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Volumn 288, Issue 47, 2013, Pages 34131-34145

Structural insights into functional overlapping and differentiation among myosin V motors

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; BINS; CYTOLOGY; FREIGHT TRANSPORTATION;

EID: 84888358879     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.507202     Document Type: Article
Times cited : (30)

References (66)
  • 1
    • 34547986066 scopus 로고    scopus 로고
    • "Should I stay or should I go?" Myosin V function in organelle trafficking
    • Desnos, C., Huet, S., and Darchen, F. (2007) "Should I stay or should I go?" Myosin V function in organelle trafficking. Biol. Cell 99, 411-423
    • (2007) Biol. Cell , vol.99 , pp. 411-423
    • Desnos, C.1    Huet, S.2    Darchen, F.3
  • 2
    • 84355161386 scopus 로고    scopus 로고
    • Walkingto work. Roles for class V myosins as cargo transporters
    • Hammer, J. A., 3rd, and Sellers, J. R. (2012) Walkingto work. Roles for class V myosins as cargo transporters. Nat. Rev. Mol. Cell Biol. 13, 13-26
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 13-26
    • Hammer III, J.A.1    Sellers, J.R.2
  • 4
    • 43049183000 scopus 로고    scopus 로고
    • Myosin V from head to tail
    • Trybus, K. M. (2008) Myosin V from head to tail. Cell Mol. Life Sci. 65, 1378-1389
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 1378-1389
    • Trybus, K.M.1
  • 5
    • 0028231886 scopus 로고
    • Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types
    • Bement, W. M., Hasson, T., Wirth, J. A., Cheney, R. E., and Mooseker, M. S. (1994) Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. Proc. Natl. Acad. Sci. U. S. A. 91, 11767
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 11767
    • Bement, W.M.1    Hasson, T.2    Wirth, J.A.3    Cheney, R.E.4    Mooseker, M.S.5
  • 6
    • 0028219183 scopus 로고
    • Cloning, analysis, and chromosomal localization of myoxin (MYH12), the human homologue to the mouse dilute gene
    • Engle, L. J., and Kennett, R. H. (1994) Cloning, analysis, and chromosomal localization of myoxin (MYH12), the human homologue to the mouse dilute gene. Genomics 19, 407-416
    • (1994) Genomics , vol.19 , pp. 407-416
    • Engle, L.J.1    Kennett, R.H.2
  • 7
    • 37549069575 scopus 로고    scopus 로고
    • Drawing the tree of eukaryotic life based on the analysis of 2, 269 manually annotated myosins from 328 species
    • Odronitz, F., and Kollmar, M. (2007) Drawing the tree of eukaryotic life based on the analysis of 2, 269 manually annotated myosins from 328 species. Genome Biol. 8, R196
    • (2007) Genome Biol. , vol.8
    • Odronitz, F.1    Kollmar, M.2
  • 8
    • 0036500526 scopus 로고    scopus 로고
    • Human myosin-Vc is a novel class V myosin expressed in epithelial cells
    • Rodriguez, O. C., and Cheney, R. E. (2002) Human myosin-Vc is a novel class V myosin expressed in epithelial cells. J. Cell Sci. 115, 991-1004
    • (2002) J. Cell Sci. , vol.115 , pp. 991-1004
    • Rodriguez, O.C.1    Cheney, R.E.2
  • 9
    • 24044500344 scopus 로고    scopus 로고
    • Myosins. Tails (and heads) of functional diversity
    • Krendel, M., and Mooseker, M. S. (2005) Myosins. Tails (and heads) of functional diversity. Physiology 20, 239-251
    • (2005) Physiology , vol.20 , pp. 239-251
    • Krendel, M.1    Mooseker, M.S.2
  • 10
    • 33846163431 scopus 로고    scopus 로고
    • When intracellular logistics fails. Genetic defects in membrane trafficking
    • Olkkonen, V. M., and Ikonen, E. (2006) When intracellular logistics fails. Genetic defects in membrane trafficking. J. Cell Sci. 119, 5031-5045
    • (2006) J. Cell Sci. , vol.119 , pp. 5031-5045
    • Olkkonen, V.M.1    Ikonen, E.2
  • 12
    • 72249100798 scopus 로고    scopus 로고
    • Motor protein-dependent membrane trafficking of KCl cotransporter-4 is important for cancer cell invasion
    • Chen, Y. F., Chou, C. Y., Wilkins, R. J., Ellory, J. C., Mount, D. B., and Shen, M. R. (2009) Motor protein-dependent membrane trafficking of KCl cotransporter-4 is important for cancer cell invasion. Cancer Res. 69, 8585-8593
    • (2009) Cancer Res. , vol.69 , pp. 8585-8593
    • Chen, Y.F.1    Chou, C.Y.2    Wilkins, R.J.3    Ellory, J.C.4    Mount, D.B.5    Shen, M.R.6
  • 13
    • 84879842793 scopus 로고    scopus 로고
    • MYO5B is epigenetically silenced and associated with MET signaling in human gastric cancer
    • Dong, W., Wang, L., and Shen, R. (2013) MYO5B is epigenetically silenced and associated with MET signaling in human gastric cancer. Dig. Dis. Sci. 58, 2038-2045
    • (2013) Dig. Dis. Sci. , vol.58 , pp. 2038-2045
    • Dong, W.1    Wang, L.2    Shen, R.3
  • 14
    • 73449131219 scopus 로고    scopus 로고
    • Upregulation of myosin Va by Snail is involved in cancer cell migration and metastasis
    • Lan, L., Han, H., Zuo, H., Chen, Z., Du, Y., Zhao, W., Gu, J., and Zhang, Z. (2010) Upregulation of myosin Va by Snail is involved in cancer cell migration and metastasis. Int. J. Cancer 126, 53-64
    • (2010) Int. J. Cancer , vol.126 , pp. 53-64
    • Lan, L.1    Han, H.2    Zuo, H.3    Chen, Z.4    Du, Y.5    Zhao, W.6    Gu, J.7    Zhang, Z.8
  • 19
    • 78650709124 scopus 로고    scopus 로고
    • The role of myosin V in exocytosis and synaptic plasticity
    • Rudolf, R., Bittins, C. M., and Gerdes, H. H. (2011) The role of myosin V in exocytosis and synaptic plasticity. J. Neurochem. 116, 177-191
    • (2011) J. Neurochem. , vol.116 , pp. 177-191
    • Rudolf, R.1    Bittins, C.M.2    Gerdes, H.H.3
  • 20
    • 0037112197 scopus 로고    scopus 로고
    • Rab11a and myosin Vb regulate recycling ofthe M4 muscarinic acetylcholine receptor
    • Volpicelli, L. A., Lah, J. J., Fang, G., Goldenring, J. R., and Levey, A. I. (2002) Rab11a and myosin Vb regulate recycling ofthe M4 muscarinic acetylcholine receptor. J. Neurosci. 22, 9776-9784
    • (2002) J. Neurosci. , vol.22 , pp. 9776-9784
    • Volpicelli, L.A.1    Lah, J.J.2    Fang, G.3    Goldenring, J.R.4    Levey, A.I.5
  • 21
    • 39549107553 scopus 로고    scopus 로고
    • The globular tail domain puts on the brake to stop the ATPase cycle of myosin Va
    • Li, X. D., Jung, H. S., Wang, Q., Ikebe, R., Craig, R., and Ikebe, M. (2008) The globular tail domain puts on the brake to stop the ATPase cycle of myosin Va. Proc. Natl. Acad. Sci. U. S. A. 105, 1140-1145
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 1140-1145
    • Li, X.D.1    Jung, H.S.2    Wang, Q.3    Ikebe, R.4    Craig, R.5    Ikebe, M.6
  • 22
    • 33746129173 scopus 로고    scopus 로고
    • Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography
    • Liu, J., Taylor, D. W., Krementsova, E. B., Trybus, K. M., and Taylor, K. A. (2006) Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography. Nature 442, 208-211
    • (2006) Nature , vol.442 , pp. 208-211
    • Liu, J.1    Taylor, D.W.2    Krementsova, E.B.3    Trybus, K.M.4    Taylor, K.A.5
  • 23
    • 33746152398 scopus 로고    scopus 로고
    • The cargo-binding domain regulates structure and activity of myosin 5
    • Thirumurugan, K., Sakamoto, T., Hammer, J. A., 3rd, Sellers, J. R., and Knight, P. J. (2006) The cargo-binding domain regulates structure and activity of myosin 5. Nature 442, 212-215
    • (2006) Nature , vol.442 , pp. 212-215
    • Thirumurugan, K.1    Sakamoto, T.2    Hammer III, J.A.3    Sellers, J.R.4    Knight, P.J.5
  • 24
    • 77951832795 scopus 로고    scopus 로고
    • The structure of the Myo4p globular tail and its function in ASH1 mRNA localization
    • Heuck, A., Fetka, I., Brewer, D. N., Hüls, D., Munson, M., Jansen, R. P., and Niessing, D. (2010) The structure of the Myo4p globular tail and its function in ASH1 mRNA localization. J. Cell Biol. 189, 497-510
    • (2010) J. Cell Biol. , vol.189 , pp. 497-510
    • Heuck, A.1    Fetka, I.2    Brewer, D.N.3    Hüls, D.4    Munson, M.5    Jansen, R.P.6    Niessing, D.7
  • 25
    • 33644548665 scopus 로고    scopus 로고
    • Structural basis for myosin V discrimination between distinct cargoes
    • Pashkova, N., Jin, Y., Ramaswamy, S., and Weisman, L. S. (2006) Structural basis for myosin V discrimination between distinct cargoes. EMBO J. 25, 693-700
    • (2006) EMBO J. , vol.25 , pp. 693-700
    • Pashkova, N.1    Jin, Y.2    Ramaswamy, S.3    Weisman, L.S.4
  • 29
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus, P. A., and Diederichs, K. (2012) Linking crystallographic model and data quality. Science 336, 1030-1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 33
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding, J., Biegert, A., and Lupas, A. N. (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33, W244-248
    • (2005) Nucleic Acids Res. , vol.33
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 34
    • 3242887695 scopus 로고    scopus 로고
    • Protein structure prediction and analysis using the Robetta server
    • Kim, D. E., Chivian, D., and Baker, D. (2004) Protein structure prediction and analysis using the Robetta server. Nucleic Acids Res. 32, W526-W531
    • (2004) Nucleic Acids Res. , vol.32
    • Kim, D.E.1    Chivian, D.2    Baker, D.3
  • 39
  • 40
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter, J., and Merritt, E. A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62, 439-450
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 42
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.1
  • 43
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 44
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V., and Svergun, D. I. (2003) Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 45
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M. B., and Svergun, D. I. (2001) Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34, 33-41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 46
    • 84867508210 scopus 로고    scopus 로고
    • Validationof macromolecular flexibility insolution by small-angle X-ray scattering (SAXS)
    • Hammel, M. (2012) Validationof macromolecular flexibility insolution by small-angle X-ray scattering (SAXS). Eur. Biophys. J. 41, 789-799
    • (2012) Eur. Biophys. J. , vol.41 , pp. 789-799
    • Hammel, M.1
  • 47
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law
    • Rambo, R. P., and Tainer, J. A. (2011) Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law. Biopolymers 95, 559-571
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 50
    • 34548861782 scopus 로고    scopus 로고
    • Protein-protein docking with backbone flexibility
    • Wang, C., Bradley, P., and Baker, D. (2007) Protein-protein docking with backbone flexibility. J. Mol. Biol. 373, 503-519
    • (2007) J. Mol. Biol. , vol.373 , pp. 503-519
    • Wang, C.1    Bradley, P.2    Baker, D.3
  • 51
    • 10344223464 scopus 로고    scopus 로고
    • Making optimal use of empirical energy functions. Force-field parameterization in crystal space
    • Krieger, E., Darden, T., Nabuurs, S. B., Finkelstein, A., and Vriend, G. (2004) Making optimal use of empirical energy functions. Force-field parameterization in crystal space. Proteins 57, 678-683
    • (2004) Proteins , vol.57 , pp. 678-683
    • Krieger, E.1    Darden, T.2    Nabuurs, S.B.3    Finkelstein, A.4    Vriend, G.5
  • 52
    • 77955358961 scopus 로고    scopus 로고
    • Using Situs for the integration of multi-resolution structures
    • Wriggers, W. (2010) Using Situs for the integration of multi-resolution structures. Biophys. Rev. 2, 21-27
    • (2010) Biophys. Rev. , vol.2 , pp. 21-27
    • Wriggers, W.1
  • 54
    • 84865075701 scopus 로고    scopus 로고
    • Overlapofcargo binding sites on myosin V coordinates the inheritance of diverse cargoes
    • Eves, P. T., Jin, Y., Brunner, M., and Weisman, L. S. (2012) Overlapofcargo binding sites on myosin V coordinates the inheritance of diverse cargoes. J. Cell Biol. 198, 69-85
    • (2012) J. Cell Biol. , vol.198 , pp. 69-85
    • Eves, P.T.1    Jin, Y.2    Brunner, M.3    Weisman, L.S.4
  • 55
    • 13444304009 scopus 로고    scopus 로고
    • Myosin V attachment to cargo requires the tight association of two functional subdomains
    • Pashkova, N., Catlett, N. L., Novak, J. L., Wu, G., Lu, R., Cohen, R. E., and Weisman, L. S. (2005) Myosin V attachment to cargo requires the tight association of two functional subdomains. J. Cell Biol. 168, 359-364
    • (2005) J. Cell Biol. , vol.168 , pp. 359-364
    • Pashkova, N.1    Catlett, N.L.2    Novak, J.L.3    Wu, G.4    Lu, R.5    Cohen, R.E.6    Weisman, L.S.7
  • 58
    • 84874400959 scopus 로고    scopus 로고
    • The Rilp-like proteins Rilpl1 and Rilpl2 regulate ciliary membrane content
    • Schaub, J. R., and Stearns, T. (2013) The Rilp-like proteins Rilpl1 and Rilpl2 regulate ciliary membrane content. Mol. Biol. Cell 24, 453-464
    • (2013) Mol. Biol. Cell , vol.24 , pp. 453-464
    • Schaub, J.R.1    Stearns, T.2
  • 59
    • 0742270613 scopus 로고    scopus 로고
    • A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34
    • Wang, T., Wong, K. K., and Hong, W. (2004) A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34. Mol. Biol. Cell 15, 815-826
    • (2004) Mol. Biol. Cell , vol.15 , pp. 815-826
    • Wang, T.1    Wong, K.K.2    Hong, W.3
  • 61
    • 84879959292 scopus 로고    scopus 로고
    • Structural basis of cargo recognitions for class V myosins
    • Wei, Z., Liu, X., Yu, C., and Zhang, M. (2013) Structural basis of cargo recognitions for class V myosins. Proc. Natl. Acad. Sci. U. S. A. 110, 11314-11319
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 11314-11319
    • Wei, Z.1    Liu, X.2    Yu, C.3    Zhang, M.4
  • 62
    • 33746842683 scopus 로고    scopus 로고
    • The globular tail domain of myosin Va functions as an inhibitor of the myosin Va motor
    • Li, X. D., Jung, H. S., Mabuchi, K., Craig, R., and Ikebe, M. (2006) The globular tail domain of myosin Va functions as an inhibitor of the myosin Va motor. J. Biol. Chem. 281, 21789-21798
    • (2006) J. Biol. Chem. , vol.281 , pp. 21789-21798
    • Li, X.D.1    Jung, H.S.2    Mabuchi, K.3    Craig, R.4    Ikebe, M.5
  • 63
    • 33846380243 scopus 로고    scopus 로고
    • Regulation and recycling of myosin V
    • Taylor, K. A. (2007) Regulation and recycling of myosin V. Curr. Opin. Cell Biol. 19, 67-74
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 67-74
    • Taylor, K.A.1
  • 65
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 66
    • 48449099381 scopus 로고    scopus 로고
    • PBEQ-Solver for online visualization of electrostatic potential of biomolecules
    • Jo, S., Vargyas, M., Vasko-Szedlar, J., Roux, B., and Im, W. (2008) PBEQ-Solver for online visualization of electrostatic potential of biomolecules. Nucleic Acids Res. 36, W270-W275
    • (2008) Nucleic Acids Res. , vol.36
    • Jo, S.1    Vargyas, M.2    Vasko-Szedlar, J.3    Roux, B.4    Im, W.5


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