    • DOI 10.1158/0008-5472.CAN-05-3480
    • den Hollander P, &, Kumar R, (2006) Dynein light chain 1 contributes to cell cycle progression by increasing cyclin-dependent kinase 2 activity in estrogen-stimulated cells. Cancer Res 66, 5941-5949. (Pubitemid 43927150)
    • (2006) Cancer Research , vol.66 , Issue.11 , pp. 5941-5949
    • Den Hollander, P.1    Kumar, R.2
  • 73
    • 71949085771 scopus 로고    scopus 로고
    • A role for dynein in the inhibition of germ cell proliferative fate
    • Dorsett M, &, Schedl T, (2009) A role for dynein in the inhibition of germ cell proliferative fate. Mol Cell Biol 29, 6128-6139.
    • (2009) Mol Cell Biol , vol.29 , pp. 6128-6139
    • Dorsett, M.1    Schedl, T.2
  • 74
    • 40549126830 scopus 로고    scopus 로고
    • Mitotic regulation by NIMA-related kinases
    • O'Regan L, Blot J, &, Fry AM, (2007) Mitotic regulation by NIMA-related kinases. Cell Div 2, 25.
    • (2007) Cell Div , vol.2 , pp. 25
    • O'Regan, L.1    Blot, J.2    Fry, A.M.3
  • 75
    • 77958457209 scopus 로고    scopus 로고
    • Aurora B kinase controls the targeting of the Astrin-SKAP complex to bioriented kinetochores
    • Schmidt JC, Kiyomitsu T, Hori T, Backer CB, Fukagawa T, &, Cheeseman IM, (2010) Aurora B kinase controls the targeting of the Astrin-SKAP complex to bioriented kinetochores. J Cell Biol 191, 269-280.
    • (2010) J Cell Biol , vol.191 , pp. 269-280
    • Schmidt, J.C.1    Kiyomitsu, T.2    Hori, T.3    Backer, C.B.4    Fukagawa, T.5    Cheeseman, I.M.6
  • 77
    • 77951209602 scopus 로고    scopus 로고
    • Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis
    • Nakano H, Funasaka T, Hashizume C, &, Wong RW, (2010) Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis. J Biol Chem 285, 10841-10849.
    • (2010) J Biol Chem , vol.285 , pp. 10841-10849
    • Nakano, H.1    Funasaka, T.2    Hashizume, C.3    Wong, R.W.4
  • 78
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: A proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • DOI 10.1126/science.1062257
    • Puthalakath H, Villunger A, O'Reilly LA, Beaumont JG, Coultas L, Cheney RE, Huang DC, &, Strasser A, (2001) Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science 293, 1829-1832. (Pubitemid 32845780)
    • (2001) Science , vol.293 , Issue.5536 , pp. 1829-1832
    • Puthalakath, H.1    Villunger, A.2    O'Reilly, L.A.3    Beaumont, J.G.4    Coultas, L.5    Cheney, R.E.6    Huang, D.C.S.7    Strasser, A.8
  • 81
    • 0030613781 scopus 로고    scopus 로고
    • Iκbα physically interacts with a cytoskeleton-associated protein through its signal response domain
    • Crepieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, &, Hiscott J, (1997) I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain. Mol Cell Biol 17, 7375-7385. (Pubitemid 27505966)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.12 , pp. 7375-7385
    • Crepieux, P.1    Kwon, H.2    Leclerc, N.3    Spencer, W.4    Richard, S.5    Lin, R.6    Hiscott, J.7
  • 82
    • 53049109525 scopus 로고    scopus 로고
    • Dynein light chain LC8 negatively regulates NF-kappaB through the redox-dependent interaction with IkappaBalpha
    • Jung Y, Kim H, Min SH, Rhee SG, &, Jeong W, (2008) Dynein light chain LC8 negatively regulates NF-kappaB through the redox-dependent interaction with IkappaBalpha. J Biol Chem 283, 23863-23871.
    • (2008) J Biol Chem , vol.283 , pp. 23863-23871
    • Jung, Y.1    Kim, H.2    Min, S.H.3    Rhee, S.G.4    Jeong, W.5
  • 83
    • 0942287237 scopus 로고    scopus 로고
    • Roles of TRP14, a Thioredoxin-related Protein in Tumor Necrosis Factor-α Signaling Pathways
    • DOI 10.1074/jbc.M307959200
    • Jeong W, Chang TS, Boja ES, Fales HM, &, Rhee SG, (2004) Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways. J Biol Chem 279, 3151-3159. (Pubitemid 38140547)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3151-3159
    • Jeong, W.1    Chang, T.-S.2    Boja, E.S.3    Fales, H.M.4    Rhee, S.G.5
  • 84
    • 73549114248 scopus 로고    scopus 로고
    • GABA(A) receptors, gephyrin and homeostatic synaptic plasticity
    • Tyagarajan SK, &, Fritschy JM, (2010) GABA(A) receptors, gephyrin and homeostatic synaptic plasticity. J Physiol 588, 101-106.
    • (2010) J Physiol , vol.588 , pp. 101-106
    • Tyagarajan, S.K.1    Fritschy, J.M.2
  • 88
    • 0034515174 scopus 로고    scopus 로고
    • The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase
    • DOI 10.1046/j.1365-2443.2000.00374.x
    • Haraguchi K, Satoh K, Yanai H, Hamada F, Kawabuchi M, &, Akiyama T, (2000) The hDLG-associated protein DAP interacts with dynein light chain and neuronal nitric oxide synthase. Genes Cells 5, 905-911. (Pubitemid 32065983)
    • (2000) Genes to Cells , vol.5 , Issue.11 , pp. 905-911
    • Haraguchi, K.1    Satoh, K.2    Yanai, H.3    Hamada, F.4    Kawabuchi, M.5    Akiyama, T.6
  • 89
    • 0034660288 scopus 로고    scopus 로고
    • Interaction of the postsynaptic density-95/guanylate kinase domain- associated protein complex with a light chain of myosin-V and dynein
    • Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, &, Sheng M, (2000) Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein. J Neurosci 20, 4524-4534. (Pubitemid 30396618)
    • (2000) Journal of Neuroscience , vol.20 , Issue.12 , pp. 4524-4534
    • Naisbitt, S.1    Valtschanoff, J.2    Allison, D.W.3    Sala, C.4    Kim, E.5    Craig, A.M.6    Weinberg, R.J.7    Sheng, M.8
  • 90
    • 33748949432 scopus 로고    scopus 로고
    • The postsynaptic density
    • DOI 10.1007/s00441-006-0274-5
    • Boeckers TM, (2006) The postsynaptic density. Cell Tissue Res 326, 409-422. (Pubitemid 44435817)
    • (2006) Cell and Tissue Research , vol.326 , Issue.2 , pp. 409-422
    • Boeckers, T.M.1
  • 91
    • 34848868837 scopus 로고    scopus 로고
    • BS69 is involved in cellular senescence through the p53-p21Cip1 pathway
    • DOI 10.1038/sj.embor.7401049, PII 7401049
    • Zhang W, Chan HM, Gao Y, Poon R, &, Wu Z, (2007) BS69 is involved in cellular senescence through the p53-p21Cip1 pathway. EMBO Rep 8, 952-958. (Pubitemid 47500479)
    • (2007) EMBO Reports , vol.8 , Issue.10 , pp. 952-958
    • Zhang, W.1    Chan, H.M.2    Gao, Y.3    Poon, R.4    Wu, Z.5
  • 92
    • 0038006754 scopus 로고    scopus 로고
    • Nuclear interaction of the dynein light chain LC8a with the TRPS1 transcription factor suppresses the transcriptional repression activity of TRPS1
    • DOI 10.1093/hmg/ddg145
    • Kaiser FJ, Tavassoli K, Van den Bemd GJ, Chang GT, Horsthemke B, Moroy T, &, Ludecke HJ, (2003) Nuclear interaction of the dynein light chain LC8a with the TRPS1 transcription factor suppresses the transcriptional repression activity of TRPS1. Hum Mol Genet 12, 1349-1358. (Pubitemid 36722615)
    • (2003) Human Molecular Genetics , vol.12 , Issue.11 , pp. 1349-1358
    • Kaiser, F.J.1    Tavassoli, K.2    Van Den Bemd, G.-J.3    Chang, G.T.G.4    Horsthemke, B.5    Moroy, T.6    Ludecke, H.-J.7
  • 93
    • 22144449244 scopus 로고    scopus 로고
    • Functional regulation of oestrogen receptor pathway by the dynein light chain 1
    • DOI 10.1038/sj.embor.7400417
    • Rayala SK, den Hollander P, Balasenthil S, Yang Z, Broaddus RR, &, Kumar R, (2005) Functional regulation of oestrogen receptor pathway by the dynein light chain 1. EMBO Rep 6, 538-544. (Pubitemid 40973962)
    • (2005) EMBO Reports , vol.6 , Issue.6 , pp. 538-544
    • Rayala, S.K.1    Den Hollander, P.2    Balasenthil, S.3    Yang, Z.4    Broaddus, R.R.5    Kumar, R.6
  • 95
    • 84860389437 scopus 로고    scopus 로고
    • The association of viral proteins with host cell dynein components during virus infection
    • Merino-Gracia J, García-Mayoral MF, &, Rodriguez-Crespo I, (2011) The association of viral proteins with host cell dynein components during virus infection. FEBS J 278, 2997-3011.
    • (2011) FEBS J , vol.278 , pp. 2997-3011
    • Merino-Gracia, J.1    García-Mayoral, M.F.2    Rodriguez-Crespo, I.3
  • 96
    • 78651390848 scopus 로고    scopus 로고
    • Light chain-dependent self-association of dynein intermediate chain
    • Nyarko A, &, Barbar E, (2011) Light chain-dependent self-association of dynein intermediate chain. J Biol Chem 286, 1556-1566.
    • (2011) J Biol Chem , vol.286 , pp. 1556-1566
    • Nyarko, A.1    Barbar, E.2
  • 98
    • 78651390848 scopus 로고    scopus 로고
    • Light chain-dependent self-association of dynein intermediate chain
    • Nyarko A, &, Barbar E, (2010) Light chain-dependent self-association of dynein intermediate chain. J Biol Chem 286, 1556-1566.
    • (2010) J Biol Chem , vol.286 , pp. 1556-1566
    • Nyarko, A.1    Barbar, E.2
  • 99
    • 77649242804 scopus 로고    scopus 로고
    • Development and application of in vivo molecular traps reveals that dynein light chain occupancy differentially affects dynein-mediated processes
    • Varma D, Dawn A, Ghosh-Roy A, Weil SJ, Ori-McKenney KM, Zhao Y, Keen J, Vallee RB, &, Williams JC, (2010) Development and application of in vivo molecular traps reveals that dynein light chain occupancy differentially affects dynein-mediated processes. Proc Natl Acad Sci USA 107, 3493-3498.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3493-3498
    • Varma, D.1    Dawn, A.2    Ghosh-Roy, A.3    Weil, S.J.4    Ori-Mckenney, K.M.5    Zhao, Y.6    Keen, J.7    Vallee, R.B.8    Williams, J.C.9
  • 101
    • 67649662047 scopus 로고    scopus 로고
    • Egalitarian is a selective RNA-binding protein linking mRNA localization signals to the dynein motor
    • Dienstbier M, Boehl F, Li X, &, Bullock SL, (2009) Egalitarian is a selective RNA-binding protein linking mRNA localization signals to the dynein motor. Genes Dev 23, 1546-1558.
    • (2009) Genes Dev , vol.23 , pp. 1546-1558
    • Dienstbier, M.1    Boehl, F.2    Li, X.3    Bullock, S.L.4
  • 102
  • 103
    • 74749103945 scopus 로고    scopus 로고
    • UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope during nuclear migration
    • Fridolfsson HN, Ly N, Meyerzon M, &, Starr DA, (2010) UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope during nuclear migration. Dev Biol 338, 237-250.
    • (2010) Dev Biol , vol.338 , pp. 237-250
    • Fridolfsson, H.N.1    Ly, N.2    Meyerzon, M.3    Starr, D.A.4
  • 104
    • 0034517593 scopus 로고    scopus 로고
    • LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome
    • DOI 10.1016/S0896-6273(00)00145-8
    • Feng Y, Olson EC, Stukenberg PT, Flanagan LA, Kirschner MW, &, Walsh CA, (2000) LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome. Neuron 28, 665-679. (Pubitemid 32038063)
    • (2000) Neuron , vol.28 , Issue.3 , pp. 665-679
    • Feng, Y.1    Olson, E.C.2    Stukenberg, P.T.3    Flanagan, L.A.4    Kirschner, M.W.5    Walsh, C.A.6
  • 105
    • 34547958546 scopus 로고    scopus 로고
    • NudE and NudEL are required for mitotic progression and are involved in dynein recruitment to kinetochores
    • DOI 10.1083/jcb.200610112
    • Stehman SA, Chen Y, McKenney RJ, &, Vallee RB, (2007) NudE and NudEL are required for mitotic progression and are involved in dynein recruitment to kinetochores. J Cell Biol 178, 583-594. (Pubitemid 47267271)
    • (2007) Journal of Cell Biology , vol.178 , Issue.4 , pp. 583-594
    • Stehman, S.A.1    Chen, Y.2    McKenney, R.J.3    Vallee, R.B.4
  • 106
    • 70450228589 scopus 로고    scopus 로고
    • Regulators of the cytoplasmic dynein motor
    • Kardon JR, &, Vale RD, (2009) Regulators of the cytoplasmic dynein motor. Nat Rev Mol Cell Biol 10, 854-865.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 854-865
    • Kardon, J.R.1    Vale, R.D.2
  • 108
    • 79952114716 scopus 로고    scopus 로고
    • Functional classification of scaffold proteins and related molecules
    • Buday L, &, Tompa P, (2010) Functional classification of scaffold proteins and related molecules. FEBS J 277, 4348-4355.
    • (2010) FEBS J , vol.277 , pp. 4348-4355
    • Buday, L.1    Tompa, P.2
  • 110
    • 0038356539 scopus 로고    scopus 로고
    • Recognition of novel viral sequences that associate with the dynein light chain LC8 identified through a pepscan technique
    • DOI 10.1016/S0014-5793(03)00516-7
    • Martinez-Moreno M, Navarro-Lerida I, Roncal F, Albar JP, Alonso C, Gavilanes F, &, Rodriguez-Crespo I, (2003) Recognition of novel viral sequences that associate with the dynein light chain LC8 identified through a pepscan technique. FEBS Lett 544, 262-267. (Pubitemid 36628074)
    • (2003) FEBS Letters , vol.544 , Issue.1-3 , pp. 262-267
    • Martinez-Moreno, M.1    Navarro-Lerida, I.2    Roncal, F.3    Albar, J.P.4    Alonso, C.5    Gavilanes, F.6    Rodriguez-Crespo, I.7
  • 112
    • 0043185695 scopus 로고    scopus 로고
    • Cyclic AMP- and calmodulin-dependent phosphorylation of 21 and 26 kDa proteins in axoneme is a prerequisite for SAAF-induced motile activation in ascidian spermatozoa
    • DOI 10.1046/j.1440-169X.2000.00489.x
    • Nomura M, Inaba K, &, Morisawa M, (2000) Cyclic AMP- and calmodulin-dependent phosphorylation of 21 and 26 kDa proteins in axoneme is a prerequisite for SAAF-induced motile activation in ascidian spermatozoa. Dev Growth Differ 42, 129-138. (Pubitemid 30202841)
    • (2000) Development Growth and Differentiation , vol.42 , Issue.2 , pp. 129-138
    • Nomura, M.1    Inaba, K.2    Morisawa, M.3
  • 113
  • 114
    • 0035012844 scopus 로고    scopus 로고
    • Rapid selection against truncation mutants in yeast reverse two-hybrid screens
    • Puthalakath H, Strasser A, &, Huang DC, (2001) Rapid selection against truncation mutants in yeast reverse two-hybrid screens. BioTechniques 30, 984-988. (Pubitemid 32429937)
    • (2001) BioTechniques , vol.30 , Issue.5 , pp. 984-988
    • Puthalakath, H.1    Strasser, A.2    Huang, D.C.S.3
  • 115
    • 79955976576 scopus 로고    scopus 로고
    • DYNLL/LC8 controls signal transduction through the Nek9/Nek6 signaling module by regulating Nek6 binding to Nek9
    • Regue L, Sdelci S, Bertran MT, Caelles C, Reverter D, &, Roig J, (2011) DYNLL/LC8 controls signal transduction through the Nek9/Nek6 signaling module by regulating Nek6 binding to Nek9. J Biol Chem 286, 18118-18129.
    • (2011) J Biol Chem , vol.286 , pp. 18118-18129
    • Regue, L.1    Sdelci, S.2    Bertran, M.T.3    Caelles, C.4    Reverter, D.5    Roig, J.6
  • 116
    • 0032509467 scopus 로고    scopus 로고
    • Protein inhibitor of neuronal nitric-oxide synthase, PIN, binds to a 17-amino acid residue fragment of the enzyme
    • Fan JS, Zhang Q, Li M, Tochio H, Yamazaki T, Shimizu M, &, Zhang M, (1998) Protein inhibitor of neuronal nitric-oxide synthase, PIN, binds to a 17-amino acid residue fragment of the enzyme. J Biol Chem 273, 33472-33481.
    • (1998) J Biol Chem , vol.273 , pp. 33472-33481
    • Fan, J.S.1    Zhang, Q.2    Li, M.3    Tochio, H.4    Yamazaki, T.5    Shimizu, M.6    Zhang, M.7
  • 117
    • 0034529440 scopus 로고    scopus 로고
    • Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and Drosophila
    • Herzig RP, Andersson U, &, Scarpulla RC, (2000) Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila. J Cell Sci 113 (Pt 23), 4263-4273. (Pubitemid 32000692)
    • (2000) Journal of Cell Science , vol.113 , Issue.23 , pp. 4263-4273
    • Herzig, R.P.1    Andersson, U.2    Scarpulla, R.C.3
  • 118
    • 0033776043 scopus 로고    scopus 로고
    • Interaction of the rabies virus P protein with the LC8 dynein light chain
    • Raux H, Flamand A, &, Blondel D, (2000) Interaction of the rabies virus P protein with the LC8 dynein light chain. J Virol 74, 10212-10216.
    • (2000) J Virol , vol.74 , pp. 10212-10216
    • Raux, H.1    Flamand, A.2    Blondel, D.3
  • 119
    • 0033775766 scopus 로고    scopus 로고
    • Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein
    • Jacob Y, Badrane H, Ceccaldi PE, &, Tordo N, (2000) Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein. J Virol 74, 10217-10222.
    • (2000) J Virol , vol.74 , pp. 10217-10222
    • Jacob, Y.1    Badrane, H.2    Ceccaldi, P.E.3    Tordo, N.4
  • 120
    • 52149091686 scopus 로고    scopus 로고
    • Cyclic AMP inhibits JNK activation by CREB-mediated induction of c-FLIP(L) and MKP-1, thereby antagonizing UV-induced apoptosis
    • Zhang J, Wang Q, Zhu N, Yu M, Shen B, Xiang J, &, Lin A, (2008) Cyclic AMP inhibits JNK activation by CREB-mediated induction of c-FLIP(L) and MKP-1, thereby antagonizing UV-induced apoptosis. Cell Death Differ 15, 1654-1662.
    • (2008) Cell Death Differ , vol.15 , pp. 1654-1662
    • Zhang, J.1    Wang, Q.2    Zhu, N.3    Yu, M.4    Shen, B.5    Xiang, J.6    Lin, A.7
  • 121
    • 33845972283 scopus 로고    scopus 로고
    • The exchange factor and diacylglycerol receptor RasGRP3 interacts with dynein light chain 1 through its C-terminal domain
    • DOI 10.1074/jbc.M605093200
    • Okamura SM, Oki-Idouchi CE, &, Lorenzo PS, (2006) The exchange factor and diacylglycerol receptor RasGRP3 interacts with dynein light chain 1 through its C-terminal domain. J Biol Chem 281, 36132-36139. (Pubitemid 46041347)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 36132-36139
    • Okamura, S.M.1    Oki-Idouchi, C.E.2    Lorenzo, P.S.3
  • 124
    • 0041384017 scopus 로고    scopus 로고
    • Targeting of incoming retroviral Gag to the centrosome involves a direct interaction with the dynein light chain 8
    • DOI 10.1242/jcs.00613
    • Petit C, Giron ML, Tobaly-Tapiero J, Bittoun P, Real E, Jacob Y, Tordo N, De The H, &, Saib A, (2003) Targeting of incoming retroviral Gag to the centrosome involves a direct interaction with the dynein light chain 8. J Cell Sci 116, 3433-3442. (Pubitemid 37038990)
    • (2003) Journal of Cell Science , vol.116 , Issue.16 , pp. 3433-3442
    • Petit, C.1    Giron, M.-L.2    Tobaly-Tapiero, J.3    Bittoun, P.4    Real, E.5    Jacob, Y.6    Tordo, N.7    De The, H.8    Saib, A.9
  • 125
    • 33644659074 scopus 로고    scopus 로고
    • The sireviruses, a plant-specific lineage of the Ty1/copia retrotransposons, interact with a family of proteins related to dynein light chain 8
    • DOI 10.1104/pp.105.065680
    • Havecker ER, Gao X, &, Voytas DF, (2005) The Sireviruses, a plant-specific lineage of the Ty1/copia retrotransposons, interact with a family of proteins related to dynein light chain 8. Plant Physiol 139, 857-868. (Pubitemid 43907112)
    • (2005) Plant Physiology , vol.139 , Issue.2 , pp. 857-868
    • Havecker, E.R.1    Gao, X.2    Voytas, D.F.3
  • 126
    • 27244435577 scopus 로고    scopus 로고
    • Isolation of a protein interacting with Vfphot1a in guard cells of Vicia faba
    • DOI 10.1104/pp.104.052639
    • Emi T, Kinoshita T, Sakamoto K, Mineyuki Y, &, Shimazaki K, (2005) Isolation of a protein interacting with Vfphot1a in guard cells of Vicia faba. Plant Physiol 138, 1615-1626. (Pubitemid 43142106)
    • (2005) Plant Physiology , vol.138 , Issue.3 , pp. 1615-1626
    • Emi, T.1    Kinoshita, T.2    Sakamoto, K.3    Mineyuki, Y.4    Shimazaki, K.-I.5
  • 127
    • 0037187823 scopus 로고    scopus 로고
    • Protein inhibitor of neuronal nitric oxide synthase interacts with protein kinase A inhibitors
    • DOI 10.1016/S0169-328X(02)00104-3, PII S0169328X02001043
    • Yu J, Yu L, Chen Z, Zheng L, Chen X, Wang X, Ren D, &, Zhao S, (2002) Protein inhibitor of neuronal nitric oxide synthase interacts with protein kinase A inhibitors. Brain Res Mol Brain Res 99, 145-149. (Pubitemid 34442231)
    • (2002) Molecular Brain Research , vol.99 , Issue.2 , pp. 145-149
    • Yu, J.1    Yu, L.2    Chen, Z.3    Zheng, L.4    Chen, X.5    Wang, X.6    Ren, D.7    Zhao, S.8
  • 129
    • 0035844885 scopus 로고    scopus 로고
    • Localization of calmodulin and dynein light chain LC8 in flagellar radial spokes
    • Yang P, Diener DR, Rosenbaum JL, &, Sale WS, (2001) Localization of calmodulin and dynein light chain LC8 in flagellar radial spokes. J Cell Biol 153, 1315-1326.
    • (2001) J Cell Biol , vol.153 , pp. 1315-1326
    • Yang, P.1    Diener, D.R.2    Rosenbaum, J.L.3    Sale, W.S.4
  • 130
    • 33646706386 scopus 로고    scopus 로고
    • spn-F encodes a novel protein that affects oocyte patterning and bristle morphology in Drosophila
    • DOI 10.1242/dev.02319
    • Abdu U, Bar D, &, Schupbach T, (2006) spn-F encodes a novel protein that affects oocyte patterning and bristle morphology in Drosophila. Development 133, 1477-1484. (Pubitemid 43732961)
    • (2006) Development , vol.133 , Issue.8 , pp. 1477-1484
    • Abdu, U.1    Bar, D.2    Schupbach, T.3
  • 132
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • DOI 10.1093/bioinformatics/bti541
    • Dosztanyi Z, Csizmok V, Tompa P, &, Simon I, (2005) IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21, 3433-3434. (Pubitemid 41222453)
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 134
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • DOI 10.1016/S0076-6879(96)66032-7
    • Lupas A, (1996) Prediction and analysis of coiled-coil structures. Methods Enzymol 266, 513-525. (Pubitemid 26165886)
    • (1996) Methods in Enzymology , vol.266 , pp. 513-525
    • Lupas, A.1
  • 135


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