메뉴 건너뛰기




Volumn 143, Issue 5, 1998, Pages 1227-1238

Nexilin: A novel actin filament-binding protein localized at cell- matrix adherens junction

Author keywords

Actin binding protein; Adherens junction; Focal contact; Integrin; Stress fiber

Indexed keywords

ACTIN BINDING PROTEIN; F ACTIN; INTEGRIN; NEXILIN; PAXILLIN; TALIN; UNCLASSIFIED DRUG; VINCULIN;

EID: 0032583119     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.5.1227     Document Type: Article
Times cited : (61)

References (81)
  • 1
    • 0016489782 scopus 로고
    • Adhesions of fibroblasts to substratum during contact inhibition observed by interference reflection microscopy
    • Abercrombie, M., and G.A. Dunn. 1975. Adhesions of fibroblasts to substratum during contact inhibition observed by interference reflection microscopy. Exp. Cell Res. 92:57-62.
    • (1975) Exp. Cell Res. , vol.92 , pp. 57-62
    • Abercrombie, M.1    Dunn, G.A.2
  • 3
    • 0030922920 scopus 로고    scopus 로고
    • Spinophilin: A novel protein phosphatase 1 binding protein localized to dendritic spines
    • Allen, P.B., C.C. Quimet, and P. Greengard. 1997. Spinophilin: a novel protein phosphatase 1 binding protein localized to dendritic spines. Proc. Natl. Acad. Sci. USA. 94:9956-9961.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9956-9961
    • Allen, P.B.1    Quimet, C.C.2    Greengard, P.3
  • 4
    • 0023000443 scopus 로고
    • Identification of a new protein localized at sites of cell-substrate adhesion
    • Beckerle, M.C. 1986. Identification of a new protein localized at sites of cell-substrate adhesion. J. Cell Biol. 103:1679-1687.
    • (1986) J. Cell Biol. , vol.103 , pp. 1679-1687
    • Beckerle, M.C.1
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0019313223 scopus 로고
    • Fimbrin, a new microfilament-associated protein present in microvilli and other cell surface structures
    • Bretscher, A., and K. Weber. 1980. Fimbrin, a new microfilament-associated protein present in microvilli and other cell surface structures. J. Cell Biol. 86: 335-340.
    • (1980) J. Cell Biol. , vol.86 , pp. 335-340
    • Bretscher, A.1    Weber, K.2
  • 9
    • 0027640146 scopus 로고
    • Microfilaments and membranes
    • Bretscher, A. 1993. Microfilaments and membranes. Curr. Opin. Cell Biol. 5:653-660.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 653-660
    • Bretscher, A.1
  • 10
    • 0020805412 scopus 로고
    • A new protein of adhesion plaques and ruffling membranes
    • Burridge, K., and L. Connell. 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
  • 12
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
    • Carlsson, L., L.E. Nystrom, I. Sundkvist, F. Markey, and U. Lindberg. 1977. Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J. Mol. Biol. 115:465-483.
    • (1977) J. Mol. Biol. , vol.115 , pp. 465-483
    • Carlsson, L.1    Nystrom, L.E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 13
    • 0026026620 scopus 로고
    • Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein
    • Chia, C.P., A.L. Hitt, and E.J. Luna. 1991. Direct binding of F-actin to ponticulin, an integral plasma membrane glycoprotein. Cell Motil. Cytoskel. 18:164-179.
    • (1991) Cell Motil. Cytoskel. , vol.18 , pp. 164-179
    • Chia, C.P.1    Hitt, A.L.2    Luna, E.J.3
  • 14
    • 0028956756 scopus 로고
    • Molecular cloning, expression, and mapping of the high affinity actin-capping domain of chicken cardiac tensin
    • Chuang, J.-Z., D.C. Lin, and S. Lin. 1995. Molecular cloning, expression, and mapping of the high affinity actin-capping domain of chicken cardiac tensin. J. Cell Biol. 128:1095-1109.
    • (1995) J. Cell Biol. , vol.128 , pp. 1095-1109
    • Chuang, J.-Z.1    Lin, D.C.2    Lin, S.3
  • 15
    • 0026075528 scopus 로고
    • Purification and characterization of zyxin, an 82,000-dalton component of adherens junctions
    • Crawford, A.W., and M.C. Beckerle. 1991. Purification and characterization of zyxin, an 82,000-dalton component of adherens junctions. J. Biol. Chem. 266: 5847-5853.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5847-5853
    • Crawford, A.W.1    Beckerle, M.C.2
  • 16
    • 0025091625 scopus 로고
    • Fimbrin is a homologue of the cytoplasmic phosphoprotein plasmin and has domains homologous with calmodulin and actin gelatin protein
    • De Arruda, M.V., S. Watson, C.-S. Lin, J. Leavitt, and P. Matsudaira. 1990. Fimbrin is a homologue of the cytoplasmic phosphoprotein plasmin and has domains homologous with calmodulin and actin gelatin protein. J. Cell Biol. 111:1064-1079.
    • (1990) J. Cell Biol. , vol.111 , pp. 1064-1079
    • De Arruda, M.V.1    Watson, S.2    Lin, C.-S.3    Leavitt, J.4    Matsudaira, P.5
  • 18
    • 0027313210 scopus 로고
    • Muscle autoantigens in thyroid-associated ophthalmopathy: The limits of molecular genetics
    • Elisei, R., D. Weightman, P. Kendall-Taylor, G. Vassart, and M. Ludgate. 1993. Muscle autoantigens in thyroid-associated ophthalmopathy: the limits of molecular genetics. J. Endocrinol. Invest. 16:533-540.
    • (1993) J. Endocrinol. Invest. , vol.16 , pp. 533-540
    • Elisei, R.1    Weightman, D.2    Kendall-Taylor, P.3    Vassart, G.4    Ludgate, M.5
  • 19
    • 0020285619 scopus 로고
    • Molecular properties and functions in vitro of chicken smooth-muscle α-actinin in comparison with those of striated-muscle α-actinins
    • Endo, T., and T. Masaki. 1982. Molecular properties and functions in vitro of chicken smooth-muscle α-actinin in comparison with those of striated-muscle α-actinins. J. Biochem. (Tokyo). 92:1457-1468.
    • (1982) J. Biochem. (Tokyo) , vol.92 , pp. 1457-1468
    • Endo, T.1    Masaki, T.2
  • 20
    • 0030245731 scopus 로고    scopus 로고
    • A model for central synaptic junctional complex formation based on the differential adhesive specificities of the cadherins
    • Fannon, A.M., and D.R. Colman. 1996. A model for central synaptic junctional complex formation based on the differential adhesive specificities of the cadherins. Neuron. 17:423-434.
    • (1996) Neuron , vol.17 , pp. 423-434
    • Fannon, A.M.1    Colman, D.R.2
  • 21
    • 0016823377 scopus 로고
    • The interaction of heavy meromyosin and subfragment 1 with actin. Physical measurements in the presence and absence of adenosine triphosphate
    • Fraser, A.B., E. Eisenberg, W.W. Kielley, and F.D. Carlson. 1975. The interaction of heavy meromyosin and subfragment 1 with actin. Physical measurements in the presence and absence of adenosine triphosphate. Biochemistry. 14:2207-2214.
    • (1975) Biochemistry , vol.14 , pp. 2207-2214
    • Fraser, A.B.1    Eisenberg, E.2    Kielley, W.W.3    Carlson, F.D.4
  • 22
    • 0018692430 scopus 로고
    • A 130K protein from chicken gizzard: Its localization at the termini of microfilament bundles in cultured chicken cells
    • Geiger, B. 1979. A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells. Cell. 18:193-205.
    • (1979) Cell , vol.18 , pp. 193-205
    • Geiger, B.1
  • 23
    • 0020637998 scopus 로고
    • Membrane-cytoskeleton interaction
    • Geiger, B. 1983. Membrane-cytoskeleton interaction. Biochim. Biophys. Acta. 737:305-341.
    • (1983) Biochim. Biophys. Acta , vol.737 , pp. 305-341
    • Geiger, B.1
  • 24
    • 0024327040 scopus 로고
    • Cytoskeleton-associated cell contacts
    • Geiger, B. 1989. Cytoskeleton-associated cell contacts. Curr. Opin. Cell Biol. 1:103-109.
    • (1989) Curr. Opin. Cell Biol. , vol.1 , pp. 103-109
    • Geiger, B.1
  • 25
    • 0025997388 scopus 로고
    • The cytoplasmic domain of adherens-type junctions
    • Geiger, B., and D. Ginsberg. 1991. The cytoplasmic domain of adherens-type junctions. Cell Motil. Cytoskel. 20:1-6.
    • (1991) Cell Motil. Cytoskel. , vol.20 , pp. 1-6
    • Geiger, B.1    Ginsberg, D.2
  • 26
    • 0022341197 scopus 로고
    • Molecular heterogeneity of adherens junctions
    • Geiger, B., T. Volk, and T. Volberg. 1985. Molecular heterogeneity of adherens junctions. J. Cell. Biol. 101:1523-1531.
    • (1985) J. Cell. Biol. , vol.101 , pp. 1523-1531
    • Geiger, B.1    Volk, T.2    Volberg, T.3
  • 27
    • 0029744106 scopus 로고    scopus 로고
    • The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts
    • Gottardi, C.J., M. Arpin, A.S. Fanning, and D. Louvard. 1996. The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts. Proc. Natl. Acad. Sci. USA. 93:10779-10784.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10779-10784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4
  • 29
    • 0028998826 scopus 로고
    • A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic
    • Hata, Y., and T.C. Südhof. 1995. A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic. J. Biol. Chem. 270: 13022-13028.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13022-13028
    • Hata, Y.1    Südhof, T.C.2
  • 30
    • 0017904573 scopus 로고
    • Cell to substratum contacts of chick fibroblasts and their relation to the microfilament system: A correlated interference-reflexion and high-voltage electron-microscope study
    • Heath, J.P., and G.A. Dunn. 1978. Cell to substratum contacts of chick fibroblasts and their relation to the microfilament system: a correlated interference-reflexion and high-voltage electron-microscope study. J. Cell Sci. 29: 197-212.
    • (1978) J. Cell Sci. , vol.29 , pp. 197-212
    • Heath, J.P.1    Dunn, G.A.2
  • 31
    • 0028670842 scopus 로고
    • Identification of a rabphilin-3A-interacting protein as GTP cyclohydrolase I in PC12 cells
    • Imazumi, K., T. Sasaki, K. Takahashi, and Y. Takai. 1994. Identification of a rabphilin-3A-interacting protein as GTP cyclohydrolase I in PC12 cells. Biochem. Biophys. Res. Commun. 205:1409-1416.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1409-1416
    • Imazumi, K.1    Sasaki, T.2    Takahashi, K.3    Takai, Y.4
  • 32
    • 0025888954 scopus 로고
    • A 220-kD undercoat-constitutive protein: Its specific localization at cadherin-based cell-cell adhesion sites
    • Itoh, M., S. Yonehara, A. Nagafuchi, Sa. Tsukita, and Sh. Tsukita. 1991. A 220-kD undercoat-constitutive protein: its specific localization at cadherin-based cell-cell adhesion sites. J. Cell Biol. 115:1449-1462.
    • (1991) J. Cell Biol. , vol.115 , pp. 1449-1462
    • Itoh, M.1    Yonehara, S.2    Nagafuchi, A.3    Tsukita, Sa.4    Tsukita, Sh.5
  • 33
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to α-catenin and actin filaments
    • Itoh, M., A. Nagafuchi, S. Moroi, and Sh. Tsukita. 1997. Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to α-catenin and actin filaments. J. Cell Biol. 138:181-192.
    • (1997) J. Cell Biol. , vol.138 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, Sh.4
  • 34
    • 0017143820 scopus 로고
    • Cell-to-substrate contacts in living fibroblasts: An interference reflexion study with an evaluation of the technique
    • Izzard, C.S., and L.R. Lochner. 1976. Cell-to-substrate contacts in living fibroblasts: an interference reflexion study with an evaluation of the technique. J. Cell Sci. 21:129-159.
    • (1976) J. Cell Sci. , vol.21 , pp. 129-159
    • Izzard, C.S.1    Lochner, L.R.2
  • 37
    • 0032030656 scopus 로고    scopus 로고
    • Integrins and GTPases in tumour cell growth, motility, and invasion
    • Keely, P., L. Parise, and R. Juliano. 1998. Integrins and GTPases in tumour cell growth, motility, and invasion. Trends Cell Biol. 8:101-107.
    • (1998) Trends Cell Biol. , vol.8 , pp. 101-107
    • Keely, P.1    Parise, L.2    Juliano, R.3
  • 38
    • 0028979956 scopus 로고
    • Interaction of α-actinin with the cadherin/catenin cell-cell adhesion complex via α-catenin
    • Knudsen, K.A., A.P. Soler, K.R. Johnson, and M.J. Wheelock. 1995. Interaction of α-actinin with the cadherin/catenin cell-cell adhesion complex via α-catenin. J. Cell Biol. 130:67-77.
    • (1995) J. Cell Biol. , vol.130 , pp. 67-77
    • Knudsen, K.A.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 39
    • 0030961752 scopus 로고    scopus 로고
    • Rho regulates association of both the ERM family and vinculin with the plasma membranes in MDCK cells
    • Kotani, H., K. Takaishi, T. Sasaki, and Y. Takai. 1997. Rho regulates association of both the ERM family and vinculin with the plasma membranes in MDCK cells. Oncogene. 14:1705-1713.
    • (1997) Oncogene , vol.14 , pp. 1705-1713
    • Kotani, H.1    Takaishi, K.2    Sasaki, T.3    Takai, Y.4
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0030459950 scopus 로고    scopus 로고
    • Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic-nuclear transport
    • Lewis, J.M., R. Baskaran, S. Taagepera, M.A. Schwartz, and J.Y. Wang. 1996. Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic-nuclear transport. Proc. Natl. Acad. Sci. USA. 93:15174-15179.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15174-15179
    • Lewis, J.M.1    Baskaran, R.2    Taagepera, S.3    Schwartz, M.A.4    Wang, J.Y.5
  • 43
    • 0026497661 scopus 로고
    • Cytoskeleton-plasma membrane interactions
    • Luna, E.J., and A.L. Hitt. 1992. Cytoskeleton-plasma membrane interactions. Science. 258:955-964.
    • (1992) Science , vol.258 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 44
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas, A. 1996. Coiled coils: new structures and new functions. Trends Biochem. Sci. 21:375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 45
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., M. Van Dyke, and J. Stock. 1991. Predicting coiled coils from protein sequences. Science. 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 47
    • 0026034515 scopus 로고
    • Modular organization of actin crosslinking proteins
    • Matsudaira, P. 1991. Modular organization of actin crosslinking proteins. Trends Biochem. Sci. 16:87-92.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 48
    • 15444340697 scopus 로고
    • Localization and subcellular distribution of smg p25A, a ras p21-like GTP-binding protein, in rat brain
    • Mizoguchi, A., S. Kim, T. Ueda, A. Kikuchi, H. Yorifuji, N. Hirooka, and Y. Takai. 1990. Localization and subcellular distribution of smg p25A, a ras p21-like GTP-binding protein, in rat brain. J. Biol. Chem. 91:257-269.
    • (1990) J. Biol. Chem. , vol.91 , pp. 257-269
    • Mizoguchi, A.1    Kim, S.2    Ueda, T.3    Kikuchi, A.4    Yorifuji, H.5    Hirooka, N.6    Takai, Y.7
  • 50
    • 0025752664 scopus 로고
    • The 102 kd cadherin-associated protein: Similarity to vinculin and posttranscriptional regulation of expression
    • Nagafuchi, A., M. Takeichi, and Sh. Tsukita. 1991. The 102 kd cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression. Cell. 65:849-857.
    • (1991) Cell , vol.65 , pp. 849-857
    • Nagafuchi, A.1    Takeichi, M.2    Tsukita, Sh.3
  • 51
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai, K., and M. Kanehisa. 1992. A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics. 14:897-911.
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 53
    • 0030967789 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: A potential mechanism for communication between sites of cell adhesion and the nucleus
    • Nix, D.A., and M.C. Beckerle. 1997. Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus. J. Cell Biol. 138:1139-1147.
    • (1997) J. Cell Biol. , vol.138 , pp. 1139-1147
    • Nix, D.A.1    Beckerle, M.C.2
  • 55
    • 0024451982 scopus 로고
    • The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species
    • Ozawa, M., H. Baribault, and R. Kemler. 1989. The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species. EMBO (Eur. Mol. Biol. Organ.) J. 8:1711-1717.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 1711-1717
    • Ozawa, M.1    Baribault, H.2    Kemler, R.3
  • 56
  • 57
    • 0028126564 scopus 로고
    • Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: A putative Rho/Rac guanine nucleotide exchange factor
    • Pasteris, N.G., A. Cadle, L.J. Losie, M.E.M. Porteous, C.E. Shwarts, R.E. Stevenson, T.W. Glover, R.S. Wilroy, and J.L. Gorski. 1994. Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: a putative Rho/Rac guanine nucleotide exchange factor. Cell. 79:669-678.
    • (1994) Cell , vol.79 , pp. 669-678
    • Pasteris, N.G.1    Cadle, A.2    Losie, L.J.3    Porteous, M.E.M.4    Shwarts, C.E.5    Stevenson, R.E.6    Glover, T.W.7    Wilroy, R.S.8    Gorski, J.L.9
  • 59
    • 0025111194 scopus 로고
    • Identification and localization of talin in chick retinal pigment epithelial cells
    • Philp, N.J., M.Y. Yoon, and R.S. Hock. 1990. Identification and localization of talin in chick retinal pigment epithelial cells. Exp. Eye Res. 51:191-198.
    • (1990) Exp. Eye Res. , vol.51 , pp. 191-198
    • Philp, N.J.1    Yoon, M.Y.2    Hock, R.S.3
  • 60
    • 0020012723 scopus 로고
    • Methods to characterize actin filament networks
    • Pollard, T.D., and J.A. Cooper. 1982. Methods to characterize actin filament networks. Methods Enzymol. 85:211-233.
    • (1982) Methods Enzymol. , vol.85 , pp. 211-233
    • Pollard, T.D.1    Cooper, J.A.2
  • 62
    • 0028981208 scopus 로고
    • α1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • Rimm, D.L., E.R. Koslov, P. Kebriaei, C.D. Cianci, and J.S. Morrow. 1995. α1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proc. Nail. Acad. Sci. USA. 92:8813-8817.
    • (1995) Proc. Nail. Acad. Sci. USA , vol.92 , pp. 8813-8817
    • Rimm, D.L.1    Koslov, E.R.2    Kebriaei, P.3    Cianci, C.D.4    Morrow, J.S.5
  • 63
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins, J., S.M. Dilworth, R.A. Laskey, and C. Dingwall. 1991. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell. 64:615-623.
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 69
    • 0023926935 scopus 로고
    • The cadherins: Cell-cell adhesion molecules controlling animal morphogenesis
    • Takeichi, M. 1988. The cadherins: cell-cell adhesion molecules controlling animal morphogenesis. Development (Camb.). 102:639-655.
    • (1988) Development (Camb.) , vol.102 , pp. 639-655
    • Takeichi, M.1
  • 70
    • 0025894092 scopus 로고
    • Cadherin cell adhesion receptors as a morphogenetic regulator
    • Takeichi, M. 1991. Cadherin cell adhesion receptors as a morphogenetic regulator. Science. 251:1451-1455.
    • (1991) Science , vol.251 , pp. 1451-1455
    • Takeichi, M.1
  • 71
    • 0030957966 scopus 로고    scopus 로고
    • SAPAPs: A family of PSD-95/SAP90-associated proteins localized at postsynaptic density
    • Takeuchi, M., Y. Hata, K. Hirao, A. Toyoda, M. Irie, and Y. Takai. 1997. SAPAPs: a family of PSD-95/SAP90-associated proteins localized at postsynaptic density. J Biol. Chem. 272:11943-11951.
    • (1997) J Biol. Chem. , vol.272 , pp. 11943-11951
    • Takeuchi, M.1    Hata, Y.2    Hirao, K.3    Toyoda, A.4    Irie, M.5    Takai, Y.6
  • 73
    • 0031081475 scopus 로고    scopus 로고
    • ERM proteins: Head-to-tail regulation of actin-plasma membrane interaction
    • Tsukita, Sa., S. Yonemura, and Sh. Tsukita. 1997. ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem. Sci. 22: 53-58.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 53-58
    • Tsukita, Sa.1    Yonemura, S.2    Tsukita, S.3
  • 74
    • 0026940189 scopus 로고
    • Molecular linkage between cadherins and actin filaments in cell-eell adherens junctions
    • Tsukita, Sh., Sa. Tsukita, A. Nagafuchi, and S. Yonemura. 1992. Molecular linkage between cadherins and actin filaments in cell-eell adherens junctions. Curr. Opin. Cell Biol. 4:834-839.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 834-839
    • Tsukita, Sh.1    Tsukita, Sa.2    Nagafuchi, A.3    Yonemura, S.4
  • 75
    • 0026245786 scopus 로고
    • Transmembrane molecular assemblies in cell-extracellular matrix interactions
    • Turner, C.E., and K. Burridge. 1991. Transmembrane molecular assemblies in cell-extracellular matrix interactions. Curr. Opin. Cell Biol. 3:849-853.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 849-853
    • Turner, C.E.1    Burridge, K.2
  • 76
    • 0025008074 scopus 로고
    • Paxillin: A new vinculin-binding protein present in focal adhesions
    • Turner, C.E., J. Glenney, Jr., and K. Burridge. 1990. Paxillin: a new vinculin-binding protein present in focal adhesions. J. Cell Biol. 111:1059-1068.
    • (1990) J. Cell Biol. , vol.111 , pp. 1059-1068
    • Turner, C.E.1    Glenney Jr., J.2    Burridge, K.3
  • 77
    • 0029807018 scopus 로고    scopus 로고
    • The catenin/cadherin adhesion system is localized in synaptic junctions bordering transmitter release zones
    • Uchida, N., Y. Honjo, K.R. Johnson, M.J. Wheelock, and M. Takeichi. 1996. The catenin/cadherin adhesion system is localized in synaptic junctions bordering transmitter release zones. J. Cell Biol. 135:767-779.
    • (1996) J. Cell Biol. , vol.135 , pp. 767-779
    • Uchida, N.1    Honjo, Y.2    Johnson, K.R.3    Wheelock, M.J.4    Takeichi, M.5
  • 78
    • 0021356621 scopus 로고
    • Unphosphorylated gelsolin is localized in regions of cell-substratum contact or attachment in Rous sarcoma virus-transformed rat cells
    • Wang, E., H.L. Yin, J.G. Krueger, L.A. Caliguiri, and I. Tamm. 1984. Unphosphorylated gelsolin is localized in regions of cell-substratum contact or attachment in Rous sarcoma virus-transformed rat cells. J. Cell Biol. 98:761-771.
    • (1984) J. Cell Biol. , vol.98 , pp. 761-771
    • Wang, E.1    Yin, H.L.2    Krueger, J.G.3    Caliguiri, L.A.4    Tamm, I.5
  • 79
    • 0023014136 scopus 로고
    • Studies on proteins that copurify with smooth muscle vinculin: Identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells
    • Wilkins, J.A., M.A. Risinger, and S. Lin. 1986. Studies on proteins that copurify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells. J. Cell Biol. 103:1483-1494.
    • (1986) J. Cell Biol. , vol.103 , pp. 1483-1494
    • Wilkins, J.A.1    Risinger, M.A.2    Lin, S.3
  • 80
    • 0030598838 scopus 로고    scopus 로고
    • An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments
    • Yang, Y., J. Dowling, Q.C. Yu, P. Kouklis, D.W. Cleveland, and E. Fuchs. 1996. An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments. Cell. 86:655-665.
    • (1996) Cell , vol.86 , pp. 655-665
    • Yang, Y.1    Dowling, J.2    Yu, Q.C.3    Kouklis, P.4    Cleveland, D.W.5    Fuchs, E.6
  • 81
    • 0030451173 scopus 로고    scopus 로고
    • The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine nucleotide exchange factor
    • Zheng, Y., D.J. Fisher, M.F. Santos, G. Tigyi, N.G. Fastens, J.L. Gorski, and Y. Xu. 1996. The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine nucleotide exchange factor. J. Biol. Chem. 271: 33169-33172.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33169-33172
    • Zheng, Y.1    Fisher, D.J.2    Santos, M.F.3    Tigyi, G.4    Fastens, N.G.5    Gorski, J.L.6    Xu, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.