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Volumn 24, Issue 18, 2013, Pages 2885-2893

The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; DNA; ENHANCED GREEN FLUORESCENT PROTEIN; PLAKIN; RAPAMYCIN; RNA; SHORT STOP; SPECTRAPLAKIN; UNCLASSIFIED DRUG;

EID: 84884473113     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-11-0798     Document Type: Article
Times cited : (38)

References (57)
  • 1
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts AS (2001). Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J Biol Chem 276, 2824-2830.
    • (2001) J Biol Chem , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 2
    • 84863452328 scopus 로고    scopus 로고
    • Spectraplakins promote microtubule-mediated axonal growth by functioning as structural microtubule-associated proteins and EB1-dependent +TIPs (tip interacting proteins)
    • Alves-Silva J et al. (2012). Spectraplakins promote microtubule-mediated axonal growth by functioning as structural microtubule-associated proteins and EB1-dependent +TIPs (tip interacting proteins). J Neurosci 32, 9143-9158.
    • (2012) J Neurosci , vol.32 , pp. 9143-9158
    • Alves-Silva, J.1
  • 3
    • 77952328557 scopus 로고    scopus 로고
    • The spectraplakin Short stop is an actin-microtubule cross-linker that contributes to organization of the microtubule network
    • Applewhite DA, Grode KD, Keller D, Zadeh AD, Zadeh A, Slep KC, Rogers SL (2010). The spectraplakin Short stop is an actin-microtubule cross-linker that contributes to organization of the microtubule network. Mol Biol Cell 21, 1714-1724.
    • (2010) Mol Biol Cell , vol.21 , pp. 1714-1724
    • Applewhite, D.A.1    Grode, K.D.2    Keller, D.3    Zadeh, A.D.4    Zadeh, A.5    Slep, K.C.6    Rogers, S.L.7
  • 5
    • 33748195107 scopus 로고    scopus 로고
    • A Rapid, Reversible, and Tunable Method to Regulate Protein Function in Living Cells Using Synthetic Small Molecules
    • DOI 10.1016/j.cell.2006.07.025, PII S0092867406010130
    • Banaszynski LA, Chen L-C, Maynard-Smith LA, Ooi AGL, Wandless TJ (2006). A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules. Cell 126, 995-1004. (Pubitemid 44310772)
    • (2006) Cell , vol.126 , Issue.5 , pp. 995-1004
    • Banaszynski, L.A.1    Chen, L.-c.2    Maynard-Smith, L.A.3    Ooi, A.G.L.4    Wandless, T.J.5
  • 6
    • 16844385435 scopus 로고    scopus 로고
    • Characterization of the FKBP? Rapamycin? FRB ternary complex
    • Banaszynski LA, Liu CW, Wandless TJ (2005). Characterization of the FKBP?rapamycin?FRB ternary complex. J Am Chem Soc 127, 4715-4721.
    • (2005) J Am Chem Soc , vol.127 , pp. 4715-4721
    • Banaszynski, L.A.1    Liu, C.W.2    Wandless, T.J.3
  • 7
    • 84860857201 scopus 로고    scopus 로고
    • Activation of moesin, a protein that links actin cytoskeleton to the plasma membrane, occurs by phosphatidylinositol 4,5-bisphosphate (PIP2) binding sequentially to two sites and releasing an autoinhibitory linker
    • Ben-Aissa K, Patino-Lopez G, Belkina NV, Maniti O, Rosales T, Hao J-J, Kruhlak MJ, Knutson JR, Picart C, Shaw S (2012). Activation of moesin, a protein that links actin cytoskeleton to the plasma membrane, occurs by phosphatidylinositol 4,5-bisphosphate (PIP2) binding sequentially to two sites and releasing an autoinhibitory linker. J Biol Chem 287, 16311-16323.
    • (2012) J Biol Chem , vol.287 , pp. 16311-16323
    • Ben-Aissa, K.1    Patino-Lopez, G.2    Belkina, N.V.3    Maniti, O.4    Rosales, T.5    Hao, J.-J.6    Kruhlak, M.J.7    Knutson, J.R.8    Picart, C.9    Shaw, S.10
  • 8
    • 0030588594 scopus 로고    scopus 로고
    • Cloning and characterization of mouse ACF7, a novel member of the dystonin subfamily of actin binding proteins
    • DOI 10.1006/geno.1996.0587
    • Bernier G, Mathieu M, De Repentigny Y, Vidal SM, Kothary R (1996). Cloning and characterization of mouse ACF7, a novel member of the dystonin subfamily of actin binding proteins. Genomics 38, 19-29. (Pubitemid 26423909)
    • (1996) Genomics , vol.38 , Issue.1 , pp. 19-29
    • Bernier, G.1    Mathieu, M.2    De Repentigny, Y.3    Vidal, S.M.4    Kothary, R.5
  • 10
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • DOI 10.1111/j.1365-2818.2006.01706.x
    • Bolte S, Cordelières FP (2006). A guided tour into subcellular colocalization analysis in light microscopy. J Microsc 224, 213-232. (Pubitemid 46010930)
    • (2006) Journal of Microscopy , vol.224 , Issue.3 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2
  • 11
    • 67349288068 scopus 로고    scopus 로고
    • Context-specific requirements of functional domains of the Spectraplakin Short stop in vivo
    • Bottenberg W, Sánchez-Soriano N, Alves-Silva J, Hahn I, Mende M, Prokop A (2009). Context-specific requirements of functional domains of the Spectraplakin Short stop in vivo. Mech Dev 126, 489-502.
    • (2009) Mech Dev , vol.126 , pp. 489-502
    • Bottenberg, W.1    Sánchez-Soriano, N.2    Alves-Silva, J.3    Hahn, I.4    Mende, M.5    Prokop, A.6
  • 14
    • 34447130835 scopus 로고    scopus 로고
    • 2+- binding helix-loop-helix EF-hand motifs
    • DOI 10.1042/BJ20070255
    • Gifford JL, Walsh MP, Vogel HJ (2007). Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs. Biochem J 405, 199-221. (Pubitemid 47075156)
    • (2007) Biochemical Journal , vol.405 , Issue.2 , pp. 199-221
    • Gifford, J.L.1    Walsh, M.P.2    Vogel, H.J.3
  • 15
    • 0034750458 scopus 로고    scopus 로고
    • MACF1 gene structure: A hybrid of plectin and dystrophin
    • DOI 10.1007/s00335-001-3037-3
    • Gong TW, Besirli CG, Lomax MI (2001). MACF1 gene structure: a hybrid of plectin and dystrophin. Mamm Genome 12, 852-861. (Pubitemid 33022284)
    • (2001) Mammalian Genome , vol.12 , Issue.11 , pp. 852-861
    • Gong, T.-W.L.1    Besirli, C.G.2    Lomax, M.I.3
  • 16
    • 77957340554 scopus 로고    scopus 로고
    • Microtubule actin crosslinking factor 1 regulates the Balbiani body and animal-vegetal polarity of the zebrafish oocyte
    • Gupta T, Marlow FL, Ferriola D, Mackiewicz K, Dapprich J, Monos D, Mullins MC (2010). Microtubule actin crosslinking factor 1 regulates the Balbiani body and animal-vegetal polarity of the zebrafish oocyte. PLoS Genet 6, e1001073.
    • (2010) PLoS Genet , vol.6
    • Gupta, T.1    Marlow, F.L.2    Ferriola, D.3    Mackiewicz, K.4    Dapprich, J.5    Monos, D.6    Mullins, M.C.7
  • 17
    • 67650627616 scopus 로고    scopus 로고
    • An EB1-binding motif acts as a microtubule tip localization signal
    • Honnappa S et al. (2009). An EB1-binding motif acts as a microtubule tip localization signal. Cell 138, 366-376.
    • (2009) Cell , vol.138 , pp. 366-376
    • Honnappa, S.1
  • 18
    • 33846332690 scopus 로고    scopus 로고
    • Structural Analysis of the Plakin Domain of Bullous Pemphigoid Antigen1 (BPAG1) Suggests that Plakins Are Members of the Spectrin Superfamily
    • DOI 10.1016/j.jmb.2006.11.036, PII S0022283606015762
    • Jefferson JJ, Ciatto C, Shapiro L, Liem RKH (2007). Structural analysis of the plakin domain of bullous pemphigoid antigen1 (BPAG1) suggests that plakins are members of the spectrin superfamily. J Mol Biol 366, 244-257. (Pubitemid 46123339)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.1 , pp. 244-257
    • Jefferson, J.J.1    Ciatto, C.2    Shapiro, L.3    Liem, R.K.H.4
  • 20
    • 80051633233 scopus 로고    scopus 로고
    • The structure of the kinesin-1 motor-tail complex reveals the mechanism of autoinhibition
    • Kaan HYK, Hackney DD, Kozielski F (2011). The structure of the kinesin-1 motor-tail complex reveals the mechanism of autoinhibition. Science 333, 883-885.
    • (2011) Science , vol.333 , pp. 883-885
    • Kaan, H.Y.K.1    Hackney, D.D.2    Kozielski, F.3
  • 21
    • 84868688221 scopus 로고    scopus 로고
    • Calcium tips the balance: A microtubule plus end to lattice binding switch operates in the carboxyl terminus of BPAG1n4
    • Kapur M, Wang W, Maloney MT, Millan I, Lundin VF, Tran T-A, Yang Y (2012). Calcium tips the balance: a microtubule plus end to lattice binding switch operates in the carboxyl terminus of BPAG1n4. EMBO Rep 13, 1021-1029.
    • (2012) EMBO Rep , vol.13 , pp. 1021-1029
    • Kapur, M.1    Wang, W.2    Maloney, M.T.3    Millan, I.4    Lundin, V.F.5    Tran, T.-A.6    Yang, Y.7
  • 22
    • 48249132926 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells
    • Kerppola TK (2008). Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annu Rev Biophys 37, 465-487.
    • (2008) Annu Rev Biophys , vol.37 , pp. 465-487
    • Kerppola, T.K.1
  • 23
    • 70349373396 scopus 로고    scopus 로고
    • Visualization of molecular interactions using bimolecular fluorescence complementation analysis: Characteristics of protein fragment complementation
    • Kerppola TK (2009). Visualization of molecular interactions using bimolecular fluorescence complementation analysis: characteristics of protein fragment complementation. Chem Soc Rev 38, 2876-2886.
    • (2009) Chem Soc Rev , vol.38 , pp. 2876-2886
    • Kerppola, T.K.1
  • 25
    • 0344845405 scopus 로고    scopus 로고
    • ACF7: An essential integrator of microtubule dynamics
    • DOI 10.1016/S0092-8674(03)00813-4
    • Kodama A, Karakesisoglou I, Wong E, Vaezi A, Fuchs E (2003). ACF7: an essential integrator of microtubule dynamics. Cell 115, 343-354. (Pubitemid 37487707)
    • (2003) Cell , vol.115 , Issue.3 , pp. 343-354
    • Kodama, A.1    Karakesisoglou, I.2    Wong, E.3    Vaezi, A.4    Fuchs, E.5
  • 26
    • 7444232111 scopus 로고    scopus 로고
    • Independent movement, dimerization and stability of tandem repeats of chicken brain α-spectrin
    • DOI 10.1016/j.jmb.2004.09.019, PII S0022283604011489
    • Kusunoki H, Minasov G, Macdonald RI, Mondrag?n A (2004). Independent movement, dimerization and stability of tandem repeats of chicken brain ?-spectrin. J Mol Biol 344, 495-511. (Pubitemid 39441220)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.2 , pp. 495-511
    • Kusunoki, H.1    Minasov, G.2    MacDonald, R.I.3    Mondragon, A.4
  • 28
    • 53049106033 scopus 로고    scopus 로고
    • Quantitative analysis of microtubule dynamics during adhesion-mediated growth cone guidance
    • Lee AC, Suter DM (2008). Quantitative analysis of microtubule dynamics during adhesion-mediated growth cone guidance. Dev Neurobiol 68, 1363-1377.
    • (2008) Dev Neurobiol , vol.68 , pp. 1363-1377
    • Lee, A.C.1    Suter, D.M.2
  • 29
    • 77955119964 scopus 로고    scopus 로고
    • Phosphorylation controls autoinhibition of cytoplasmic linker protein-170
    • Lee H-S et al. (2010). Phosphorylation controls autoinhibition of cytoplasmic linker protein-170. Mol Biol Cell 21, 2661-2673.
    • (2010) Mol Biol Cell , vol.21 , pp. 2661-2673
    • Lee, H.-S.1
  • 30
    • 0034143380 scopus 로고    scopus 로고
    • Short stop is allelic to kakapo, and encodes rod-like cytoskeletal- associated proteins required for axon extension
    • Lee S, Harris KL, Whitington PM, Kolodziej PA (2000). Short stop is allelic to kakapo, and encodes rod-like cytoskeletal-associated proteins required for axon extension. J Neurosci 20, 1096-1108. (Pubitemid 30220467)
    • (2000) Journal of Neuroscience , vol.20 , Issue.3 , pp. 1096-1108
    • Lee, S.1    Harris, K.-L.2    Whitington, P.M.3    Kolodziej, P.A.4
  • 31
    • 0036339710 scopus 로고    scopus 로고
    • The plakin short stop and the RhoA GTPase are required for E-cadherin-dependent apical surface remodeling during tracheal tube fusion
    • Lee S, Kolodziej PA (2002a). The plakin Short Stop and the RhoA GTPase are required for E-cadherin-dependent apical surface remodeling during tracheal tube fusion. Development 129, 1509-1520. (Pubitemid 34874171)
    • (2002) Development , vol.129 , Issue.6 , pp. 1509-1520
    • Lee, S.1    Kolodziej, P.A.2
  • 32
    • 0036332841 scopus 로고    scopus 로고
    • Short stop provides an essential link between F-actin and microtubules during axon extension
    • Lee S, Kolodziej PA (2002b). Short Stop provides an essential link between F-actin and microtubules during axon extension. Development 129, 1195-1204. (Pubitemid 34874142)
    • (2002) Development , vol.129 , Issue.5 , pp. 1195-1204
    • Lee, S.1    Kolodziej, P.A.2
  • 33
    • 0043202969 scopus 로고    scopus 로고
    • The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • DOI 10.1016/S0960-9822(03)00540-2
    • Li F, Higgs HN (2003). The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr Biol 13, 1335-1340. (Pubitemid 36953308)
    • (2003) Current Biology , vol.13 , Issue.15 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 34
    • 21644453158 scopus 로고    scopus 로고
    • Spectraplakins and nesprins, giant spectrin repeat proteins participating in the organization of the cytoskeleton and the nuclear envelope
    • Määttä A, Hutchison CJ, Watson MD (2004). Spectraplakins and nesprins, giant spectrin repeat proteins participating in the organization of the cytoskeleton and the nuclear envelope. Symp Soc Exp Biol 2004, 265-277.
    • (2004) Symp Soc Exp Biol , vol.2004 , pp. 265-277
    • Määttä, A.1    Hutchison, C.J.2    Watson, M.D.3
  • 35
    • 2442505592 scopus 로고    scopus 로고
    • The Abl-related gene (Arg) requires its F-actin-microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion
    • DOI 10.1083/jcb.200308055
    • Miller AL, Wang Y, Mooseker MS, Koleske AJ (2004). The Abl-related gene (Arg) requires its F-actin-microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion. J Cell Biol 165, 407-419. (Pubitemid 38649915)
    • (2004) Journal of Cell Biology , vol.165 , Issue.3 , pp. 407-419
    • Miller, A.L.1    Wang, Y.2    Mooseker, M.S.3    Koleske, A.J.4
  • 37
    • 42049102564 scopus 로고    scopus 로고
    • Culture of Drosophila S2 cells and their use for RNAi-mediated loss-of-function studies and immunofluorescence microscopy
    • DOI 10.1038/nprot.2008.18, PII NPROT.2008.18
    • Rogers SL, Rogers GC (2008). Culture of Drosophila S2 cells and their use for RNAi-mediated loss-of-function studies and immunofluorescence microscopy. Nat Protoc 3, 606-611. (Pubitemid 351516756)
    • (2008) Nature Protocols , vol.3 , Issue.4 , pp. 606-611
    • Rogers, S.L.1    Rogers, G.C.2
  • 38
    • 0037009077 scopus 로고    scopus 로고
    • Drosophila EB1 is important for proper assembly, dynamics, and positioning of the mitotic spindle
    • DOI 10.1083/jcb.200202032
    • Rogers SL, Rogers GC, Sharp DJ, Vale RD (2002). Drosophila EB1 is important for proper assembly, dynamics, and positioning of the mitotic spindle. J Cell Biol 158, 873-884. (Pubitemid 35001079)
    • (2002) Journal of Cell Biology , vol.158 , Issue.5 , pp. 873-884
    • Rogers, S.L.1    Rogers, G.C.2    Sharp, D.J.3    Vale, R.D.4
  • 39
    • 0141641125 scopus 로고    scopus 로고
    • Maintaining epithelial integrity: A function for gigantic spectraplakin isoforms in adherens junctions
    • DOI 10.1083/jcb.200307089
    • Röper K, Brown NH (2003). Maintaining epithelial integrity: a function for gigantic spectraplakin isoforms in adherens junctions. J Cell Biol 162, 1305-1315. (Pubitemid 37210886)
    • (2003) Journal of Cell Biology , vol.162 , Issue.7 , pp. 1305-1315
    • Roper, K.1    Brown, N.H.2
  • 40
    • 0037112997 scopus 로고    scopus 로고
    • The 'spectraplakins': Cytoskeletal giants with characteristics of both spectrin and plakin families
    • DOI 10.1242/jcs.00157
    • Röper K, Gregory SL, Brown NH (2002). The "spectraplakins" : cytoskeletal giants with characteristics of both spectrin and plakin families. J Cell Sci 115, 4215-4225. (Pubitemid 35460693)
    • (2002) Journal of Cell Science , vol.115 , Issue.22 , pp. 4215-4225
    • Roper, K.1    Gregory, S.L.2    Brown, N.H.3
  • 42
    • 0042882289 scopus 로고    scopus 로고
    • Drosophila pod-1 crosslinks both actin and microtubules and controls the targeting of axons
    • DOI 10.1016/S0896-6273(03)00508-7
    • Rothenberg ME, Rogers SL, Vale RD, Jan LY, Jan Y-N (2003). Drosophila pod-1 crosslinks both actin and microtubules and controls the targeting of axons. Neuron 39, 779-791. (Pubitemid 37088090)
    • (2003) Neuron , vol.39 , Issue.5 , pp. 779-791
    • Rothenberg, M.E.1    Rogers, S.L.2    Vale, R.D.3    Jan, L.Y.4    Jan, Y.-N.5
  • 43
    • 0037043342 scopus 로고    scopus 로고
    • Dual-wavelength fluorescent speckle microscopy reveals coupling of microtubule and actin movements in migrating cells
    • Salmon WC, Adams MC, Waterman-Storer CM (2002). Dual-wavelength fluorescent speckle microscopy reveals coupling of microtubule and actin movements in migrating cells. J Cell Biol 158, 31-37.
    • (2002) J Cell Biol , vol.158 , pp. 31-37
    • Salmon, W.C.1    Adams, M.C.2    Waterman-Storer, C.M.3
  • 44
    • 0037043343 scopus 로고    scopus 로고
    • Filopodia and actin arcs guide the assembly and transport of two populations of microtubules with unique dynamic parameters in neuronal growth cones
    • Schaefer AW, Kabir N, Forscher P (2002). Filopodia and actin arcs guide the assembly and transport of two populations of microtubules with unique dynamic parameters in neuronal growth cones. J Cell Biol 158, 139-152.
    • (2002) J Cell Biol , vol.158 , pp. 139-152
    • Schaefer, A.W.1    Kabir, N.2    Forscher, P.3
  • 45
    • 13944255721 scopus 로고    scopus 로고
    • Structural determinants for EB1-mediated recruitment of APC and spectraplakins to the microtubule plus end
    • DOI 10.1083/jcb.200410114
    • Slep KC, Rogers SL, Elliott SL, Ohkura H, Kolodziej PA, Vale RD (2005). Structural determinants for EB1-mediated recruitment of APC and spectraplakins to the microtubule plus end. J Cell Biol 168, 587-598. (Pubitemid 40271024)
    • (2005) Journal of Cell Biology , vol.168 , Issue.4 , pp. 587-598
    • Slep, K.C.1    Rogers, S.L.2    Elliott, S.L.3    Ohkura, H.4    Kolodziej, P.A.5    Vale, R.D.6
  • 46
    • 34748862943 scopus 로고    scopus 로고
    • Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170, and EB1
    • DOI 10.1016/j.molcel.2007.07.023, PII S1097276507004960
    • Slep KC, Vale RD (2007). Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1. Mol Cell 27, 976-991. (Pubitemid 47488185)
    • (2007) Molecular Cell , vol.27 , Issue.6 , pp. 976-991
    • Slep, K.C.1    Vale, R.D.2
  • 47
    • 34249685610 scopus 로고    scopus 로고
    • Plakins in development and disease
    • DOI 10.1016/j.yexcr.2007.03.039, PII S0014482707001097
    • Sonnenberg A, Liem RKH (2007). Plakins in development and disease. Exp Cell Res 313, 2189-2203. (Pubitemid 46842974)
    • (2007) Experimental Cell Research , vol.313 , Issue.10 , pp. 2189-2203
    • Sonnenberg, A.1    Liem, R.K.H.2
  • 48
    • 0032583165 scopus 로고    scopus 로고
    • Kakapo, a novel cytoskeletal-associated protein is essential for the restricted localization of the neuregulin-like factor, vein, at the muscle- tendon junction site
    • DOI 10.1083/jcb.143.5.1259
    • Strumpf D, Volk T (1998). Kakapo, a novel cytoskeletal-associated protein is essential for the restricted localization of the neuregulin-like factor, Vein, at the muscle-tendon junction site. J Cell Biol 143, 1259-1270. (Pubitemid 28559827)
    • (1998) Journal of Cell Biology , vol.143 , Issue.5 , pp. 1259-1270
    • Strumpf, D.1    Volk, T.2
  • 50
    • 84862603775 scopus 로고    scopus 로고
    • Spectraplakins: Master orchestrators of cytoskeletal dynamics
    • Suozzi KC, Wu X, Fuchs E (2012). Spectraplakins: master orchestrators of cytoskeletal dynamics. J Cell Biol 197, 465-475.
    • (2012) J Cell Biol , vol.197 , pp. 465-475
    • Suozzi, K.C.1    Wu, X.2    Fuchs, E.3
  • 51
  • 52
    • 0038457895 scopus 로고    scopus 로고
    • Regulation of leading edge microtubule and actin dynamics downstream of Rac1
    • DOI 10.1083/jcb.200303082
    • Wittmann T, Bokoch GM, Waterman-Storer CM (2003). Regulation of leading edge microtubule and actin dynamics downstream of Rac1. J Cell Biol 161, 845-851. (Pubitemid 36718418)
    • (2003) Journal of Cell Biology , vol.161 , Issue.5 , pp. 845-851
    • Wittmann, T.1    Bokoch, G.M.2    Waterman-Storer, C.M.3
  • 53
    • 67649383550 scopus 로고    scopus 로고
    • The kinesin-1 tail conformationally restricts the nucleotide pocket
    • Wong YL, Dietrich KA, Naber N, Cooke R, Rice SE (2009). The kinesin-1 tail conformationally restricts the nucleotide pocket. Biophys J 96, 2799-2807.
    • (2009) Biophys J , vol.96 , pp. 2799-2807
    • Wong, Y.L.1    Dietrich, K.A.2    Naber, N.3    Cooke, R.4    Rice, S.E.5
  • 54
    • 77955379085 scopus 로고    scopus 로고
    • Kinesin's light chains inhibit the head- and microtubule-binding activity of its tail
    • Wong YL, Rice SE (2010). Kinesin's light chains inhibit the head- and microtubule-binding activity of its tail. Proc Natl Acad Sci USA 107, 11781-11786.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 11781-11786
    • Wong, Y.L.1    Rice, S.E.2
  • 55
    • 52949098421 scopus 로고    scopus 로고
    • ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity
    • Wu X, Kodama A, Fuchs E (2008). ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity. Cell 135, 137-148.
    • (2008) Cell , vol.135 , pp. 137-148
    • Wu, X.1    Kodama, A.2    Fuchs, E.3
  • 56
    • 79551675515 scopus 로고    scopus 로고
    • Skin stem cells orchestrate directional migration by regulating microtubule-ACF7 connections through GSK3?
    • Wu X, Shen Q-T, Oristian DS, Lu CP, Zheng Q, Wang H-W, Fuchs E (2011). Skin stem cells orchestrate directional migration by regulating microtubule-ACF7 connections through GSK3?. Cell 144, 341-352.
    • (2011) Cell , vol.144 , pp. 341-352
    • Wu, X.1    Shen, Q.-T.2    Oristian, D.S.3    Lu, C.P.4    Zheng, Q.5    Wang, H.-W.6    Fuchs, E.7
  • 57
    • 0032708680 scopus 로고    scopus 로고
    • Diversity of conformational states and changes within the EF-hand protein superfamily
    • DOI 10.1002/(SICI)1097-0134(19991115)37:3<499::AID-PROT17>3.0.CO;2- Y
    • Yap KL, Ames JB, Swindells MB, Ikura M (1999). Diversity of conformational states and changes within the EF-hand protein superfamily. Proteins 37, 499-507. (Pubitemid 29519739)
    • (1999) Proteins: Structure, Function and Genetics , vol.37 , Issue.3 , pp. 499-507
    • Yap, K.L.1    Ames, J.B.2    Swindells, M.B.3    Ikura, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.