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Volumn 47, Issue 23, 2008, Pages 6251-6259

NMR characterization of structural and dynamics perturbations due to a single point mutation in Drosophila DLC8 dimer: Functional implications

Author keywords

[No Author keywords available]

Indexed keywords

ALUMINUM; AMINES; COMPLEXATION; CRYSTAL ATOMIC STRUCTURE; CRYSTAL STRUCTURE; DYNAMICS; MECHANICS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PERTURBATION TECHNIQUES; TARGETS;

EID: 44949253210     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800531g     Document Type: Article
Times cited : (11)

References (45)
  • 1
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: An ancient motor protein involved in multiple modes of transport
    • Vallee, R. B., Williams, J. C., Varma, D., and Barnhart, L. E. (2004) Dynein: An ancient motor protein involved in multiple modes of transport. J. Neurobiol. 58, 189-200.
    • (2004) J. Neurobiol , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 2
    • 0032005975 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins in organelle transport and cell division
    • Hirokawa, N., Noda, Y., and Okada, Y. (1998) Kinesin and dynein superfamily proteins in organelle transport and cell division. Curr. Opin. Cell Biol. 10, 60-73.
    • (1998) Curr. Opin. Cell Biol , vol.10 , pp. 60-73
    • Hirokawa, N.1    Noda, Y.2    Okada, Y.3
  • 3
    • 0028170819 scopus 로고
    • DYNEINS: Molecular structure and cellular function
    • Holzbaur, E. L., and Vallee, R. B. (1994) DYNEINS: molecular structure and cellular function. Annu. Rev. Cell Biol. 10, 339-372.
    • (1994) Annu. Rev. Cell Biol , vol.10 , pp. 339-372
    • Holzbaur, E.L.1    Vallee, R.B.2
  • 4
    • 13844275634 scopus 로고    scopus 로고
    • Dynein cargo gets its groove back
    • Pfister, K. K. (2005) Dynein cargo gets its groove back. Structure (London) 13, 172-173.
    • (2005) Structure (London) , vol.13 , pp. 172-173
    • Pfister, K.K.1
  • 5
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallée, R. B., and Sheetz, M. P. (1996) Targeting of motor proteins. Science 271, 1539-1544.
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallée, R.B.1    Sheetz, M.P.2
  • 6
    • 31344449610 scopus 로고    scopus 로고
    • pH driven conformational dynamics and dimer-to-monomer transition in DLC8
    • Mohan, P. M., Barve, M., Chatterjee, A., and Hosur, R. V. (2006) pH driven conformational dynamics and dimer-to-monomer transition in DLC8. Protein Sci. 15, 335-342.
    • (2006) Protein Sci , vol.15 , pp. 335-342
    • Mohan, P.M.1    Barve, M.2    Chatterjee, A.3    Hosur, R.V.4
  • 7
    • 0035852805 scopus 로고    scopus 로고
    • Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein
    • Barbar, E., Kleinman, B., Imhoff, D., Li, M., Hays, T. S., and Hare, M. (2001) Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein. Biochemistry 40, 1596-1605.
    • (2001) Biochemistry , vol.40 , pp. 1596-1605
    • Barbar, E.1    Kleinman, B.2    Imhoff, D.3    Li, M.4    Hays, T.S.5    Hare, M.6
  • 9
    • 0142039800 scopus 로고    scopus 로고
    • Structure of the monomeric 8-kDa dynein light chain and mechanism of the domain-swapped dimer assembly
    • Wang, W., Lo, K. W., Kan, H. M., Fan, J. S., and 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.
    • (2003) J. Biol. Chem , vol.278 , pp. 41491-41499
    • Wang, W.1    Lo, K.W.2    Kan, H.M.3    Fan, J.S.4    Zhang, M.5
  • 10
    • 0029858301 scopus 로고    scopus 로고
    • PIN: An associated protein inhibitor of neuronal nitric oxide synthase
    • Jaffrey, S. R., and Snyder, S. H. (1996) PIN: an associated protein inhibitor of neuronal nitric oxide synthase. Science 274, 774-777.
    • (1996) Science 274 , pp. 774-777
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 11
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath, H., Huang, D. C., O'Reilly, L. A., King, S. M., and 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.
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 14
    • 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, D. W., Sala, C., Kim, E., Craig, A. M., Weinberg, R. J., and 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.
    • (2000) J. Neurosci , vol.20 , 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
  • 15
    • 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
    • Lo, K. W., Kan, H. M., Chan, L. N., Xu, W. G., Wang, K. P., Wu, Z., Sheng, M., and 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.
    • (2005) J. Biol. Chem , vol.280 , pp. 8172-8179
    • Lo, K.W.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
  • 16
    • 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., and 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
  • 17
    • 0035958082 scopus 로고    scopus 로고
    • The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif
    • Lo, K. W., Naisbitt, S., Fan, J. S., Sheng, M., and 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
  • 19
    • 12844272185 scopus 로고    scopus 로고
    • Dynein light chain 1 phosphorylation controls macropinocytosis
    • Yang, Z., Vadlamudi, R. K., and Kumar, R. (2005) Dynein light chain 1 phosphorylation controls macropinocytosis. J. Biol. Chem. 280, 654-659.
    • (2005) J. Biol. Chem , vol.280 , pp. 654-659
    • Yang, Z.1    Vadlamudi, R.K.2    Kumar, R.3
  • 20
    • 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, S. K., Chen, M., Ma, J., Zhang, M., and 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
  • 21
    • 34447127515 scopus 로고    scopus 로고
    • Potential role for phosphorylation in differential regulation of the assembly of dynein light chains
    • Song, Y., Benison, G., Nyarko, A., Hays, T. S., and Barbar, E. (2007) Potential role for phosphorylation in differential regulation of the assembly of dynein light chains. J. Biol. Chem. 282, 17272-17279.
    • (2007) J. Biol. Chem , vol.282 , pp. 17272-17279
    • Song, Y.1    Benison, G.2    Nyarko, A.3    Hays, T.S.4    Barbar, E.5
  • 22
    • 34250817437 scopus 로고    scopus 로고
    • Mutational analysis of active site residues in the Staphylococcus aureus transpeptidase SrtA
    • Frankel, B. A., Tong, Y., Bentley, M. L., Fitzgerald, M. C., and McCafferty, D. G. (2007) Mutational analysis of active site residues in the Staphylococcus aureus transpeptidase SrtA. Biochemistry 46, 7269-7278.
    • (2007) Biochemistry , vol.46 , pp. 7269-7278
    • Frankel, B.A.1    Tong, Y.2    Bentley, M.L.3    Fitzgerald, M.C.4    McCafferty, D.G.5
  • 24
    • 36548999391 scopus 로고    scopus 로고
    • Predicting the effect of a point mutation on a protein fold: The villin and advillin headpieces and their Pro62Ala mutants
    • Piana, S., Laio, A., Marinelli, F., Van, T. M., Bourry, D., Ampe, C., and Martins, J. C. (2008) Predicting the effect of a point mutation on a protein fold: the villin and advillin headpieces and their Pro62Ala mutants. J. Mol. Biol. 375, 460-470.
    • (2008) J. Mol. Biol , vol.375 , pp. 460-470
    • Piana, S.1    Laio, A.2    Marinelli, F.3    Van, T.M.4    Bourry, D.5    Ampe, C.6    Martins, J.C.7
  • 25
    • 35248900503 scopus 로고    scopus 로고
    • Unfolding energetics and conformational stability of DLC8 monomer
    • Krishna Mohan, P. M. (2007) Unfolding energetics and conformational stability of DLC8 monomer. Biochimie 89, 1409-1415.
    • (2007) Biochimie , vol.89 , pp. 1409-1415
    • Krishna Mohan, P.M.1
  • 26
    • 34547692741 scopus 로고    scopus 로고
    • A single Gly114Arg mutation stabilizes the hexameric subunit assembly and changes the substrate specificity of halo-archaeal nucleoside diphosphate kinase
    • Ishibashi, M., Tatsuda, S., Izutsu, K., Kumeda, K., Arakawa, T., and Tokunaga, M. (2007) A single Gly114Arg mutation stabilizes the hexameric subunit assembly and changes the substrate specificity of halo-archaeal nucleoside diphosphate kinase. FEBS Lett. 581, 4073-4079.
    • (2007) FEBS Lett , vol.581 , pp. 4073-4079
    • Ishibashi, M.1    Tatsuda, S.2    Izutsu, K.3    Kumeda, K.4    Arakawa, T.5    Tokunaga, M.6
  • 27
    • 0142169165 scopus 로고    scopus 로고
    • Crystal structures of engrailed homeodomain mutants: Implications for stability and dynamics
    • Stollar, E. J., Mayor, U., Lovell, S. C., Federici, L., Freund, S. M., Fersht, A. R., and Luisi, B. F. (2003) Crystal structures of engrailed homeodomain mutants: implications for stability and dynamics. J. Biol. Chem. 278, 43699-43708.
    • (2003) J. Biol. Chem , vol.278 , pp. 43699-43708
    • Stollar, E.J.1    Mayor, U.2    Lovell, S.C.3    Federici, L.4    Freund, S.M.5    Fersht, A.R.6    Luisi, B.F.7
  • 28
    • 34547650465 scopus 로고    scopus 로고
    • A novel tripartite motif involved in aquaporin topogenesis, monomer folding and tetramerization
    • Buck, T. M., Wagner, J., Grund, S., and Skach, W. R. (2007) A novel tripartite motif involved in aquaporin topogenesis, monomer folding and tetramerization. Nat. Struct. Mol. Biol. 14, 762-769.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 762-769
    • Buck, T.M.1    Wagner, J.2    Grund, S.3    Skach, W.R.4
  • 29
    • 33847118925 scopus 로고    scopus 로고
    • Dimer dissociation and unfolding mechanism of coagulation factor XI apple 4 domain: Spectroscopic and mutational analysis
    • Riley, P. W., Cheng, H., Samuel, D., Roder, H., and Walsh, P. N. (2007) Dimer dissociation and unfolding mechanism of coagulation factor XI apple 4 domain: spectroscopic and mutational analysis. J. Mol. Biol. 367, 558-573.
    • (2007) J. Mol. Biol , vol.367 , pp. 558-573
    • Riley, P.W.1    Cheng, H.2    Samuel, D.3    Roder, H.4    Walsh, P.N.5
  • 30
    • 27444442808 scopus 로고    scopus 로고
    • Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation
    • Nyarko, A., Cochrun, L., Norwood, S., Pursifull, N., Voth, A., and 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.
    • (2005) Biochemistry , vol.44 , pp. 14248-14255
    • Nyarko, A.1    Cochrun, L.2    Norwood, S.3    Pursifull, N.4    Voth, A.5    Barbar, E.6
  • 33
    • 27644503431 scopus 로고    scopus 로고
    • An experimental investigation of conformational fluctuations in proteins G and L
    • Tunnicliffe, R. B., Waby, J. L., Williams, R. J., and Williamson, M. P. (2005) An experimental investigation of conformational fluctuations in proteins G and L. Structure (London) 13, 1677-1684.
    • (2005) Structure (London) , vol.13 , pp. 1677-1684
    • Tunnicliffe, R.B.1    Waby, J.L.2    Williams, R.J.3    Williamson, M.P.4
  • 34
    • 0025904730 scopus 로고
    • Defining solution conformations of small linear peptides
    • Dyson, H. J., and Wright, P. E. (1991) Defining solution conformations of small linear peptides. Annu. Rev. Biophys. Biophys. Chem. 20, 519-538.
    • (1991) Annu. Rev. Biophys. Biophys. Chem , vol.20 , pp. 519-538
    • Dyson, H.J.1    Wright, P.E.2
  • 36
    • 33847660005 scopus 로고    scopus 로고
    • NMR insights into dynamics regulated target binding of DLC8 dimer
    • Krishna Mohan, P. M., and Hosur, R. V. (2007) NMR insights into dynamics regulated target binding of DLC8 dimer. Biochem. Biophys. Res. Commun. 355, 950-955.
    • (2007) Biochem. Biophys. Res. Commun , vol.355 , pp. 950-955
    • Krishna Mohan, P.M.1    Hosur, R.V.2
  • 37
    • 0242362190 scopus 로고    scopus 로고
    • Many residues in cytochrome c populate alternative states under equilibrium conditions
    • Williamson, M. P. (2003) Many residues in cytochrome c populate alternative states under equilibrium conditions. Proteins 53, 731-739.
    • (2003) Proteins , vol.53 , pp. 731-739
    • Williamson, M.P.1
  • 38
    • 39749139381 scopus 로고    scopus 로고
    • Differential native state ruggedness of the two Ca2+-binding domains in a Ca2+ sensor protein
    • Mohan, P. M., Mukherjee, S., and Chary, K. V. (2008) Differential native state ruggedness of the two Ca2+-binding domains in a Ca2+ sensor protein. Proteins 70, 1147-1153.
    • (2008) Proteins , vol.70 , pp. 1147-1153
    • Mohan, P.M.1    Mukherjee, S.2    Chary, K.V.3
  • 40
    • 0031160103 scopus 로고    scopus 로고
    • Temperature dependence of 1H chemical shifts in proteins
    • Baxter, N. J., and Williamson, M. P. (1997) Temperature dependence of 1H chemical shifts in proteins. J. Biomol. NMR 9, 359-369.
    • (1997) J. Biomol. NMR , vol.9 , pp. 359-369
    • Baxter, N.J.1    Williamson, M.P.2
  • 41
    • 0022556699 scopus 로고
    • 1H-NMR assignment and secondary structure of a herpes simplex virus glycoprotein D-1 antigenic domain
    • Williamson, M. P., Hall, M. J., and Handa, B. K. (1986) 1H-NMR assignment and secondary structure of a herpes simplex virus glycoprotein D-1 antigenic domain. Eur. J. Biochem. 158, 527-536.
    • (1986) Eur. J. Biochem , vol.158 , pp. 527-536
    • Williamson, M.P.1    Hall, M.J.2    Handa, B.K.3
  • 42
    • 0026534189 scopus 로고
    • Conformational isomerism of endothelin in acidic aqueous media: A quantitative NOESY analysis
    • Andersen, N. H., Chen, C. P., Marschner, T. M., Krystek, S. R., Jr., and Bassolino, D. A. (1992) Conformational isomerism of endothelin in acidic aqueous media: a quantitative NOESY analysis. Biochemistry 31, 1280-1295.
    • (1992) Biochemistry , vol.31 , pp. 1280-1295
    • Andersen, N.H.1    Chen, C.P.2    Marschner, T.M.3    Krystek Jr., S.R.4    Bassolino, D.A.5
  • 43
    • 0034984208 scopus 로고    scopus 로고
    • Nmr probes of molecular dynamics: Overview and comparison with other techniques
    • Palmer, A. G. (2001) Nmr probes of molecular dynamics: overview and comparison with other techniques. Annu. Rev. Biophys. Biomol. Struct. 30, 129-155.
    • (2001) Annu. Rev. Biophys. Biomol. Struct , vol.30 , pp. 129-155
    • Palmer, A.G.1
  • 44
    • 0035996716 scopus 로고    scopus 로고
    • Backbone dynamics of the 8 kDa dynein light chain dimer reveals molecular basis of the protein's functional diversity
    • Fan, J. S., Zhang, Q., Tochio, H., and 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.
    • (2002) J. Biomol. NMR , vol.23 , pp. 103-114
    • Fan, J.S.1    Zhang, Q.2    Tochio, H.3    Zhang, M.4
  • 45
    • 0035830488 scopus 로고    scopus 로고
    • Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain
    • Fan, J., Zhang, Q., Tochio, H., Li, M., and Zhang, M. (2001) Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain. J. Mol. Biol. 306, 97-108.
    • (2001) J. Mol. Biol , vol.306 , pp. 97-108
    • Fan, J.1    Zhang, Q.2    Tochio, H.3    Li, M.4    Zhang, M.5


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