메뉴 건너뛰기




Volumn 117, Issue 24, 2004, Pages 5825-5834

Myosin 3A transgene expression produces abnormal actin filament bundles in transgenic Xenopus laevis rod photoreceptors

Author keywords

Actin; Calycal process; Myosin; Photoreceptors; Xenopus laevis

Indexed keywords

CYTOSKELETON PROTEIN; GREEN FLUORESCENT PROTEIN; MOLECULAR MOTOR; MYOSIN III; MYOSIN IIIA; OPSIN; UNCLASSIFIED DRUG;

EID: 12344284231     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01512     Document Type: Article
Times cited : (20)

References (23)
  • 1
    • 0345133276 scopus 로고    scopus 로고
    • Myosin XVa localizes to the tips of inner ear sensory cell stereocilia and is essential for staircase formation of the hair bundle
    • Belyantseva, I. A., Boger, E. T. and Friedman, T. B. (2003). Myosin XVa localizes to the tips of inner ear sensory cell stereocilia and is essential for staircase formation of the hair bundle. Proc. Natl. Acad. Sci. USA 100, 13958-13963.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13958-13963
    • Belyantseva, I.A.1    Boger, E.T.2    Friedman, T.B.3
  • 2
    • 0036122307 scopus 로고    scopus 로고
    • Myosin-X is an unconventional myosin that undergoes intrafilopodial motility
    • Berg, J. S. and Cheney, R. E. (2002). Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat. Cell Biol. 4, 246-250.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 246-250
    • Berg, J.S.1    Cheney, R.E.2
  • 3
    • 0037342963 scopus 로고    scopus 로고
    • Myo3A, one of two class III myosin genes expressed in vertebrate retina, is localized to the calycal processes of rod and cone photoreceptors and is expressed in the sacculus
    • Dosé, A. C., Hillman, D. W., Wong, C., Sohlberg, L., Lin-Jones, J. and Burnside, B. (2003). Myo3A, one of two class III myosin genes expressed in vertebrate retina, is localized to the calycal processes of rod and cone photoreceptors and is expressed in the sacculus. Mol. Biol. Cell 14, 1058-1073.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1058-1073
    • Dosé, A.C.1    Hillman, D.W.2    Wong, C.3    Sohlberg, L.4    Lin-Jones, J.5    Burnside, B.6
  • 4
    • 12344298343 scopus 로고    scopus 로고
    • Myosin III in photoreceptors: What does it do?
    • (ed. D. S. Williams). Hackensack, NJ: World Scientific
    • Dosé, A. C., Lin-Jones, J. and Burnside, B. (2004). Myosin III in photoreceptors: what does it do? In Cell Biology and Disease of the Outer Retina (ed. D. S. Williams). Hackensack, NJ: World Scientific.
    • (2004) Cell Biology and Disease of the Outer Retina
    • Dosé, A.C.1    Lin-Jones, J.2    Burnside, B.3
  • 5
    • 0141429959 scopus 로고    scopus 로고
    • Localization of a class III myosin to filopodia tips in transfected HeLa cells requires an actin-binding site in its tail domain
    • Erickson, F. L., Corsa, A. C., Dosé, A. C. and Burnside, B. (2003). Localization of a class III myosin to filopodia tips in transfected HeLa cells requires an actin-binding site in its tail domain. Mol. Biol. Cell 14, 4173-4180.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4173-4180
    • Erickson, F.L.1    Corsa, A.C.2    Dosé, A.C.3    Burnside, B.4
  • 6
    • 0034663930 scopus 로고    scopus 로고
    • An intact SH3 domain is required for myosin I-induced actin polymerization
    • Geli, M. I., Lombardi, R., Schmelzl, B. and Riezman, H. (2000). An intact SH3 domain is required for myosin I-induced actin polymerization. EMBO J. 19, 4281-4291.
    • (2000) EMBO J. , vol.19 , pp. 4281-4291
    • Geli, M.I.1    Lombardi, R.2    Schmelzl, B.3    Riezman, H.4
  • 7
    • 0029857718 scopus 로고    scopus 로고
    • Role of the ninaC proteins in photoreceptor cell structure: Ultrastructure of ninaC deletion mutants and binding to actin filaments
    • Hicks, J. L., Liu, X. and Williams, D. S. (1996). Role of the ninaC proteins in photoreceptor cell structure: ultrastructure of ninaC deletion mutants and binding to actin filaments. Cell Motil. Cytoskeleton 35, 367-379.
    • (1996) Cell Motil. Cytoskeleton , vol.35 , pp. 367-379
    • Hicks, J.L.1    Liu, X.2    Williams, D.S.3
  • 10
    • 0038015108 scopus 로고    scopus 로고
    • Determination of human myosin III as a motor protein having a protein kinase activity
    • Komiaba, S., Inoue, A., Maruta, S., Hosoya, H. and Ikebe, M. (2003). Determination of human myosin III as a motor protein having a protein kinase activity. J. Biol. Chem. 278, 21352-21360.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21352-21360
    • Komiaba, S.1    Inoue, A.2    Maruta, S.3    Hosoya, H.4    Ikebe, M.5
  • 11
    • 0034351423 scopus 로고    scopus 로고
    • The roles of unconventional myosins in hearing and deafness
    • Libby, R. T. and Steel, K. P. (2000). The roles of unconventional myosins in hearing and deafness. Essays Biochem. 35, 159-174.
    • (2000) Essays Biochem. , vol.35 , pp. 159-174
    • Libby, R.T.1    Steel, K.P.2
  • 12
    • 0041342077 scopus 로고    scopus 로고
    • Disruption of kinesin II function using a dominant negative-acting transgene in Xenopus laevis rods results in photoreceptor degeneration
    • Lin-Jones, J., Parker, E., Wu, M., Knox, B. E. and Burnside, B. (2003). Disruption of kinesin II function using a dominant negative-acting transgene in Xenopus laevis rods results in photoreceptor degeneration. Invest. Ophthalmol. Vis. Sci. 44 3614-3621.
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 3614-3621
    • Lin-Jones, J.1    Parker, E.2    Wu, M.3    Knox, B.E.4    Burnside, B.5
  • 13
    • 0035965360 scopus 로고    scopus 로고
    • Xenopus rhodopsin promoter. Identification of immediate upstream sequences necessary for high level, rod-specific transcription
    • Mani, S. S., Batni, S., Whitaker, L., Chen, S., Engbretson, G. and Knox, B. E. (2001). Xenopus rhodopsin promoter. Identification of immediate upstream sequences necessary for high level, rod-specific transcription. J. Biol. Chem. 276, 36557-36565.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36557-36565
    • Mani, S.S.1    Batni, S.2    Whitaker, L.3    Chen, S.4    Engbretson, G.5    Knox, B.E.6
  • 14
    • 0024284065 scopus 로고
    • The Drosophila ninaC locus encodes two photoreceptor cell specific proteins with domains homologous to protein kinases and the myosin heavy chain head
    • Montell, C. and Rubin, G. M. (1988). The Drosophila ninaC locus encodes two photoreceptor cell specific proteins with domains homologous to protein kinases and the myosin heavy chain head. Cell 52, 757-772.
    • (1988) Cell , vol.52 , pp. 757-772
    • Montell, C.1    Rubin, G.M.2
  • 15
    • 0035958847 scopus 로고    scopus 로고
    • A functional rhodopsin-green fluorescent protein fusion protein localizes correctly in transgenic Xenopus laevis retinal rods and is expressed in a time-dependent pattern
    • Moritz, O. L., Tam, B. M., Papermaster, D. S. and Nakayama, T. (2001). A functional rhodopsin-green fluorescent protein fusion protein localizes correctly in transgenic Xenopus laevis retinal rods and is expressed in a time-dependent pattern. J. Biol. Chem. 276, 28242-28251.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28242-28251
    • Moritz, O.L.1    Tam, B.M.2    Papermaster, D.S.3    Nakayama, T.4
  • 16
    • 0022479906 scopus 로고
    • The teleost cone cytoskeleton. Localization of actin, microtubules, and intermediate filaments
    • Nagle, B. W., Okamoto, C., Taggart, B. and Burnside, B. (1986). The teleost cone cytoskeleton. Localization of actin, microtubules, and intermediate filaments. Invest. Ophthalmol. Vis. Sci. 27, 689-701.
    • (1986) Invest. Ophthalmol. Vis. Sci. , vol.27 , pp. 689-701
    • Nagle, B.W.1    Okamoto, C.2    Taggart, B.3    Burnside, B.4
  • 17
    • 0019831710 scopus 로고
    • Actin-dependent cell elongation in teleost retinal rods: Requirement for actin filament assembly
    • O'Connor, P. and Burnside, B. (1981). Actin-dependent cell elongation in teleost retinal rods: requirement for actin filament assembly. J. Cell Biol. 89, 517-524.
    • (1981) J. Cell Biol. , vol.89 , pp. 517-524
    • O'Connor, P.1    Burnside, B.2
  • 19
    • 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
  • 20
    • 0032883786 scopus 로고    scopus 로고
    • Identification of a novel actin binding motif in smooth muscle myosin light chain kinase
    • Smith, L., So, X., Lin, P., Zhi, G. and Stull, J. T. (1999). Identification of a novel actin binding motif in smooth muscle myosin light chain kinase. J. Biol. Chem. 274, 29433-29438.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29433-29438
    • Smith, L.1    So, X.2    Lin, P.3    Zhi, G.4    Stull, J.T.5
  • 23
    • 0033366539 scopus 로고    scopus 로고
    • Termination of phototransduction requires binding of the NINAC myosin III and the PDZ protein INAD
    • Wes, P. D., Xu, X. Z., Li, H. S., Chien, F., Doberstein, S. K. and Montell, C. (1999). Termination of phototransduction requires binding of the NINAC myosin III and the PDZ protein INAD. Nat. Neurosci. 2, 447-453.
    • (1999) Nat. Neurosci. , vol.2 , pp. 447-453
    • Wes, P.D.1    Xu, X.Z.2    Li, H.S.3    Chien, F.4    Doberstein, S.K.5    Montell, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.