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Volumn 23, Issue 2, 2013, Pages 81-89

Regulation and control of myosin-I by the motor and light chain-binding domains

Author keywords

Light chain binding domain; Mechanochemistry; Motor domain; Myosin I

Indexed keywords

MYOSIN I;

EID: 84872845163     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2012.10.008     Document Type: Review
Times cited : (49)

References (95)
  • 1
    • 0035163726 scopus 로고    scopus 로고
    • A millennial myosin census
    • Berg J.S., et al. A millennial myosin census. Mol. Biol. Cell 2001, 12:780-794.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 780-794
    • Berg, J.S.1
  • 2
    • 67649607122 scopus 로고    scopus 로고
    • The enterocyte microvillus is a vesicle-generating organelle
    • McConnell R.E., et al. The enterocyte microvillus is a vesicle-generating organelle. J. Cell Biol. 2009, 185:1285-1298.
    • (2009) J. Cell Biol. , vol.185 , pp. 1285-1298
    • McConnell, R.E.1
  • 3
    • 84864743481 scopus 로고    scopus 로고
    • Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis
    • Cheng J., et al. Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis. Mol. Biol. Cell 2012, 23:2891-2904.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2891-2904
    • Cheng, J.1
  • 4
    • 54849439728 scopus 로고    scopus 로고
    • CaMKII-mediated phosphorylation of the myosin motor Myo1c is required for insulin-stimulated GLUT4 translocation in adipocytes
    • Yip M.F., et al. CaMKII-mediated phosphorylation of the myosin motor Myo1c is required for insulin-stimulated GLUT4 translocation in adipocytes. Cell Metab. 2008, 8:384-398.
    • (2008) Cell Metab. , vol.8 , pp. 384-398
    • Yip, M.F.1
  • 5
    • 84863089556 scopus 로고    scopus 로고
    • Myo1c regulates lipid raft recycling to control cell spreading, migration and Salmonella invasion
    • Brandstaetter H., et al. Myo1c regulates lipid raft recycling to control cell spreading, migration and Salmonella invasion. J. Cell Sci. 2012, 125:1991-2003.
    • (2012) J. Cell Sci. , vol.125 , pp. 1991-2003
    • Brandstaetter, H.1
  • 6
    • 84866735100 scopus 로고    scopus 로고
    • Membrane-bound Myo1c powers asymmetric motility of actin filaments
    • Pyrpassopoulos S., et al. Membrane-bound Myo1c powers asymmetric motility of actin filaments. Curr. Biol. 2012, 22:1688-1692.
    • (2012) Curr. Biol. , vol.22 , pp. 1688-1692
    • Pyrpassopoulos, S.1
  • 7
    • 79959954909 scopus 로고    scopus 로고
    • Myosin 1b promotes the formation of post-Golgi carriers by regulating actin assembly and membrane remodelling at the trans-Golgi network
    • Almeida C.G., et al. Myosin 1b promotes the formation of post-Golgi carriers by regulating actin assembly and membrane remodelling at the trans-Golgi network. Nat. Cell Biol. 2011, 13:779-789.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 779-789
    • Almeida, C.G.1
  • 8
    • 84859619448 scopus 로고    scopus 로고
    • Enterocyte microvillus-derived vesicles detoxify bacterial products and regulate epithelial-microbial interactions
    • Shifrin D.A., et al. Enterocyte microvillus-derived vesicles detoxify bacterial products and regulate epithelial-microbial interactions. Curr. Biol. 2012, 22:627-631.
    • (2012) Curr. Biol. , vol.22 , pp. 627-631
    • Shifrin, D.A.1
  • 9
    • 34249098669 scopus 로고    scopus 로고
    • Myosin-1a powers the sliding of apical membrane along microvillar actin bundles
    • McConnell R.E., Tyska M.J. Myosin-1a powers the sliding of apical membrane along microvillar actin bundles. J. Cell Biol. 2007, 177:671-681.
    • (2007) J. Cell Biol. , vol.177 , pp. 671-681
    • McConnell, R.E.1    Tyska, M.J.2
  • 10
    • 13444256475 scopus 로고    scopus 로고
    • A model of stereocilia adaptation based on single molecule mechanical studies of myosin I
    • Batters C., et al. A model of stereocilia adaptation based on single molecule mechanical studies of myosin I. Philos. Trans. R. Soc. Lond. B: Biol. Sci. 2004, 359:1895-1905.
    • (2004) Philos. Trans. R. Soc. Lond. B: Biol. Sci. , vol.359 , pp. 1895-1905
    • Batters, C.1
  • 11
    • 74249105441 scopus 로고    scopus 로고
    • Myosin 1G (Myo1G) is a haematopoietic specific myosin that localises to the plasma membrane and regulates cell elasticity
    • Olety B., et al. Myosin 1G (Myo1G) is a haematopoietic specific myosin that localises to the plasma membrane and regulates cell elasticity. FEBS Lett. 2010, 584:493-499.
    • (2010) FEBS Lett. , vol.584 , pp. 493-499
    • Olety, B.1
  • 12
    • 23944492960 scopus 로고    scopus 로고
    • Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast
    • Sirotkin V., et al. Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast. J. Cell Biol. 2005, 170:637-648.
    • (2005) J. Cell Biol. , vol.170 , pp. 637-648
    • Sirotkin, V.1
  • 13
    • 84865067150 scopus 로고    scopus 로고
    • Myo1c facilitates G-actin transport to the leading edge of migrating endothelial cells
    • Fan Y., et al. Myo1c facilitates G-actin transport to the leading edge of migrating endothelial cells. J. Cell Biol. 2012, 198:47-55.
    • (2012) J. Cell Biol. , vol.198 , pp. 47-55
    • Fan, Y.1
  • 14
    • 33750487863 scopus 로고    scopus 로고
    • Myosin-1c couples assembling actin to membranes to drive compensatory endocytosis
    • Sokac A.M., et al. Myosin-1c couples assembling actin to membranes to drive compensatory endocytosis. Dev. Cell 2006, 11:629-640.
    • (2006) Dev. Cell , vol.11 , pp. 629-640
    • Sokac, A.M.1
  • 15
    • 46149083971 scopus 로고    scopus 로고
    • A Rictor-Myo1c complex participates in dynamic cortical actin events in 3T3-L1 adipocytes
    • Hagan G.N., et al. A Rictor-Myo1c complex participates in dynamic cortical actin events in 3T3-L1 adipocytes. Mol. Cell. Biol. 2008, 28:4215-4226.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4215-4226
    • Hagan, G.N.1
  • 16
    • 0034644632 scopus 로고    scopus 로고
    • A myosin I isoform in the nucleus
    • Pestic-Dragovich L., et al. A myosin I isoform in the nucleus. Science 2000, 290:337-341.
    • (2000) Science , vol.290 , pp. 337-341
    • Pestic-Dragovich, L.1
  • 17
    • 18244409866 scopus 로고    scopus 로고
    • Myosin-1a is critical for normal brush border structure and composition
    • Tyska M.J., et al. Myosin-1a is critical for normal brush border structure and composition. Mol. Biol. Cell 2005, 16:2443-2457.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2443-2457
    • Tyska, M.J.1
  • 18
    • 0037180775 scopus 로고    scopus 로고
    • Glucose transporter recycling in response to insulin is facilitated by myosin Myo1c
    • Bose A., et al. Glucose transporter recycling in response to insulin is facilitated by myosin Myo1c. Nature 2002, 420:821-824.
    • (2002) Nature , vol.420 , pp. 821-824
    • Bose, A.1
  • 19
    • 34548188298 scopus 로고    scopus 로고
    • Activation of RalA is required for insulin-stimulated Glut4 trafficking to the plasma membrane via the exocyst and the motor protein Myo1c
    • Chen X.W., et al. Activation of RalA is required for insulin-stimulated Glut4 trafficking to the plasma membrane via the exocyst and the motor protein Myo1c. Dev. Cell 2007, 13:391-404.
    • (2007) Dev. Cell , vol.13 , pp. 391-404
    • Chen, X.W.1
  • 20
    • 33846821794 scopus 로고    scopus 로고
    • Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis
    • Krendel M., et al. Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis. FEBS Lett. 2007, 581:644-650.
    • (2007) FEBS Lett. , vol.581 , pp. 644-650
    • Krendel, M.1
  • 21
    • 0033749378 scopus 로고    scopus 로고
    • Coevolution of head, neck, and tail domains of myosin heavy chains
    • Korn E.D. Coevolution of head, neck, and tail domains of myosin heavy chains. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:12559-12564.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12559-12564
    • Korn, E.D.1
  • 22
    • 33750515229 scopus 로고    scopus 로고
    • Myo1c Binds phosphoinositides through a putative pleckstrin homology domain
    • Hokanson D.E., et al. Myo1c Binds phosphoinositides through a putative pleckstrin homology domain. Mol. Biol. Cell 2006, 17:4856-4865.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4856-4865
    • Hokanson, D.E.1
  • 23
    • 33644771150 scopus 로고    scopus 로고
    • Myo1c binds tightly and specifically to phosphatidylinositol 4,5-bisphosphate and inositol 1,4,5-trisphosphate
    • Hokanson D.E., Ostap E.M. Myo1c binds tightly and specifically to phosphatidylinositol 4,5-bisphosphate and inositol 1,4,5-trisphosphate. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:3118-3123.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 3118-3123
    • Hokanson, D.E.1    Ostap, E.M.2
  • 24
    • 0037077215 scopus 로고    scopus 로고
    • The kinetic mechanism of Myo1e (human myosin-IC)
    • El Mezgueldi M., et al. The kinetic mechanism of Myo1e (human myosin-IC). J. Biol. Chem. 2002, 277:21514-21521.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21514-21521
    • El Mezgueldi, M.1
  • 25
    • 0031445915 scopus 로고    scopus 로고
    • Kinetic characterization of brush border myosin-I ATPase
    • Jontes J.D., et al. Kinetic characterization of brush border myosin-I ATPase. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:14332-14337.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 14332-14337
    • Jontes, J.D.1
  • 26
    • 33749008779 scopus 로고    scopus 로고
    • Temperature dependence of nucleotide association and kinetic characterization of myo1b
    • Lewis J.H., et al. Temperature dependence of nucleotide association and kinetic characterization of myo1b. Biochemistry 2006, 45:11589-11597.
    • (2006) Biochemistry , vol.45 , pp. 11589-11597
    • Lewis, J.H.1
  • 27
    • 29244458650 scopus 로고    scopus 로고
    • Biochemical and motile properties of Myo1b splice isoforms
    • Lin T., et al. Biochemical and motile properties of Myo1b splice isoforms. J. Biol. Chem. 2005, 280:41562-41567.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41562-41567
    • Lin, T.1
  • 28
    • 0037108276 scopus 로고    scopus 로고
    • Mechanism of regulation of Acanthamoeba myosin-IC by heavy-chain phosphorylation
    • Ostap E.M., et al. Mechanism of regulation of Acanthamoeba myosin-IC by heavy-chain phosphorylation. Biochemistry 2002, 41:12450-12456.
    • (2002) Biochemistry , vol.41 , pp. 12450-12456
    • Ostap, E.M.1
  • 29
    • 0029915892 scopus 로고    scopus 로고
    • Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase
    • Ostap E.M., Pollard T.D. Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase. J. Cell Biol. 1996, 132:1053-1060.
    • (1996) J. Cell Biol. , vol.132 , pp. 1053-1060
    • Ostap, E.M.1    Pollard, T.D.2
  • 30
    • 2342512278 scopus 로고    scopus 로고
    • Myo1c is designed for the adaptation response in the inner ear
    • Batters C., et al. Myo1c is designed for the adaptation response in the inner ear. EMBO J. 2004, 23:1433-1440.
    • (2004) EMBO J. , vol.23 , pp. 1433-1440
    • Batters, C.1
  • 31
    • 0033618274 scopus 로고    scopus 로고
    • Transient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. A myosin I designed for maintenance of tension?
    • Coluccio L.M., Geeves M.A. Transient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. A myosin I designed for maintenance of tension?. J. Biol. Chem. 1999, 274:21575-21580.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21575-21580
    • Coluccio, L.M.1    Geeves, M.A.2
  • 32
    • 33644990897 scopus 로고    scopus 로고
    • Dictyostelium myosin-IE is a fast molecular motor involved in phagocytosis
    • Durrwang U., et al. Dictyostelium myosin-IE is a fast molecular motor involved in phagocytosis. J. Cell Sci. 2006, 119:550-558.
    • (2006) J. Cell Sci. , vol.119 , pp. 550-558
    • Durrwang, U.1
  • 33
    • 41949108658 scopus 로고    scopus 로고
    • Mechanism, regulation, and functional properties of Dictyostelium myosin-1B
    • Tsiavaliaris G., et al. Mechanism, regulation, and functional properties of Dictyostelium myosin-1B. J. Biol. Chem. 2008, 283:4520-4527.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4520-4527
    • Tsiavaliaris, G.1
  • 34
    • 84866291356 scopus 로고    scopus 로고
    • Myosin IC generates power over a range of loads via a new tension-sensing mechanism
    • Greenberg M.J., et al. Myosin IC generates power over a range of loads via a new tension-sensing mechanism. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:E2433-E2440.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109
    • Greenberg, M.J.1
  • 35
    • 0024312342 scopus 로고
    • The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme
    • Mooseker M.S., Coleman T.R. The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme. J. Cell Biol. 1989, 108:2395-2400.
    • (1989) J. Cell Biol. , vol.108 , pp. 2395-2400
    • Mooseker, M.S.1    Coleman, T.R.2
  • 36
    • 1642333310 scopus 로고    scopus 로고
    • Relating biochemistry and function in the myosin superfamily
    • De La Cruz E.M., Ostap E.M. Relating biochemistry and function in the myosin superfamily. Curr. Opin. Cell Biol. 2004, 16:61-67.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 61-67
    • De La Cruz, E.M.1    Ostap, E.M.2
  • 37
    • 82755192841 scopus 로고    scopus 로고
    • Shaking the myosin family tree: biochemical kinetics defines four types of myosin motor
    • Bloemink M.J., Geeves M.A. Shaking the myosin family tree: biochemical kinetics defines four types of myosin motor. Semin. Cell Dev. Biol. 2011, 22:961-967.
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 961-967
    • Bloemink, M.J.1    Geeves, M.A.2
  • 38
    • 0029006373 scopus 로고
    • TEDS rule: a molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head
    • Bement W.M., Mooseker M.S. TEDS rule: a molecular rationale for differential regulation of myosins by phosphorylation of the heavy chain head. Cell Motil. Cytoskeleton 1995, 31:87-92.
    • (1995) Cell Motil. Cytoskeleton , vol.31 , pp. 87-92
    • Bement, W.M.1    Mooseker, M.S.2
  • 39
    • 70450230344 scopus 로고    scopus 로고
    • Ste20-kinase-dependent TEDS-site phosphorylation modulates the dynamic localisation and endocytic function of the fission yeast class I myosin, Myo1
    • Attanapola S.L., et al. Ste20-kinase-dependent TEDS-site phosphorylation modulates the dynamic localisation and endocytic function of the fission yeast class I myosin, Myo1. J. Cell Sci. 2009, 122:3856-3861.
    • (2009) J. Cell Sci. , vol.122 , pp. 3856-3861
    • Attanapola, S.L.1
  • 40
    • 46849089895 scopus 로고    scopus 로고
    • Myosin I can act as a molecular force sensor
    • Laakso J.M., et al. Myosin I can act as a molecular force sensor. Science 2008, 321:133-136.
    • (2008) Science , vol.321 , pp. 133-136
    • Laakso, J.M.1
  • 41
    • 76249094825 scopus 로고    scopus 로고
    • Control of myosin-I force sensing by alternative splicing
    • Laakso J.M., et al. Control of myosin-I force sensing by alternative splicing. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:698-702.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 698-702
    • Laakso, J.M.1
  • 42
    • 84862696215 scopus 로고    scopus 로고
    • Calcium regulation of myosin-I tension sensing
    • Lewis J.H., et al. Calcium regulation of myosin-I tension sensing. Biophys. J. 2012, 102:2799-2807.
    • (2012) Biophys. J. , vol.102 , pp. 2799-2807
    • Lewis, J.H.1
  • 43
    • 0027499951 scopus 로고
    • Identification, characterization and cloning of myr 1, a mammalian myosin-I
    • Ruppert C., et al. Identification, characterization and cloning of myr 1, a mammalian myosin-I. J. Cell Biol. 1993, 120:1393-1403.
    • (1993) J. Cell Biol. , vol.120 , pp. 1393-1403
    • Ruppert, C.1
  • 44
    • 33645758327 scopus 로고    scopus 로고
    • Force generation in single conventional actomyosin complexes under high dynamic load
    • Takagi Y., et al. Force generation in single conventional actomyosin complexes under high dynamic load. Biophys. J. 2006, 90:1295-1307.
    • (2006) Biophys. J. , vol.90 , pp. 1295-1307
    • Takagi, Y.1
  • 45
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell G.I. Models for the specific adhesion of cells to cells. Science 1978, 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 46
    • 0242609969 scopus 로고    scopus 로고
    • Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers
    • Veigel C., et al. Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers. Nat. Cell Biol. 2003, 5:980-986.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 980-986
    • Veigel, C.1
  • 47
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • Veigel C., et al. Load-dependent kinetics of myosin-V can explain its high processivity. Nat. Cell Biol. 2005, 7:861-869.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 861-869
    • Veigel, C.1
  • 48
    • 79952802312 scopus 로고    scopus 로고
    • A hearing loss-associated myo1c mutation (R156W) decreases the myosin duty ratio and force sensitivity
    • Lin T., et al. A hearing loss-associated myo1c mutation (R156W) decreases the myosin duty ratio and force sensitivity. Biochemistry 2011, 50:1831-1838.
    • (2011) Biochemistry , vol.50 , pp. 1831-1838
    • Lin, T.1
  • 49
    • 0029559076 scopus 로고
    • Localization of the rat myosin I molecules myr 1 and myr 2 and in vivo targeting of their tail domains
    • Ruppert C., et al. Localization of the rat myosin I molecules myr 1 and myr 2 and in vivo targeting of their tail domains. J. Cell Sci. 1995, 108:3775-3786.
    • (1995) J. Cell Sci. , vol.108 , pp. 3775-3786
    • Ruppert, C.1
  • 50
    • 44449142420 scopus 로고    scopus 로고
    • Calcium sensitivity of the cross-bridge cycle of Myo1c, the adaptation motor in the inner ear
    • Adamek N., et al. Calcium sensitivity of the cross-bridge cycle of Myo1c, the adaptation motor in the inner ear. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:5710-5715.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 5710-5715
    • Adamek, N.1
  • 51
    • 0036180246 scopus 로고    scopus 로고
    • A chemical-genetic strategy implicates myosin-1c in adaptation by hair cells
    • Holt J.R., et al. A chemical-genetic strategy implicates myosin-1c in adaptation by hair cells. Cell 2002, 108:371-381.
    • (2002) Cell , vol.108 , pp. 371-381
    • Holt, J.R.1
  • 52
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: a molecular motor
    • Rayment I., et al. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 1993, 261:50-58.
    • (1993) Science , vol.261 , pp. 50-58
    • Rayment, I.1
  • 54
    • 0033535556 scopus 로고    scopus 로고
    • The motor protein myosin-I produces its working stroke in two steps
    • Veigel C., et al. The motor protein myosin-I produces its working stroke in two steps. Nature 1999, 398:530-533.
    • (1999) Nature , vol.398 , pp. 530-533
    • Veigel, C.1
  • 55
    • 77950552549 scopus 로고    scopus 로고
    • The epithelial splicing factors ESRP1 and ESRP2 positively and negatively regulate diverse types of alternative splicing events
    • Warzecha C.C., et al. The epithelial splicing factors ESRP1 and ESRP2 positively and negatively regulate diverse types of alternative splicing events. RNA Biol. 2009, 6:546-562.
    • (2009) RNA Biol. , vol.6 , pp. 546-562
    • Warzecha, C.C.1
  • 57
    • 0025264994 scopus 로고
    • Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro
    • Collins K., et al. Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro. J. Cell Biol. 1990, 110:1137-1147.
    • (1990) J. Cell Biol. , vol.110 , pp. 1137-1147
    • Collins, K.1
  • 58
    • 0032486408 scopus 로고    scopus 로고
    • 2+ binding to its light chain calmodulin
    • 2+ binding to its light chain calmodulin. J. Biol. Chem. 1998, 273:14605-14611.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14605-14611
    • Stoffler, H.E.1    Bahler, M.2
  • 60
    • 0035943018 scopus 로고    scopus 로고
    • Motor domain-dependent localization of myo1b (myr-1)
    • Tang N., Ostap E.M. Motor domain-dependent localization of myo1b (myr-1). Curr. Biol. 2001, 11:1131-1135.
    • (2001) Curr. Biol. , vol.11 , pp. 1131-1135
    • Tang, N.1    Ostap, E.M.2
  • 61
    • 77949457529 scopus 로고    scopus 로고
    • Tropomyosin and myosin-II cellular levels promote actomyosin ring assembly in fission yeast
    • Stark B.C., et al. Tropomyosin and myosin-II cellular levels promote actomyosin ring assembly in fission yeast. Mol. Biol. Cell 2010, 21:989-1000.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 989-1000
    • Stark, B.C.1
  • 62
    • 84864589401 scopus 로고    scopus 로고
    • Tropomyosin is essential for processive movement of a class V myosin from budding yeast
    • Hodges A.R., et al. Tropomyosin is essential for processive movement of a class V myosin from budding yeast. Curr. Biol. 2012, 22:1410-1416.
    • (2012) Curr. Biol. , vol.22 , pp. 1410-1416
    • Hodges, A.R.1
  • 63
    • 0029977811 scopus 로고    scopus 로고
    • A high molecular mass non-muscle tropomyosin isoform stimulates retrograde organelle transport
    • Pelham R.J., et al. A high molecular mass non-muscle tropomyosin isoform stimulates retrograde organelle transport. J. Cell Sci. 1996, 109:981-989.
    • (1996) J. Cell Sci. , vol.109 , pp. 981-989
    • Pelham, R.J.1
  • 64
    • 0027933182 scopus 로고
    • Differential regulation of skeletal muscle myosin-II and brush border myosin-I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms
    • Fanning A.S., et al. Differential regulation of skeletal muscle myosin-II and brush border myosin-I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms. Cell Motil. Cytoskeleton 1994, 29:29-45.
    • (1994) Cell Motil. Cytoskeleton , vol.29 , pp. 29-45
    • Fanning, A.S.1
  • 65
    • 0037013903 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of a class-I myosin
    • Kollmar M., et al. Crystal structure of the motor domain of a class-I myosin. EMBO J. 2002, 21:2517-2525.
    • (2002) EMBO J. , vol.21 , pp. 2517-2525
    • Kollmar, M.1
  • 66
    • 33947213792 scopus 로고    scopus 로고
    • Myosin surface loop 4 modulates inhibition of actomyosin 1b ATPase activity by tropomyosin
    • Lieto-Trivedi A., et al. Myosin surface loop 4 modulates inhibition of actomyosin 1b ATPase activity by tropomyosin. Biochemistry 2007, 46:2779-2786.
    • (2007) Biochemistry , vol.46 , pp. 2779-2786
    • Lieto-Trivedi, A.1
  • 67
    • 60849138840 scopus 로고    scopus 로고
    • Tropomyosins as discriminators of myosin function
    • Ostap E.M. Tropomyosins as discriminators of myosin function. Adv. Exp. Med. Biol. 2008, 644:273-282.
    • (2008) Adv. Exp. Med. Biol. , vol.644 , pp. 273-282
    • Ostap, E.M.1
  • 68
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
    • McKillop D.F., Geeves M.A. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 1993, 65:693-701.
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 69
    • 0029148548 scopus 로고
    • Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii
    • Baines I.C., et al. Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii. J. Cell Biol. 1995, 130:591-603.
    • (1995) J. Cell Biol. , vol.130 , pp. 591-603
    • Baines, I.C.1
  • 70
    • 0036547906 scopus 로고    scopus 로고
    • Myosin I is required for hypha formation in Candida albicans
    • Oberholzer U., et al. Myosin I is required for hypha formation in Candida albicans. Eukaryot. Cell 2002, 1:213-228.
    • (2002) Eukaryot. Cell , vol.1 , pp. 213-228
    • Oberholzer, U.1
  • 71
    • 0031933790 scopus 로고    scopus 로고
    • The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function
    • Novak K.D., Titus M.A. The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function. Mol. Biol. Cell 1998, 9:75-88.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 75-88
    • Novak, K.D.1    Titus, M.A.2
  • 72
    • 33744959045 scopus 로고    scopus 로고
    • TEDS site phosphorylation of the yeast myosins I is required for ligand-induced but not for constitutive endocytosis of the G protein-coupled receptor Ste2p
    • Grosshans B.L., et al. TEDS site phosphorylation of the yeast myosins I is required for ligand-induced but not for constitutive endocytosis of the G protein-coupled receptor Ste2p. J. Biol. Chem. 2006, 281:11104-11114.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11104-11114
    • Grosshans, B.L.1
  • 73
    • 0036547070 scopus 로고    scopus 로고
    • Myosin-1c interacts with hair-cell receptors through its calmodulin-binding IQ domains
    • Cyr J.L., et al. Myosin-1c interacts with hair-cell receptors through its calmodulin-binding IQ domains. J. Neurosci. 2002, 22:2487-2495.
    • (2002) J. Neurosci. , vol.22 , pp. 2487-2495
    • Cyr, J.L.1
  • 74
    • 79960384705 scopus 로고    scopus 로고
    • A calmodulin-related light chain from fission yeast that functions with myosin-I and PI 4-kinase
    • Sammons M.R., et al. A calmodulin-related light chain from fission yeast that functions with myosin-I and PI 4-kinase. J. Cell Sci. 2011, 124:2466-2477.
    • (2011) J. Cell Sci. , vol.124 , pp. 2466-2477
    • Sammons, M.R.1
  • 75
    • 33646547984 scopus 로고    scopus 로고
    • Identification and characterization of an 8-kDa light chain associated with Dictyostelium discoideum MyoB, a class I myosin
    • Crawley S.W., et al. Identification and characterization of an 8-kDa light chain associated with Dictyostelium discoideum MyoB, a class I myosin. J. Biol. Chem. 2006, 281:6307-6315.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6307-6315
    • Crawley, S.W.1
  • 76
    • 41049117567 scopus 로고    scopus 로고
    • CIB1 and CaBP1 bind to the myo1c regulatory domain
    • Tang N., et al. CIB1 and CaBP1 bind to the myo1c regulatory domain. J. Muscle Res. Cell Motil. 2007, 28:285-291.
    • (2007) J. Muscle Res. Cell Motil. , vol.28 , pp. 285-291
    • Tang, N.1
  • 77
    • 0029987840 scopus 로고    scopus 로고
    • Overlapping functions of myosin-I isoforms?
    • Ostap E.M., Pollard T.D. Overlapping functions of myosin-I isoforms?. J. Cell Biol. 1996, 133:221-224.
    • (1996) J. Cell Biol. , vol.133 , pp. 221-224
    • Ostap, E.M.1    Pollard, T.D.2
  • 78
    • 77949443128 scopus 로고    scopus 로고
    • Differential localization and dynamics of class I myosins in the enterocyte microvillus
    • Benesh A.E., et al. Differential localization and dynamics of class I myosins in the enterocyte microvillus. Mol. Biol. Cell 2010, 21:970-978.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 970-978
    • Benesh, A.E.1
  • 79
    • 0030692707 scopus 로고    scopus 로고
    • Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis
    • Jontes J.D., Milligan R.A. Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis. J. Cell Biol. 1997, 139:683-693.
    • (1997) J. Cell Biol. , vol.139 , pp. 683-693
    • Jontes, J.D.1    Milligan, R.A.2
  • 80
    • 0032489923 scopus 로고    scopus 로고
    • Three-dimensional structure of Acanthamoeba castellanii myosin-IB (MIB) determined by cryoelectron microscopy of decorated actin filaments
    • Jontes J.D., et al. Three-dimensional structure of Acanthamoeba castellanii myosin-IB (MIB) determined by cryoelectron microscopy of decorated actin filaments. J. Cell Biol. 1998, 141:155-162.
    • (1998) J. Cell Biol. , vol.141 , pp. 155-162
    • Jontes, J.D.1
  • 81
    • 77954315036 scopus 로고    scopus 로고
    • Leveraging the membrane - cytoskeleton interface with myosin-1
    • McConnell R.E., Tyska M.J. Leveraging the membrane - cytoskeleton interface with myosin-1. Trends Cell Biol. 2010, 20:418-426.
    • (2010) Trends Cell Biol. , vol.20 , pp. 418-426
    • McConnell, R.E.1    Tyska, M.J.2
  • 82
    • 0026721410 scopus 로고
    • Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC
    • Doberstein S.K., Pollard T.D. Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC. J. Cell Biol. 1992, 117:1241-1249.
    • (1992) J. Cell Biol. , vol.117 , pp. 1241-1249
    • Doberstein, S.K.1    Pollard, T.D.2
  • 83
    • 78049263512 scopus 로고    scopus 로고
    • Myo1e binds anionic phospholipids with high affinity
    • Feeser E.A., et al. Myo1e binds anionic phospholipids with high affinity. Biochemistry 2010, 49:9353-9360.
    • (2010) Biochemistry , vol.49 , pp. 9353-9360
    • Feeser, E.A.1
  • 84
    • 84859740875 scopus 로고    scopus 로고
    • Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain
    • Mazerik J.N., Tyska M.J. Myosin-1A targets to microvilli using multiple membrane binding motifs in the tail homology 1 (TH1) domain. J. Biol. Chem. 2012, 287:13104-13115.
    • (2012) J. Biol. Chem. , vol.287 , pp. 13104-13115
    • Mazerik, J.N.1    Tyska, M.J.2
  • 85
    • 70350350076 scopus 로고    scopus 로고
    • Kinetics of the interaction of myo1c with phosphoinositides
    • McKenna J.M., Ostap E.M. Kinetics of the interaction of myo1c with phosphoinositides. J. Biol. Chem. 2009, 284:28650-28659.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28650-28659
    • McKenna, J.M.1    Ostap, E.M.2
  • 86
    • 77956257788 scopus 로고    scopus 로고
    • Localization of myosin 1b to actin protrusions requires phosphoinositide binding
    • Komaba S., Coluccio L.M. Localization of myosin 1b to actin protrusions requires phosphoinositide binding. J. Biol. Chem. 2010, 285:27686-27693.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27686-27693
    • Komaba, S.1    Coluccio, L.M.2
  • 87
    • 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)
    • Patino-Lopez G., et al. 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. 2010, 285:8675-8686.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8675-8686
    • Patino-Lopez, G.1
  • 88
    • 57649133951 scopus 로고    scopus 로고
    • Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge
    • Brzeska H., et al. Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge. J. Biol. Chem. 2008, 283:32014-32023.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32014-32023
    • Brzeska, H.1
  • 89
    • 2442560225 scopus 로고    scopus 로고
    • A role for myosin-1A in the localization of a brush border disaccharidase
    • Tyska M.J., Mooseker M.S. A role for myosin-1A in the localization of a brush border disaccharidase. J. Cell Biol. 2004, 165:395-405.
    • (2004) J. Cell Biol. , vol.165 , pp. 395-405
    • Tyska, M.J.1    Mooseker, M.S.2
  • 90
    • 33747422135 scopus 로고    scopus 로고
    • Myosin motor Myo1c and its receptor NEMO/IKK-gamma promote TNF-alpha-induced serine307 phosphorylation of IRS-1
    • Nakamori Y., et al. Myosin motor Myo1c and its receptor NEMO/IKK-gamma promote TNF-alpha-induced serine307 phosphorylation of IRS-1. J. Cell Biol. 2006, 173:665-671.
    • (2006) J. Cell Biol. , vol.173 , pp. 665-671
    • Nakamori, Y.1
  • 91
    • 79956081242 scopus 로고    scopus 로고
    • Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane
    • Arif E., et al. Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane. Mol. Cell. Biol. 2011, 31:2134-2150.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2134-2150
    • Arif, E.1
  • 92
    • 23744467959 scopus 로고    scopus 로고
    • PHR1, an integral membrane protein of the inner ear sensory cells, directly interacts with myosin 1c and myosin VIIa
    • Etournay R., et al. PHR1, an integral membrane protein of the inner ear sensory cells, directly interacts with myosin 1c and myosin VIIa. J. Cell Sci. 2005, 118:2891-2899.
    • (2005) J. Cell Sci. , vol.118 , pp. 2891-2899
    • Etournay, R.1
  • 93
    • 79961136595 scopus 로고    scopus 로고
    • Myosin-1C associates with microtubules and stabilizes the mitotic spindle during cell division
    • Rump A., et al. Myosin-1C associates with microtubules and stabilizes the mitotic spindle during cell division. J. Cell Sci. 2011, 124:2521-2528.
    • (2011) J. Cell Sci. , vol.124 , pp. 2521-2528
    • Rump, A.1
  • 94
    • 0030936970 scopus 로고    scopus 로고
    • The myosin-I-binding protein Acan125 binds the SH3 domain and belongs to the superfamily of leucine-rich repeat proteins
    • Xu P., et al. The myosin-I-binding protein Acan125 binds the SH3 domain and belongs to the superfamily of leucine-rich repeat proteins. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:3685-3690.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 3685-3690
    • Xu, P.1
  • 95
    • 0035954433 scopus 로고    scopus 로고
    • The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains
    • Jung G., et al. The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains. J. Cell Biol. 2001, 153:1479-1497.
    • (2001) J. Cell Biol. , vol.153 , pp. 1479-1497
    • Jung, G.1


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