메뉴 건너뛰기




Volumn 18, Issue 4, 2007, Pages 1507-1518

The myosin IXb motor activity targets the myosin IXb RhoGAP domain as cargo to sites of actin polymerization

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; MYOSIN; PROTEIN MYO9B; PROTEIN SUBUNIT; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 34247232108     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-08-0771     Document Type: Article
Times cited : (54)

References (38)
  • 1
    • 0031231083 scopus 로고    scopus 로고
    • Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
    • Ahmadian, M. R., Stege, P., Scheffzek, K., and Wittinghofer, A. (1997). Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nat. Struct. Biol. 4, 686-689.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 686-689
    • Ahmadian, M.R.1    Stege, P.2    Scheffzek, K.3    Wittinghofer, A.4
  • 2
    • 0343819894 scopus 로고    scopus 로고
    • Are class III and class IX myosins motorized signalling molecules?
    • Bähler, M. (2000). Are class III and class IX myosins motorized signalling molecules? Biochim. Biophys. Acta Mol. Cell Res. 1496, 52-59.
    • (2000) Biochim. Biophys. Acta Mol. Cell Res , vol.1496 , pp. 52-59
    • Bähler, M.1
  • 3
    • 0025162268 scopus 로고
    • Functions of the myosin ATP and actin binding sites are required for C. elegans thick filament assembly
    • Bejsovec, A. and Anderson, P. (1990). Functions of the myosin ATP and actin binding sites are required for C. elegans thick filament assembly. Cell 60, 133-140.
    • (1990) Cell , vol.60 , pp. 133-140
    • Bejsovec, A.1    Anderson, P.2
  • 4
    • 3042796979 scopus 로고    scopus 로고
    • GAP control: Regulating the regulators of small GTPases
    • Bernards, A. and Settleman, J. (2004). GAP control: regulating the regulators of small GTPases. Trends Cell Biol. 14, 377-385.
    • (2004) Trends Cell Biol , vol.14 , pp. 377-385
    • Bernards, A.1    Settleman, J.2
  • 5
    • 0032485859 scopus 로고    scopus 로고
    • Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain
    • Furch, M., Geeves, M. A., and Manstein, D. J. (1998). Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain. Biochemistry 37, 6317-6326.
    • (1998) Biochemistry , vol.37 , pp. 6317-6326
    • Furch, M.1    Geeves, M.A.2    Manstein, D.J.3
  • 6
    • 0034519957 scopus 로고    scopus 로고
    • Functional role for the class IX myosin myr5 in epithelial cell infection by Shigella flexneri
    • Graf, B., Bähler, M., Hilpelä, P., Bowe, C., and Adam, T. (2000). Functional role for the class IX myosin myr5 in epithelial cell infection by Shigella flexneri. Cell. Microbiol. 2, 601-616.
    • (2000) Cell. Microbiol , vol.2 , pp. 601-616
    • Graf, B.1    Bähler, M.2    Hilpelä, P.3    Bowe, C.4    Adam, T.5
  • 7
    • 0032714620 scopus 로고    scopus 로고
    • Cloning of the murine unconventional myosin gene Myo9b and identification of alternative splicing
    • Grewal, P. K., Jones, A. M., Maconochie, M., Lemmers, R.J.F., Frants, R. R., and Hewitt, J. E. (1999). Cloning of the murine unconventional myosin gene Myo9b and identification of alternative splicing. Gene 240, 389-398.
    • (1999) Gene , vol.240 , pp. 389-398
    • Grewal, P.K.1    Jones, A.M.2    Maconochie, M.3    Lemmers, R.J.F.4    Frants, R.R.5    Hewitt, J.E.6
  • 8
    • 0036222522 scopus 로고    scopus 로고
    • Myosin IXb is a single-headed minus-end-directed processive motor
    • Inoue, A., Saito, J., Ikebe, R., and Ikebe, M. (2002). Myosin IXb is a single-headed minus-end-directed processive motor. Nat. Cell Biol. 4, 302-306.
    • (2002) Nat. Cell Biol , vol.4 , pp. 302-306
    • Inoue, A.1    Saito, J.2    Ikebe, R.3    Ikebe, M.4
  • 9
    • 0035793563 scopus 로고    scopus 로고
    • Two conserved lysines at the 50/20-kDa junction of myosin are necessary for triggering actin activation
    • Joel, P. B., Trybus, K. M., and Sweeney, H. L. (2001). Two conserved lysines at the 50/20-kDa junction of myosin are necessary for triggering actin activation. J. Biol. Chem. 276, 2998-3003.
    • (2001) J. Biol. Chem , vol.276 , pp. 2998-3003
    • Joel, P.B.1    Trybus, K.M.2    Sweeney, H.L.3
  • 10
    • 33646056142 scopus 로고    scopus 로고
    • A unique ATP hydrolysis mechanism of single-headed processive myosin, Myosin IX
    • Kambara, T. and Ikebe, M. (2006). A unique ATP hydrolysis mechanism of single-headed processive myosin, Myosin IX. J. Biol. Chem. 281, 4949-4957.
    • (2006) J. Biol. Chem , vol.281 , pp. 4949-4957
    • Kambara, T.1    Ikebe, M.2
  • 12
    • 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
  • 13
    • 24344482090 scopus 로고    scopus 로고
    • Localized RhoA activation as a requirement for the induction of membrane ruffling
    • Kurokawa, K. and Matsuda, M. (2005). Localized RhoA activation as a requirement for the induction of membrane ruffling. Mol. Biol. Cell 16, 4294-4303.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4294-4303
    • Kurokawa, K.1    Matsuda, M.2
  • 14
    • 0037213689 scopus 로고    scopus 로고
    • Rho GTPase-activating proteins in cell regulation
    • Moon, S. Y. and Zheng, Y. (2003). Rho GTPase-activating proteins in cell regulation. Trends Cell Biol. 13, 13-22.
    • (2003) Trends Cell Biol , vol.13 , pp. 13-22
    • Moon, S.Y.1    Zheng, Y.2
  • 15
    • 0039521743 scopus 로고    scopus 로고
    • The rat myosin myr 5 is a GTPase-activating protein for Rho in vivo: Essential role of arginine 1695
    • Muller, R. T., Honnert, U., Reinhard, J., and Bahler, M. (1997). The rat myosin myr 5 is a GTPase-activating protein for Rho in vivo: essential role of arginine 1695. Mol. Biol. Cell 8, 2039-2053.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2039-2053
    • Muller, R.T.1    Honnert, U.2    Reinhard, J.3    Bahler, M.4
  • 16
    • 0033596962 scopus 로고    scopus 로고
    • The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity
    • Murphy, C. T. and Spudich, J. A. (1999). The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity. Biochemistry 38, 3785-3792.
    • (1999) Biochemistry , vol.38 , pp. 3785-3792
    • Murphy, C.T.1    Spudich, J.A.2
  • 17
    • 28244490257 scopus 로고    scopus 로고
    • Kinetic mechanism of Myosin IXB and the contributions of two class IX-specific regions
    • Nalavadi, V., Nyitrai, M., Bertolini, C., Adamek, N., Geeves, M. A., and Bähler, M. (2005). Kinetic mechanism of Myosin IXB and the contributions of two class IX-specific regions. J. Biol. Chem. 280, 38957-38968.
    • (2005) J. Biol. Chem , vol.280 , pp. 38957-38968
    • Nalavadi, V.1    Nyitrai, M.2    Bertolini, C.3    Adamek, N.4    Geeves, M.A.5    Bähler, M.6
  • 18
    • 0037341905 scopus 로고    scopus 로고
    • Redox-dependent down-regulation of Rho by Rac
    • Nimnual, A. S., Taylor, L. J., and Bar-Sagi, D. (2003). Redox-dependent down-regulation of Rho by Rac. Nat. Cell Biol. 5, 236-241.
    • (2003) Nat. Cell Biol , vol.5 , pp. 236-241
    • Nimnual, A.S.1    Taylor, L.J.2    Bar-Sagi, D.3
  • 20
    • 0037320618 scopus 로고    scopus 로고
    • Native Myosin-IXb is a plus-, not a minus-end-directed motor
    • O'Connell, C. B., and Mooseker, M. S. (2003). Native Myosin-IXb is a plus-, not a minus-end-directed motor. Nat. Cell Biol. 5, 171-172.
    • (2003) Nat. Cell Biol , vol.5 , pp. 171-172
    • O'Connell, C.B.1    Mooseker, M.S.2
  • 21
    • 33746658154 scopus 로고    scopus 로고
    • FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling
    • Ohta, Y., Hartwig, J. H., and Stossel, T. P. (2006). FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling. Nat. Cell Biol. 8, 803-814.
    • (2006) Nat. Cell Biol , vol.8 , pp. 803-814
    • Ohta, Y.1    Hartwig, J.H.2    Stossel, T.P.3
  • 22
    • 33646197411 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of RhoA activity in migrating cells
    • Pertz, O., Hodgson, L., Klemke, R. L., and Hahn, K. M. (2006). Spatiotemporal dynamics of RhoA activity in migrating cells. Nature 440, 1069-1072.
    • (2006) Nature , vol.440 , pp. 1069-1072
    • Pertz, O.1    Hodgson, L.2    Klemke, R.L.3    Hahn, K.M.4
  • 24
    • 0034804337 scopus 로고    scopus 로고
    • Reduced protein diffusion rate by cytoskeleton in vegetative and polarized dictyostelium cells
    • Potma, E. O., de Boeij, W. P., Bosgraaf, L., Roelofs, J., van Haastert, P. J., and Wiersma, D. A. (2001). Reduced protein diffusion rate by cytoskeleton in vegetative and polarized dictyostelium cells. Biophys. J. 82, 2010-2019.
    • (2001) Biophys. J , vol.82 , pp. 2010-2019
    • Potma, E.O.1    de Boeij, W.P.2    Bosgraaf, L.3    Roelofs, J.4    van Haastert, P.J.5    Wiersma, D.A.6
  • 25
    • 0028911031 scopus 로고
    • A novel type of myosin implicated in signalling by rho family GT-Pases
    • Reinhard, J., Scheel, A. A., Diekmann, D., Hall, A., Ruppert, C., and Bähler, M. (1995). A novel type of myosin implicated in signalling by rho family GT-Pases. EMBO J. 14, 697-704.
    • (1995) EMBO J , vol.14 , pp. 697-704
    • Reinhard, J.1    Scheel, A.A.2    Diekmann, D.3    Hall, A.4    Ruppert, C.5    Bähler, M.6
  • 26
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J. and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 27
    • 0033615966 scopus 로고    scopus 로고
    • Rac downregulates Rho activity: Reciprocal balance between both GTPases determines cellular morphology and migratory behavior
    • Sander, E. E., ten Klooster, J. P., van Delft, S., van der Kammen, R. A., and Collard, J. G. (1999). Rac downregulates Rho activity: reciprocal balance between both GTPases determines cellular morphology and migratory behavior. J. Cell Biol. 147, 1009-1022.
    • (1999) J. Cell Biol , vol.147 , pp. 1009-1022
    • Sander, E.E.1    ten Klooster, J.P.2    van Delft, S.3    van der Kammen, R.A.4    Collard, J.G.5
  • 28
    • 0032127912 scopus 로고    scopus 로고
    • GTPase-activating proteins: Helping hands to complement an active site
    • Scheffzek, K., Ahmadian, M. R., and Wittinghofer, A. (1998). GTPase-activating proteins: helping hands to complement an active site. Trends Biochem. Sci. 23, 257-262.
    • (1998) Trends Biochem. Sci , vol.23 , pp. 257-262
    • Scheffzek, K.1    Ahmadian, M.R.2    Wittinghofer, A.3
  • 29
    • 0030664537 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of the switch I region in the ATPase site of Dictyostelium discoideum Myosin II
    • Shimada, T., Sasaki, N., Ohkura, R., and Sutoh, K. (1997). Alanine scanning mutagenesis of the switch I region in the ATPase site of Dictyostelium discoideum Myosin II. Biochemistry 36, 14037-14043.
    • (1997) Biochemistry , vol.36 , pp. 14037-14043
    • Shimada, T.1    Sasaki, N.2    Ohkura, R.3    Sutoh, K.4
  • 30
    • 18444414614 scopus 로고    scopus 로고
    • ROCK and mDia1 antagonize in Rho-dependent Rac activation in Swiss 3T3 fibroblasts
    • Tsuji, T. et al. (2002). ROCK and mDia1 antagonize in Rho-dependent Rac activation in Swiss 3T3 fibroblasts. J. Cell Biol. 157, 819-830.
    • (2002) J. Cell Biol , vol.157 , pp. 819-830
    • Tsuji, T.1
  • 31
    • 0036218579 scopus 로고    scopus 로고
    • MYO1A (Brush Border Myosin I) dynamics in the brush border of LLC-PK1-CL4 cells
    • Tyska, M. J. and Mooseker, M. S. (2002). MYO1A (Brush Border Myosin I) dynamics in the brush border of LLC-PK1-CL4 cells. Biophys. J. 82, 1869-1883.
    • (2002) Biophys. J , vol.82 , pp. 1869-1883
    • Tyska, M.J.1    Mooseker, M.S.2
  • 32
    • 0344758986 scopus 로고    scopus 로고
    • Regulation of cell polarity and protrusion formation by targeting RhoA for degradation
    • Wang, H. R., Zhang, Y., Ozdamar, B., Ogunjimi, A. A., Alexandrova, E., Thomsen, G. H., and Wrana, J. L. (2003). Regulation of cell polarity and protrusion formation by targeting RhoA for degradation. Science 302, 1775-1779.
    • (2003) Science , vol.302 , pp. 1775-1779
    • Wang, H.R.1    Zhang, Y.2    Ozdamar, B.3    Ogunjimi, A.A.4    Alexandrova, E.5    Thomsen, G.H.6    Wrana, J.L.7
  • 33
    • 0037039770 scopus 로고    scopus 로고
    • Single-molecule speckle analysis of actin filament turnover in lamellipodia
    • Watanabe, N. and Mitchison, T. J. (2002). Single-molecule speckle analysis of actin filament turnover in lamellipodia. Science 295, 1083-1086.
    • (2002) Science , vol.295 , pp. 1083-1086
    • Watanabe, N.1    Mitchison, T.J.2
  • 35
    • 0029991890 scopus 로고    scopus 로고
    • Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail
    • Wirth, J. A., Jensen, K. A., Post, P. L., Bement, W. M., and Mooseker, M. S. (1996). Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail. J. Cell Sci. 109, 653-661.
    • (1996) J. Cell Sci , vol.109 , pp. 653-661
    • Wirth, J.A.1    Jensen, K.A.2    Post, P.L.3    Bement, W.M.4    Mooseker, M.S.5
  • 36
    • 33644865751 scopus 로고    scopus 로고
    • Neutrophil polarization: Spatiotemporal dynamics of RhoA activity support a self-organizing mechanism
    • Wong, K., Pertz, O., Hahn, K., and Bourne, H. (2006). Neutrophil polarization: Spatiotemporal dynamics of RhoA activity support a self-organizing mechanism. Proc. Natl. Acad. Sci. USA 103, 3639-3644.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 3639-3644
    • Wong, K.1    Pertz, O.2    Hahn, K.3    Bourne, H.4
  • 38
    • 1542267772 scopus 로고    scopus 로고
    • Functional role of loop 2 in myosin V
    • Yengo, C. M. and Sweeney, H. L. (2004). Functional role of loop 2 in myosin V. Biochemistry. 43, 2605-2612.
    • (2004) Biochemistry , vol.43 , pp. 2605-2612
    • Yengo, C.M.1    Sweeney, H.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.