메뉴 건너뛰기




Volumn 288, Issue 42, 2013, Pages 30029-30041

Functional characterization of human myosin-18A and its interaction with F-actin and GOLPH3

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETONS; DIRECT INTERACTIONS; F-ACTIN; FUNCTIONAL CHARACTERIZATION; MOLECULAR BASIS; MOTOR DOMAIN; N-TERMINAL EXTENSION;

EID: 84886892623     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.497180     Document Type: Article
Times cited : (55)

References (46)
  • 1
    • 82755192841 scopus 로고    scopus 로고
    • Shaking the myosin family tree. Biochemical kinetics defines four types of myosin motor
    • Bloemink, M. J., and Geeves, M. A. (2011) Shaking the myosin family tree. Biochemical kinetics defines four types of myosin motor. Semin. Cell Dev. Biol. 22, 961-967
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 961-967
    • Bloemink, M.J.1    Geeves, M.A.2
  • 2
    • 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
  • 3
    • 0034595081 scopus 로고    scopus 로고
    • Isolation of a novel PDZ-containing myosin from hematopoietic supportive bone marrow stromal cell lines
    • Furusawa, T., Ikawa, S., Yanai, N., and Obinata, M. (2000) Isolation of a novel PDZ-containing myosin from hematopoietic supportive bone marrow stromal cell lines. Biochem. Biophys. Res. Commun. 270, 67-75
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 67-75
    • Furusawa, T.1    Ikawa, S.2    Yanai, N.3    Obinata, M.4
  • 5
    • 17644385550 scopus 로고    scopus 로고
    • The N-terminal domain of MYO18A has an ATP-insensitive actin-binding site
    • Isogawa, Y., Kon, T., Inoue, T., Ohkura, R., Yamakawa, H., Ohara, O., and Sutoh, K. (2005) The N-terminal domain of MYO18A has an ATP-insensitive actin-binding site. Biochemistry 44, 6190-6196
    • (2005) Biochemistry , vol.44 , pp. 6190-6196
    • Isogawa, Y.1    Kon, T.2    Inoue, T.3    Ohkura, R.4    Yamakawa, H.5    Ohara, O.6    Sutoh, K.7
  • 6
    • 78649491922 scopus 로고    scopus 로고
    • Exon array analysis using re-defined probe sets results in reliable identification of alternatively spliced genes in non-small cell lung cancer
    • Langer, W., Sohler, F., Leder, G., Beckmann, G., Seidel, H., Gröne, J., Hummel, M., and Sommer, A. (2010) Exon array analysis using re-defined probe sets results in reliable identification of alternatively spliced genes in non-small cell lung cancer. BMC Genomics 11, 676
    • (2010) BMC Genomics , vol.11 , pp. 676
    • Langer, W.1    Sohler, F.2    Leder, G.3    Beckmann, G.4    Seidel, H.5    Gröne, J.6    Hummel, M.7    Sommer, A.8
  • 8
    • 59949103230 scopus 로고    scopus 로고
    • Identification of a MYO18A-PDGFRB fusion gene in an eosinophilia- associated atypical myeloproliferative neoplasm with a t(5;17)(q33-34;q11.2)
    • Walz, C., Haferlach, C., Hänel, A., Metzgeroth, G., Erben, P., Gosenca, D., Hochhaus, A., Cross, N. C., and Reiter, A. (2009) Identification of a MYO18A-PDGFRB fusion gene in an eosinophilia-associated atypical myeloproliferative neoplasm with a t(5;17)(q33-34;q11.2). Genes Chromosomes Cancer 48, 179-183
    • (2009) Genes Chromosomes Cancer , vol.48 , pp. 179-183
    • Walz, C.1    Haferlach, C.2    Hänel, A.3    Metzgeroth, G.4    Erben, P.5    Gosenca, D.6    Hochhaus, A.7    Cross, N.C.8    Reiter, A.9
  • 9
    • 84865397771 scopus 로고    scopus 로고
    • A three-way translocation of MLL, MLLT11, and the novel reciprocal partner gene MYO18A in a child with acute myeloid leukemia
    • Ussowicz, M., Jaskowiec, A., Meyer, C., Marschalek, R., Chybicka, A., Szczepanski, T., and Haus, O. (2012) A three-way translocation of MLL, MLLT11, and the novel reciprocal partner gene MYO18A in a child with acute myeloid leukemia. Cancer Genet. 205, 261-265
    • (2012) Cancer Genet. , vol.205 , pp. 261-265
    • Ussowicz, M.1    Jaskowiec, A.2    Meyer, C.3    Marschalek, R.4    Chybicka, A.5    Szczepanski, T.6    Haus, O.7
  • 10
    • 0037569636 scopus 로고    scopus 로고
    • Genome structure and differential expression of two isoforms of a novel PDZ-containing myosin (MysPDZ) (Myo18A)
    • Mori, K., Furusawa, T., Okubo, T., Inoue, T., Ikawa, S., Yanai, N., Mori, K. J., and Obinata, M. (2003) Genome structure and differential expression of two isoforms of a novel PDZ-containing myosin (MysPDZ) (Myo18A). J. Biochem. 133, 405-413
    • (2003) J. Biochem. , vol.133 , pp. 405-413
    • Mori, K.1    Furusawa, T.2    Okubo, T.3    Inoue, T.4    Ikawa, S.5    Yanai, N.6    Mori, K.J.7    Obinata, M.8
  • 12
    • 79958726446 scopus 로고    scopus 로고
    • Drosophila melanogaster myosin-18 represents a highly divergent motor with actin tethering properties
    • Guzik-Lendrum, S., Nagy, A., Takagi, Y., Houdusse, A., and Sellers, J. R. (2011) Drosophila melanogaster myosin-18 represents a highly divergent motor with actin tethering properties. J. Biol. Chem. 286, 21755-21766
    • (2011) J. Biol. Chem. , vol.286 , pp. 21755-21766
    • Guzik-Lendrum, S.1    Nagy, A.2    Takagi, Y.3    Houdusse, A.4    Sellers, J.R.5
  • 13
    • 75649094184 scopus 로고    scopus 로고
    • Identification of MYO18A as a novel interacting partner of the PAK2/PIX/ GIT1 complex and its potential function in modulating epithelial cell migration
    • Hsu, R.-M., Tsai, M.-H., Hsieh, Y.-J., Lyu, P.-C., and Yu, J.-S. (2010) Identification of MYO18A as a novel interacting partner of the PAK2/PIX/ GIT1 complex and its potential function in modulating epithelial cell migration. Mol. Biol. Cell 21, 287-301
    • (2010) Mol. Biol. Cell , vol.21 , pp. 287-301
    • Hsu, R.-M.1    Tsai, M.-H.2    Hsieh, Y.-J.3    Lyu, P.-C.4    Yu, J.-S.5
  • 14
    • 52949140261 scopus 로고    scopus 로고
    • A tripartite complex containing MRCK modulates lamellar actomyosin retrograde flow
    • Tan, I., Yong, J., Dong, J. M., Lim, L., and Leung, T. (2008) A tripartite complex containing MRCK modulates lamellar actomyosin retrograde flow. Cell 135, 123-136
    • (2008) Cell , vol.135 , pp. 123-136
    • Tan, I.1    Yong, J.2    Dong, J.M.3    Lim, L.4    Leung, T.5
  • 17
    • 0015526770 scopus 로고
    • Intrinsic fluorescence of actin
    • Lehrer, S. S., and Kerwar, G. (1972) Intrinsic fluorescence of actin. Biochemistry 11, 1211-1217
    • (1972) Biochemistry , vol.11 , pp. 1211-1217
    • Lehrer, S.S.1    Kerwar, G.2
  • 18
    • 79952315441 scopus 로고    scopus 로고
    • Phalloidin perturbs the interaction of human nonmuscle myosin isoforms 2A and 2C1 with F-actin
    • Diensthuber, R. P., Müller, M., Heissler, S. M., Taft, M. H., Chizhov, I., and Manstein, D. J. (2011) Phalloidin perturbs the interaction of human nonmuscle myosin isoforms 2A and 2C1 with F-actin. FEBS Lett. 585, 767-771
    • (2011) FEBS Lett. , vol.585 , pp. 767-771
    • Diensthuber, R.P.1    Müller, M.2    Heissler, S.M.3    Taft, M.H.4    Chizhov, I.5    Manstein, D.J.6
  • 19
    • 0032766063 scopus 로고    scopus 로고
    • Role of the salt-bridge between switch-1 and switch-2 of Dictyostelium myosin
    • Furch, M., Fujita-Becker, S., Geeves, M. A., Holmes, K. C., and Manstein, D. J. (1999) Role of the salt-bridge between switch-1 and switch-2 of Dictyostelium myosin. J. Mol. Biol. 290, 797-809
    • (1999) J. Mol. Biol. , vol.290 , pp. 797-809
    • Furch, M.1    Fujita-Becker, S.2    Geeves, M.A.3    Holmes, K.C.4    Manstein, D.J.5
  • 20
    • 0016794154 scopus 로고
    • The kinetic mechanism of the manganous ion-dependent adenosine triphosphatase of myosin subfragment 1
    • Bagshaw, C. R. (1975) The kinetic mechanism of the manganous ion-dependent adenosine triphosphatase of myosin subfragment 1. FEBS Lett. 58, 197-201
    • (1975) FEBS Lett. , vol.58 , pp. 197-201
    • Bagshaw C, R.1
  • 22
    • 0030472486 scopus 로고    scopus 로고
    • Anovel stopped-flow method for measuring the affinity of actin for myosin head fragments using microgram quantities of protein
    • Kurzawa, S. E., and Geeves, M. A. (1996)Anovel stopped-flow method for measuring the affinity of actin for myosin head fragments using microgram quantities of protein. J. Muscle Res. Cell. Motil. 17, 669-676
    • (1996) J. Muscle Res. Cell. Motil. , vol.17 , pp. 669-676
    • Kurzawa, S.E.1    Geeves, M.A.2
  • 23
    • 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
  • 25
    • 79958703016 scopus 로고    scopus 로고
    • Comparative kinetic and functional characterization of the motor domains of human nonmuscle myosin- 2C isoforms
    • Heissler, S. M., and Manstein, D. J. (2011) Comparative kinetic and functional characterization of the motor domains of human nonmuscle myosin- 2C isoforms. J. Biol. Chem. 286, 21191-21202
    • (2011) J. Biol. Chem. , vol.286 , pp. 21191-21202
    • Heissler, S.M.1    Manstein, D.J.2
  • 26
    • 33751559579 scopus 로고    scopus 로고
    • Screening for ligands using a generic and high-throughput light-scattering-based assay
    • Senisterra, G. A., Markin, E., Yamazaki, K., Hui, R., Vedadi, M., and Awrey, D. E. (2006) Screening for ligands using a generic and high-throughput light-scattering-based assay. J. Biomol. Screen. 11, 940-948
    • (2006) J. Biomol. Screen. , vol.11 , pp. 940-948
    • Senisterra, G.A.1    Markin, E.2    Yamazaki, K.3    Hui, R.4    Vedadi, M.5    Awrey, D.E.6
  • 27
    • 33845917564 scopus 로고    scopus 로고
    • Why molecules move along a temperature gradient
    • Duhr, S., and Braun, D. (2006) Why molecules move along a temperature gradient. Proc. Natl. Acad. Sci. U.S.A. 103, 19678-19682
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 19678-19682
    • Duhr, S.1    Braun, D.2
  • 28
    • 84855254333 scopus 로고    scopus 로고
    • Protein-binding assays in biological liquids using microscale thermophoresis
    • Wienken, C. J., Baaske, P., Rothbauer, U., Braun, D., and Duhr, S. (2010) Protein-binding assays in biological liquids using microscale thermophoresis. Nat. Commun. 1, 100
    • (2010) Nat. Commun. , vol.1 , pp. 100
    • Wienken, C.J.1    Baaske, P.2    Rothbauer, U.3    Braun, D.4    Duhr, S.5
  • 29
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER. A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., and Zhang, Y. (2010) I-TASSER. A unified platform for automated protein structure and function prediction. Nat. Protoc. 5, 725-738
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 30
    • 34249869832 scopus 로고    scopus 로고
    • Ab initio modeling of small proteins by iterative TASSER simulations
    • Wu, S., Skolnick, J., and Zhang, Y. (2007) Ab initio modeling of small proteins by iterative TASSER simulations. BMC Biol. 5, 17
    • (2007) BMC Biol. , vol.5 , pp. 17
    • Wu, S.1    Skolnick, J.2    Zhang, Y.3
  • 32
    • 0029927237 scopus 로고    scopus 로고
    • Thermal unfolding of Acanthamoeba myosin II and skeletal muscle myosin
    • Zolkiewski, M., Redowicz, M. J., Korn, E. D., and Ginsburg, A. (1996) Thermal unfolding of Acanthamoeba myosin II and skeletal muscle myosin. Biophys. Chem. 59, 365-371
    • (1996) Biophys. Chem. , vol.59 , pp. 365-371
    • Zolkiewski, M.1    Redowicz, M.J.2    Korn, E.D.3    Ginsburg, A.4
  • 33
    • 0034681913 scopus 로고    scopus 로고
    • Charge changes in loop 2 affect the thermal unfolding of the myosin motor domain bound to F-actin
    • Ponomarev, M. A., Furch, M., Levitsky, D. I., and Manstein, D. J. (2000) Charge changes in loop 2 affect the thermal unfolding of the myosin motor domain bound to F-actin. Biochemistry 39, 4527-4532
    • (2000) Biochemistry , vol.39 , pp. 4527-4532
    • Ponomarev, M.A.1    Furch, M.2    Levitsky, D.I.3    Manstein, D.J.4
  • 34
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains. Targeting signalling molecules to sub-membranous sites
    • Ponting, C. P., Phillips, C., Davies, K. E., and Blake, D. J. (1997) PDZ domains. Targeting signalling molecules to sub-membranous sites. BioEssays 19, 469-479
    • (1997) BioEssays , vol.19 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 35
    • 0031460029 scopus 로고    scopus 로고
    • PDZ domain proteins. Scaffolds for signaling complexes
    • Ranganathan, R., and Ross, E. M. (1997) PDZ domain proteins. Scaffolds for signaling complexes. Curr. Biol. 7, R770-R773
    • (1997) Curr. Biol. , vol.7
    • Ranganathan, R.1    Ross, E.M.2
  • 36
    • 0032499768 scopus 로고    scopus 로고
    • Functional transitions in myosin. Formation of a critical salt-bridge and transmission of effect to the sensitive tryptophan
    • Onishi, H., Kojima, S., Katoh, K., Fujiwara, K., Martinez, H. M., and Morales, M. F. (1998) Functional transitions in myosin. Formation of a critical salt-bridge and transmission of effect to the sensitive tryptophan. Proc. Natl. Acad. Sci. U.S.A. 95, 6653-6658
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6653-6658
    • Onishi, H.1    Kojima, S.2    Katoh, K.3    Fujiwara, K.4    Martinez, H.M.5    Morales, M.F.6
  • 39
    • 34547134747 scopus 로고    scopus 로고
    • Evidence for an interaction between the SH3 domain and the N-terminal extension of the essential light chain in class II myosins
    • Lowey, S., Saraswat, L. D., Liu, H., Volkmann, N., and Hanein, D. (2007) Evidence for an interaction between the SH3 domain and the N-terminal extension of the essential light chain in class II myosins. J. Mol. Biol. 371, 902-913
    • (2007) J. Mol. Biol. , vol.371 , pp. 902-913
    • Lowey, S.1    Saraswat, L.D.2    Liu, H.3    Volkmann, N.4    Hanein, D.5
  • 40
    • 0026329490 scopus 로고
    • Determination of cytosolic ADP and AMP concentrations and the free energy of ATP hydrolysis in human muscle and brain tissues with 31P NMR spectroscopy
    • Roth, K., and Weiner, M. W. (1991) Determination of cytosolic ADP and AMP concentrations and the free energy of ATP hydrolysis in human muscle and brain tissues with 31P NMR spectroscopy. Magn. Reson. Med. 22, 505-511
    • (1991) Magn. Reson. Med. , vol.22 , pp. 505-511
    • Roth, K.1    Weiner, M.W.2
  • 41
    • 18144450120 scopus 로고
    • Phosphagen and metabolite content during contraction in porcine carotid artery
    • Krisanda, J. M., and Paul, R. J. (1983) Phosphagen and metabolite content during contraction in porcine carotid artery. Am. J. Physiol. 244, C385-C390
    • (1983) Am. J. Physiol. , vol.244
    • Krisanda, J.M.1    Paul, R.J.2
  • 42
    • 0031709567 scopus 로고    scopus 로고
    • MgADP promotes a catch-like state developed through force-calcium hysteresis in tonic smooth muscle
    • Khromov, A., Somlyo, A. V., and Somlyo, A. P. (1998) MgADP promotes a catch-like state developed through force-calcium hysteresis in tonic smooth muscle. Biophys. J. 75, 1926-1934
    • (1998) Biophys. J. , vol.75 , pp. 1926-1934
    • Khromov, A.1    Somlyo, A.V.2    Somlyo, A.P.3
  • 44
    • 80052461316 scopus 로고    scopus 로고
    • Proteomics analysis of the ezrin interactome in B cells reveals a novel association with Myo18aα
    • Matsui, K., Parameswaran, N., Bagheri, N., Willard, B., and Gupta, N. (2011) Proteomics analysis of the ezrin interactome in B cells reveals a novel association with Myo18aα. J. Proteome Res. 10, 3983-3992
    • (2011) J. Proteome Res. , vol.10 , pp. 3983-3992
    • Matsui, K.1    Parameswaran, N.2    Bagheri, N.3    Willard, B.4    Gupta, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.