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Volumn 22, Issue 18, 2012, Pages 1688-1692

Membrane-bound Myo1c powers asymmetric motility of actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

MOLECULAR MOTOR; MYOSIN I; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOPROTEIN; PLASMA PROTEIN; PLATELET PROTEIN P47;

EID: 84866735100     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2012.06.069     Document Type: Article
Times cited : (49)

References (34)
  • 1
    • 77954315036 scopus 로고    scopus 로고
    • Leveraging the membrane - Cytoskeleton interface with myosin-1
    • R.E. McConnell, and M.J. Tyska Leveraging the membrane - cytoskeleton interface with myosin-1 Trends Cell Biol. 20 2010 418 426
    • (2010) Trends Cell Biol. , vol.20 , pp. 418-426
    • McConnell, R.E.1    Tyska, M.J.2
  • 3
    • 33750515229 scopus 로고    scopus 로고
    • Myo1c binds phosphoinositides through a putative pleckstrin homology domain
    • DOI 10.1091/mbc.E06-05-0449
    • D.E. Hokanson, J.M. Laakso, T. Lin, D. Sept, and E.M. Ostap Myo1c binds phosphoinositides through a putative pleckstrin homology domain Mol. Biol. Cell 17 2006 4856 4865 (Pubitemid 44665754)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.11 , pp. 4856-4865
    • Hokanson, D.E.1    Laakso, J.M.2    Lin, T.3    Sept, D.4    Ostap, E.M.5
  • 4
    • 77950573946 scopus 로고    scopus 로고
    • Myosin 1G is an abundant class i myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH)
    • G. Patino-Lopez, L. Aravind, X. Dong, M.J. Kruhlak, E.M. Ostap, and S. Shaw Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH) J. Biol. Chem. 285 2010 8675 8686
    • (2010) J. Biol. Chem. , vol.285 , pp. 8675-8686
    • Patino-Lopez, G.1    Aravind, L.2    Dong, X.3    Kruhlak, M.J.4    Ostap, E.M.5    Shaw, S.6
  • 5
    • 0025365190 scopus 로고
    • Binding of brush border myosin i to phospholipid vesicles
    • S.M. Hayden, J.S. Wolenski, and M.S. Mooseker Binding of brush border myosin I to phospholipid vesicles J. Cell Biol. 111 1990 443 451
    • (1990) J. Cell Biol. , vol.111 , pp. 443-451
    • Hayden, S.M.1    Wolenski, J.S.2    Mooseker, M.S.3
  • 6
    • 0024744488 scopus 로고
    • Plasma membrane association of Acanthamoeba myosin i
    • H. Miyata, B. Bowers, and E.D. Korn Plasma membrane association of Acanthamoeba myosin I J. Cell Biol. 109 1989 1519 1528
    • (1989) J. Cell Biol. , vol.109 , pp. 1519-1528
    • Miyata, H.1    Bowers, B.2    Korn, E.D.3
  • 7
    • 78650183852 scopus 로고    scopus 로고
    • Single-molecule adhesion forces and attachment lifetimes of myosin-I phosphoinositide interactions
    • S. Pyrpassopoulos, H. Shuman, and E.M. Ostap Single-molecule adhesion forces and attachment lifetimes of myosin-I phosphoinositide interactions Biophys. J. 99 2010 3916 3922
    • (2010) Biophys. J. , vol.99 , pp. 3916-3922
    • Pyrpassopoulos, S.1    Shuman, H.2    Ostap, E.M.3
  • 8
    • 0026595130 scopus 로고
    • Myosin-I moves actin filaments on a phospholipid substrate: Implications for membrane targeting
    • H.G. Zot, S.K. Doberstein, and T.D. Pollard Myosin-I moves actin filaments on a phospholipid substrate: implications for membrane targeting J. Cell Biol. 116 1992 367 376
    • (1992) J. Cell Biol. , vol.116 , pp. 367-376
    • Zot, H.G.1    Doberstein, S.K.2    Pollard, T.D.3
  • 9
    • 0028909736 scopus 로고
    • Phospholipid membrane-associated brush border myosin-I activity
    • H.G. Zot Phospholipid membrane-associated brush border myosin-I activity Cell Motil. Cytoskeleton 30 1995 26 37
    • (1995) Cell Motil. Cytoskeleton , vol.30 , pp. 26-37
    • Zot, H.G.1
  • 11
    • 33750487863 scopus 로고    scopus 로고
    • Myosin-1c Couples Assembling Actin to Membranes to Drive Compensatory Endocytosis
    • DOI 10.1016/j.devcel.2006.09.002, PII S1534580706003959
    • A.M. Sokac, C. Schietroma, C.B. Gundersen, and W.M. Bement Myosin-1c couples assembling actin to membranes to drive compensatory endocytosis Dev. Cell 11 2006 629 640 (Pubitemid 44644962)
    • (2006) Developmental Cell , vol.11 , Issue.5 , pp. 629-640
    • Sokac, A.M.1    Schietroma, C.2    Gundersen, CameronB.3    Bement, W.M.4
  • 12
  • 13
    • 84863089556 scopus 로고    scopus 로고
    • Myo1c regulates lipid raft recycling to control cell spreading, migration and Salmonella invasion
    • H. Brandstaetter, J. Kendrick-Jones, and F. Buss Myo1c regulates lipid raft recycling to control cell spreading, migration and Salmonella invasion J. Cell Sci. 125 2012 1991 2003
    • (2012) J. Cell Sci. , vol.125 , pp. 1991-2003
    • Brandstaetter, H.1    Kendrick-Jones, J.2    Buss, F.3
  • 14
    • 70350350076 scopus 로고    scopus 로고
    • Kinetics of the interaction of myo1c with phosphoinositides
    • J.M. McKenna, and E.M. Ostap Kinetics of the interaction of myo1c with phosphoinositides J. Biol. Chem. 284 2009 28650 28659
    • (2009) J. Biol. Chem. , vol.284 , pp. 28650-28659
    • McKenna, J.M.1    Ostap, E.M.2
  • 17
    • 84859740875 scopus 로고    scopus 로고
    • Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain
    • J.N. Mazerik, and M.J. Tyska Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain J. Biol. Chem. 287 2012 13104 13115
    • (2012) J. Biol. Chem. , vol.287 , pp. 13104-13115
    • Mazerik, J.N.1    Tyska, M.J.2
  • 18
    • 29244458650 scopus 로고    scopus 로고
    • Biochemical and motile properties of Myo1b splice isoform
    • DOI 10.1074/jbc.M508653200
    • T. Lin, N. Tang, and E.M. Ostap Biochemical and motile properties of Myo1b splice isoforms J. Biol. Chem. 280 2005 41562 41567 (Pubitemid 41832218)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41562-41567
    • Lin, T.1    Tang, N.2    Ostap, E.M.3
  • 22
    • 0027219972 scopus 로고
    • Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry
    • J.S. Wolenski, S.M. Hayden, P. Forscher, and M.S. Mooseker Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry J. Cell Biol. 122 1993 613 621 (Pubitemid 23226678)
    • (1993) Journal of Cell Biology , vol.122 , Issue.3 , pp. 613-621
    • Wolenski, J.S.1    Hayden, S.M.2    Forscher, P.3    Mooseker, M.S.4
  • 23
    • 69949144222 scopus 로고    scopus 로고
    • Determining the local shear viscosity of a lipid bilayer system by reverse non-equilibrium molecular dynamics simulations
    • T.J. Müller, and F. Müller-Plathe Determining the local shear viscosity of a lipid bilayer system by reverse non-equilibrium molecular dynamics simulations ChemPhysChem 10 2009 2305 2315
    • (2009) ChemPhysChem , vol.10 , pp. 2305-2315
    • Müller, T.J.1    Müller-Plathe, F.2
  • 24
    • 0342419447 scopus 로고    scopus 로고
    • Single lipid diffusion in Langmuir monolayers
    • DOI 10.1021/la000795n
    • M.B. Forstner, J. Kas, and A.F. Martin Single lipid diffusion in languir monolayers Langmuir 17 2001 567 570 (Pubitemid 32873123)
    • (2001) Langmuir , vol.17 , Issue.3 , pp. 567-570
    • Forstner, M.B.1    Kas, J.2    Martin, D.3
  • 26
    • 0027533269 scopus 로고
    • Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape
    • DOI 10.1083/jcb.120.4.923
    • F. Gittes, B. Mickey, J. Nettleton, and J. Howard Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape J. Cell Biol. 120 1993 923 934 (Pubitemid 23056298)
    • (1993) Journal of Cell Biology , vol.120 , Issue.4 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4
  • 27
    • 0027390794 scopus 로고
    • Right-handed rotation of an actin filament in an in vitro motile system
    • DOI 10.1038/361269a0
    • T. Nishizaka, T. Yagi, Y. Tanaka, and S. Ishiwata Right-handed rotation of an actin filament in an in vitro motile system Nature 361 1993 269 271 (Pubitemid 23034479)
    • (1993) Nature , vol.361 , Issue.6409 , pp. 269-271
    • Nishizaka, T.1    Yagi, T.2    Tanaka, Y.3    Ishiwata, S.4
  • 28
    • 0031806323 scopus 로고    scopus 로고
    • Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers
    • S.C. Hopkins, C. Sabido-David, J.E. Corrie, M. Irving, and Y.E. Goldman Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers Biophys. J. 74 1998 3093 3110 (Pubitemid 28268133)
    • (1998) Biophysical Journal , vol.74 , Issue.6 , pp. 3093-3110
    • Hopkins, S.C.1    Sabido-David, C.2    Corrie, J.E.T.3    Irving, M.4    Goldman, Y.E.5
  • 29
    • 33645749163 scopus 로고    scopus 로고
    • Type ID unconventional myosin controls left-right asymmetry in Drosophila
    • P. Spéder, G. Adám, and S. Noselli Type ID unconventional myosin controls left-right asymmetry in Drosophila Nature 440 2006 803 807
    • (2006) Nature , vol.440 , pp. 803-807
    • Spéder, P.1    Adám, G.2    Noselli, S.3
  • 31
    • 0141867843 scopus 로고    scopus 로고
    • Motor protein control of ion flux is an early step in embryonic left-right asymmetry
    • DOI 10.1002/bies.10339
    • M. Levin Motor protein control of ion flux is an early step in embryonic left-right asymmetry Bioessays 25 2003 1002 1010 (Pubitemid 37221524)
    • (2003) BioEssays , vol.25 , Issue.10 , pp. 1002-1010
    • Levin, M.1
  • 32
    • 0025364567 scopus 로고
    • The development of handedness in left/right asymmetry
    • N.A. Brown, and L. Wolpert The development of handedness in left/right asymmetry Development 109 1990 1 9
    • (1990) Development , vol.109 , pp. 1-9
    • Brown, N.A.1    Wolpert, L.2
  • 33
    • 58849094579 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of a PH domain: New insights into the membrane docking reaction
    • J.D. Knight, and J.J. Falke Single-molecule fluorescence studies of a PH domain: new insights into the membrane docking reaction Biophys. J. 96 2009 566 582
    • (2009) Biophys. J. , vol.96 , pp. 566-582
    • Knight, J.D.1    Falke, J.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.