메뉴 건너뛰기




Volumn 36, Issue 3, 1996, Pages 440-448

Molecular cloning and domain structure of human myosin-VIIa, the gene product defective in Usher syndrome 1B

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN;

EID: 0030587490     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1006/geno.1996.0489     Document Type: Article
Times cited : (118)

References (33)
  • 1
    • 10344225790 scopus 로고
    • Wizardry at the cell cortex
    • Algrain, M., Arpin, M., and Louvard, D. (1993a). Wizardry at the cell cortex. Curr. Biol. 3: 451-454.
    • (1993) Curr. Biol. , vol.3 , pp. 451-454
    • Algrain, M.1    Arpin, M.2    Louvard, D.3
  • 2
    • 0027393093 scopus 로고
    • Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker
    • Algrain, M., Turunen, O., Valheri, A., Louvard, D., and Arpin, M. (1993b). Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J. Cell Biol. 120: 129-139.
    • (1993) J. Cell Biol. , vol.120 , pp. 129-139
    • Algrain, M.1    Turunen, O.2    Valheri, A.3    Louvard, D.4    Arpin, M.5
  • 3
    • 0028231886 scopus 로고
    • Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types
    • Bement, W. M., Hasson, T., Wirth, J. A., Cheney, R. E., and Mooseker, M. S. (1994). Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. Proc. Natl. Acad. Sci. USA 91: 6549-6553.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6549-6553
    • Bement, W.M.1    Hasson, T.2    Wirth, J.A.3    Cheney, R.E.4    Mooseker, M.S.5
  • 4
    • 0027183643 scopus 로고
    • Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells
    • Berryman, M., Franck, Z., and Bretscher, A. (1993). Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. J. Cell Sci. 105: 1025-1043.
    • (1993) J. Cell Sci. , vol.105 , pp. 1025-1043
    • Berryman, M.1    Franck, Z.2    Bretscher, A.3
  • 5
    • 0024542907 scopus 로고
    • Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor
    • Bretscher, A. (1989). Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor. J. Cell Biol. 108: 921-930.
    • (1989) J. Cell Biol. , vol.108 , pp. 921-930
    • Bretscher, A.1
  • 6
    • 0029609581 scopus 로고
    • Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains
    • Bretscher, A., Gary, R., and Berryman, M. (1995). Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains. Biochemistry 34: 16830-16837.
    • (1995) Biochemistry , vol.34 , pp. 16830-16837
    • Bretscher, A.1    Gary, R.2    Berryman, M.3
  • 7
    • 0020805412 scopus 로고
    • A new protein of adhesion plaques and ruffling membranes
    • Burridge, K., and Connell, L. (1983). A new protein of adhesion plaques and ruffling membranes. J. Cell Biol. 97: 359-367.
    • (1983) J. Cell Biol. , vol.97 , pp. 359-367
    • Burridge, K.1    Connell, L.2
  • 9
    • 0026668462 scopus 로고
    • The organization of the human monoamine oxidase genes and long range physical mapping around them
    • Chen, Z.-Y., Powell, J. F., Hsu, P., Breakefield, X. O., and Craig, I. W. (1992b). The organization of the human monoamine oxidase genes and long range physical mapping around them. Genomics 14: 75-82.
    • (1992) Genomics , vol.14 , pp. 75-82
    • Chen, Z.-Y.1    Powell, J.F.2    Hsu, P.3    Breakefield, X.O.4    Craig, I.W.5
  • 11
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin, J. M., Przybyla, A. E., MacDonald, R. J., and Rutter, W. J. (1979). Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18: 5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 12
    • 0023871492 scopus 로고
    • Identification of the protein 4.1 binding site to phosphatidylserine vesicles
    • Cohen, A. M., Liu, S. C., Lawler, J., Derick, L., and Palek, J. (1988). Identification of the protein 4.1 binding site to phosphatidylserine vesicles. Biochemistry 27: 614-619.
    • (1988) Biochemistry , vol.27 , pp. 614-619
    • Cohen, A.M.1    Liu, S.C.2    Lawler, J.3    Derick, L.4    Palek, J.5
  • 13
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site
    • Gary, R., and Bretscher, A. (1995). Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site. Mol. Biol. Cell 6: 1061-1075.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1061-1075
    • Gary, R.1    Bretscher, A.2
  • 15
    • 0028280744 scopus 로고
    • The structure and function of unconventional myosins: A review
    • Hammer, J. A. (1994). The structure and function of unconventional myosins: A review. J. Muscle Res. Cell Motil. 15: 1-10.
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 1-10
    • Hammer, J.A.1
  • 16
    • 0028787263 scopus 로고
    • Expression in cochlea and retina of myosin-VIIa, the gene product defective in Usher syndrome type 1B
    • Hasson, T., Heintzelman, M. B., Santos-Sacchi, J., Corey, D. P., and Mooseker, M. S. (1995). Expression in cochlea and retina of myosin-VIIa, the gene product defective in Usher syndrome type 1B. Proc. Natl. Acad. Sci. USA 92: 9815-9819.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9815-9819
    • Hasson, T.1    Heintzelman, M.B.2    Santos-Sacchi, J.3    Corey, D.P.4    Mooseker, M.S.5
  • 17
    • 0029163054 scopus 로고
    • Molecular motors, membrane movements and physiology: Emerging roles for myosins
    • Hasson, T., and Mooseker, M. S. (1995). Molecular motors, membrane movements and physiology: Emerging roles for myosins. Curr. Opin. Cell Biol. 7: 587-594.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 587-594
    • Hasson, T.1    Mooseker, M.S.2
  • 18
    • 0025223279 scopus 로고
    • A new Acanthamoeba myosin heavy chain: Cloning of the gene and immunological identification of the polypeptide
    • Horowitz, J. A., and Hammer, J. A., III (1990). A new Acanthamoeba myosin heavy chain: Cloning of the gene and immunological identification of the polypeptide. J. Biol. Chem. 265: 20646-20652.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20646-20652
    • Horowitz, J.A.1    Hammer J.A. III2
  • 20
    • 0025781338 scopus 로고
    • Identification of a calcium-dependent calmodulin-binding domain in Xenopus membrane skeleton protein 4.1
    • Kelly, G. M., Zelus, B. D., and Moon, R. T. (1991). Identification of a calcium-dependent calmodulin-binding domain in Xenopus membrane skeleton protein 4.1. J. Biol. Chem. 266: 12469-12473.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12469-12473
    • Kelly, G.M.1    Zelus, B.D.2    Moon, R.T.3
  • 21
    • 0026760578 scopus 로고
    • Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin
    • Krieg, J., and Hunter, T. (1992). Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin. J. Biol. Chem. 267: 921-930.
    • (1992) J. Biol. Chem. , vol.267 , pp. 921-930
    • Krieg, J.1    Hunter, T.2
  • 22
    • 0028237630 scopus 로고
    • In vitro binding studies suggest a membrane-associated complex between erythroid p55, protein 4.1, and glycophorin C
    • Marfatia, S. M., Lue, R. A., Branton, D., and Chishti, A. H. (1994). In vitro binding studies suggest a membrane-associated complex between erythroid p55, protein 4.1, and glycophorin C. J. Biol. Chem. 269: 8631-8634.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8631-8634
    • Marfatia, S.M.1    Lue, R.A.2    Branton, D.3    Chishti, A.H.4
  • 24
    • 0028146835 scopus 로고
    • Identification of functional domains in the cytoskeletal protein talin
    • Niggli, V., Kaufmann, S., Goldmann, W. G., Weber, T., and Isenberg, G. (1994). Identification of functional domains in the cytoskeletal protein talin. Eur. J. Biochem. 224: 951-957.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 951-957
    • Niggli, V.1    Kaufmann, S.2    Goldmann, W.G.3    Weber, T.4    Isenberg, G.5
  • 25
    • 0025313592 scopus 로고
    • Functional studies of the domains of talin
    • Nuckolls, G. H., Turner, C. E., and Burridge, K. (1990). Functional studies of the domains of talin. J. Cell Biol. 100: 1635-1644.
    • (1990) J. Cell Biol. , vol.100 , pp. 1635-1644
    • Nuckolls, G.H.1    Turner, C.E.2    Burridge, K.3
  • 26
    • 0029966327 scopus 로고    scopus 로고
    • A novel plant calmodulin-binding protein with a kinesin heavy chain motor domain
    • Reddy, A. S. N., Safadi, F., Narasimhulu, S. B., Golovkin, M., and Hu, X. (1996). A novel plant calmodulin-binding protein with a kinesin heavy chain motor domain. J. Biol. Chem. 271: 7052-7060.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7052-7060
    • Reddy, A.S.N.1    Safadi, F.2    Narasimhulu, S.B.3    Golovkin, M.4    Hu, X.5
  • 27
    • 4243962932 scopus 로고
    • Purification and characterization of high-molecular-weight myosin I (HMMI), and unconventional myosin from Acanthamoeba
    • Repezza, M., Sellers, J., Urrutia, R., and Hammer, J. (1994). Purification and characterization of high-molecular-weight myosin I (HMMI), and unconventional myosin from Acanthamoeba. Mol. Biol. Cell (Suppl.) 5: 277a.
    • (1994) Mol. Biol. Cell , vol.5 , Issue.SUPPL.
    • Repezza, M.1    Sellers, J.2    Urrutia, R.3    Hammer, J.4
  • 28
    • 0018892655 scopus 로고
    • Two mRNAs with different 3′ ends encode membrane-bound and secreted forms of immunoglobulin μ chain
    • Roger, J., Early, P., Carter, C., Calame, K., Bond, M., Hood, L., and Wall, R. (1980). Two mRNAs with different 3′ ends encode membrane-bound and secreted forms of immunoglobulin μ chain. Cell 20: 303-312.
    • (1980) Cell , vol.20 , pp. 303-312
    • Roger, J.1    Early, P.2    Carter, C.3    Calame, K.4    Bond, M.5    Hood, L.6    Wall, R.7
  • 29
    • 0026802046 scopus 로고
    • A gene family consisting of ezrin, radixin, and moesin. Its specific localization at actin filament/plasma membrane association sites
    • Sato, N., Funayama, N., Nagafuchi, A., Yonemura, S., Tsukita, S., and Tsukita, S. (1992). A gene family consisting of ezrin, radixin, and moesin. Its specific localization at actin filament/plasma membrane association sites. J. Cell Sci. 103: 131-143.
    • (1992) J. Cell Sci. , vol.103 , pp. 131-143
    • Sato, N.1    Funayama, N.2    Nagafuchi, A.3    Yonemura, S.4    Tsukita, S.5    Tsukita, S.6
  • 30
    • 0003154314 scopus 로고
    • Molecular cloning of myosins from the bullfrog saccular macula: A candidate for the adaptation motor
    • Sole, C. K., Derfler, B. H., Duyk, G. M., and Corey, D. P. (1994). Molecular cloning of myosins from the bullfrog saccular macula: A candidate for the adaptation motor. Auditory Neurosci. 1: 63-75.
    • (1994) Auditory Neurosci. , vol.1 , pp. 63-75
    • Sole, C.K.1    Derfler, B.H.2    Duyk, G.M.3    Corey, D.P.4
  • 33
    • 0021673231 scopus 로고
    • Role of the conserved AAUAAA sequence: Four AAUAAA points prevent messenger RNA 3′ end formation
    • Wickens, M., and Stephenson, P. (1984). Role of the conserved AAUAAA sequence: Four AAUAAA points prevent messenger RNA 3′ end formation. Science 226: 1045-1051.
    • (1984) Science , vol.226 , pp. 1045-1051
    • Wickens, M.1    Stephenson, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.