메뉴 건너뛰기




Volumn 409, Issue 3, 2008, Pages 657-667

Human α-synemin interacts directly with vinculin and metavinculin

Author keywords

Costamere; Focal adhesion; Intermediate filament; Metavinculin; Synemin; Vinculin

Indexed keywords

COSTAMERE; FOCAL ADHESION; INTERMEDIATE FILAMENTS; METAVINCULIN; SYNEMIN; VINCULIN;

EID: 38949130021     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071188     Document Type: Article
Times cited : (37)

References (51)
  • 1
    • 0018842868 scopus 로고
    • Intermediate filaments as mechanical integrators of cellular space
    • Lazarides, E. (1980) Intermediate filaments as mechanical integrators of cellular space. Nature 283, 249-256
    • (1980) Nature , vol.283 , pp. 249-256
    • Lazarides, E.1
  • 2
    • 4143134431 scopus 로고    scopus 로고
    • Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds
    • Coulombe, P. A. and Wong, P. (2004) Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds. Nat. Cell Biol. 6, 699-706
    • (2004) Nat. Cell Biol , vol.6 , pp. 699-706
    • Coulombe, P.A.1    Wong, P.2
  • 3
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function, and disease. Annu. Rev. Biochem
    • Fuchs, E. and Weber, K. (1994) Intermediate filaments: structure, dynamics, function, and disease. Annu. Rev. Biochem. 63, 345-382
    • (1994) , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 4
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann, H. and Aebi, U. (2004) Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 73, 749-789
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 5
    • 0034907507 scopus 로고    scopus 로고
    • Genes for intermediate filament proteins and the draft sequence of the human genome: Novel keratin genes and a surprisingly high number ot pseudogenes related to keratin genes 8 and 18
    • Hesse, M., Magin, T. M. and Weber, K. (2001) Genes for intermediate filament proteins and the draft sequence of the human genome: novel keratin genes and a surprisingly high number ot pseudogenes related to keratin genes 8 and 18. J. Cell Sci. 114, 2569-2575
    • (2001) J. Cell Sci , vol.114 , pp. 2569-2575
    • Hesse, M.1    Magin, T.M.2    Weber, K.3
  • 6
    • 0024347440 scopus 로고
    • Intermediate filaments
    • Robson, R. M. (1989) Intermediate filaments. Curr. Opin. Cell Biol. 1, 36-43
    • (1989) Curr. Opin. Cell Biol , vol.1 , pp. 36-43
    • Robson, R.M.1
  • 8
    • 0037335755 scopus 로고    scopus 로고
    • Molecular architecture of intermediate filaments
    • Strelkov, S. V., Herrmann, H. and Aebi, U. (2003) Molecular architecture of intermediate filaments. BioEssays 25, 243-251
    • (2003) BioEssays , vol.25 , pp. 243-251
    • Strelkov, S.V.1    Herrmann, H.2    Aebi, U.3
  • 10
    • 10744230626 scopus 로고    scopus 로고
    • Characterization of mammalian synemin, an intermediate filament protein present in all four classes of muscle cells and some neuroglial cells: Co-localization and interaction with type III intermediate filament proteins and keratins
    • Hirako, Y., Yamakawa, H., Tsujimura, Y., Nishizawa, Y., Okumura, M., Usukura, J., Matsumoto, H., Jackson, K. W., Owaribe, K. and Ohara, O. (2003) Characterization of mammalian synemin, an intermediate filament protein present in all four classes of muscle cells and some neuroglial cells: co-localization and interaction with type III intermediate filament proteins and keratins. Cell Tissue Res. 313, 195-207
    • (2003) Cell Tissue Res , vol.313 , pp. 195-207
    • Hirako, Y.1    Yamakawa, H.2    Tsujimura, Y.3    Nishizawa, Y.4    Okumura, M.5    Usukura, J.6    Matsumoto, H.7    Jackson, K.W.8    Owaribe, K.9    Ohara, O.10
  • 12
    • 33747840986 scopus 로고    scopus 로고
    • Synemin expression is widespread in liver fibrosis and is induced in proliferating and malignant biliary epithelial cells
    • Schmitt-Graeff, A., Jing, R., Nitschke, R., Desmouliere, A. and Skalli, O. (2006) Synemin expression is widespread in liver fibrosis and is induced in proliferating and malignant biliary epithelial cells. Hum. Pathol. 37, 1200-1210
    • (2006) Hum. Pathol , vol.37 , pp. 1200-1210
    • Schmitt-Graeff, A.1    Jing, R.2    Nitschke, R.3    Desmouliere, A.4    Skalli, O.5
  • 13
    • 0020096836 scopus 로고
    • Synemin and vimentin are components of intermediate filaments in avian erythrocytes
    • Granger, B. L., Repasky, E. A. and Lazarides, E. (1982) Synemin and vimentin are components of intermediate filaments in avian erythrocytes. J. Cell Biol. 92, 299-312
    • (1982) J. Cell Biol , vol.92 , pp. 299-312
    • Granger, B.L.1    Repasky, E.A.2    Lazarides, E.3
  • 14
    • 0021676702 scopus 로고
    • Expression of the intermediate-filament-associated protein synemin in chicken lens cells
    • Granger, B. L. and Lazarides, E. (1984) Expression of the intermediate-filament-associated protein synemin in chicken lens cells. Mol. Cell Biol. 4, 1943-1950
    • (1984) Mol. Cell Biol , vol.4 , pp. 1943-1950
    • Granger, B.L.1    Lazarides, E.2
  • 15
    • 0034087208 scopus 로고    scopus 로고
    • Intermediate filament protein synemin is transiently expressed in a subset of astrocytes during development
    • Sultana, S., Sernett, S. W., Bellin, R. M., Robson, R. M. and Skalli, O. (2000) Intermediate filament protein synemin is transiently expressed in a subset of astrocytes during development. Glia 30, 143-153
    • (2000) Glia , vol.30 , pp. 143-153
    • Sultana, S.1    Sernett, S.W.2    Bellin, R.M.3    Robson, R.M.4    Skalli, O.5
  • 17
    • 18244395587 scopus 로고    scopus 로고
    • Intermediate filament protein synemin is present in human reactive and malignant astrocytes and associates with ruffled membranes in astrocytoma cells
    • Jing, R., Pizzolato, G., Robson, R. M., Gabbiani, G. and Skalli, O. (2005) Intermediate filament protein synemin is present in human reactive and malignant astrocytes and associates with ruffled membranes in astrocytoma cells. Glia 50, 107-120
    • (2005) Glia , vol.50 , pp. 107-120
    • Jing, R.1    Pizzolato, G.2    Robson, R.M.3    Gabbiani, G.4    Skalli, O.5
  • 19
  • 20
    • 0032878518 scopus 로고    scopus 로고
    • Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with α-actinin may anchor synemin-containing heterofilaments
    • Bellin, R. M., Sernett, S. W., Becker, B., Ip, W., Huiatt, T. W. and Robson, R. M. (1999) Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with α-actinin may anchor synemin-containing heterofilaments. J. Biol. Chem. 274, 29493-29499
    • (1999) J. Biol. Chem , vol.274 , pp. 29493-29499
    • Bellin, R.M.1    Sernett, S.W.2    Becker, B.3    Ip, W.4    Huiatt, T.W.5    Robson, R.M.6
  • 23
    • 0035943673 scopus 로고    scopus 로고
    • Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres
    • Bellin, R. M., Huiatt, T. W., Critchley, D. R. and Robson, R. M. (2001) Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres. J. Biol. Chem. 276, 32330-32337
    • (2001) J. Biol. Chem , vol.276 , pp. 32330-32337
    • Bellin, R.M.1    Huiatt, T.W.2    Critchley, D.R.3    Robson, R.M.4
  • 24
    • 0010935732 scopus 로고
    • A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements ('costameres') mark sites of attachment between myofibrils and sarcolemma
    • Pardo, J. V., Siliciano, J. D. and Craig, S. W. (1983) A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements ('costameres') mark sites of attachment between myofibrils and sarcolemma. Proc. Natl. Acad. Sci. U.S.A. 80, 1008-1012
    • (1983) Proc. Natl. Acad. Sci. U.S.A , vol.80 , pp. 1008-1012
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 25
    • 0021009545 scopus 로고
    • γ-actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites
    • Craig, S. W. and Pardo, J. V. (1983) γ-actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites. Cell Motil. 3, 449-462
    • (1983) Cell Motil , vol.3 , pp. 449-462
    • Craig, S.W.1    Pardo, J.V.2
  • 26
    • 0038190993 scopus 로고    scopus 로고
    • Costameres: The Achilles' heel of Herculean muscle
    • Ervasti, J. M. (2003) Costameres: the Achilles' heel of Herculean muscle. J. Biol. Chem. 278, 13591-13594
    • (2003) J. Biol. Chem , vol.278 , pp. 13591-13594
    • Ervasti, J.M.1
  • 28
    • 0013523644 scopus 로고
    • Vinculin, an intracellular protein localized at specialized sites where microfilament bundles terminate at cell membranes
    • Geiger, B., Tokuyasu, K. T., Dutton, A. H. and Singer, S. J. (1980) Vinculin, an intracellular protein localized at specialized sites where microfilament bundles terminate at cell membranes. Proc. Natl. Acad, Sci. U.S.A. 77, 4127-4131
    • (1980) Proc. Natl. Acad, Sci. U.S.A , vol.77 , pp. 4127-4131
    • Geiger, B.1    Tokuyasu, K.T.2    Dutton, A.H.3    Singer, S.J.4
  • 29
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir, E. and Geiger, B. (2001) Molecular complexity and dynamics of cell-matrix adhesions. J. Cell Sci. 114, 3583-3590
    • (2001) J. Cell Sci , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 30
    • 0024205182 scopus 로고
    • cDNA-derived sequence of chicken embryo vinculin
    • Coutu, M. D. and Craig, S. W. (1988) cDNA-derived sequence of chicken embryo vinculin. Proc. Natl. Acad. Sci. U.S.A. 85, 8535-8539
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 8535-8539
    • Coutu, M.D.1    Craig, S.W.2
  • 31
    • 0026504630 scopus 로고
    • An additional exon in the human vinculin gene specifically encodes meta-vinculin-specific difference peptide. Cross-species comparison reveals variable and conserved motifs in the meta-vinculin insert
    • Koteliansky, V. E., Ogryzko, E. P., Zhidkova, N. I., Weller, P. A., Critchley, D. R., Vancompernolle, K., Vandekerckhove, J., Strasser, P., Way, M., Gimona, M. et al. (1992) An additional exon in the human vinculin gene specifically encodes meta-vinculin-specific difference peptide. Cross-species comparison reveals variable and conserved motifs in the meta-vinculin insert. Eur. J. Biochem. 204, 767-772
    • (1992) Eur. J. Biochem , vol.204 , pp. 767-772
    • Koteliansky, V.E.1    Ogryzko, E.P.2    Zhidkova, N.I.3    Weller, P.A.4    Critchley, D.R.5    Vancompernolle, K.6    Vandekerckhove, J.7    Strasser, P.8    Way, M.9    Gimona, M.10
  • 32
    • 0026748284 scopus 로고
    • Chicken vinculin and meta-vinculin are derived from a single gene by alternative splicing of a 207-base pair exon unique to meta-vinculin
    • Byrne, B. J., Kaczorowski, Y. J., Coutu, M. D. and Craig, S. W. (1992) Chicken vinculin and meta-vinculin are derived from a single gene by alternative splicing of a 207-base pair exon unique to meta-vinculin. J. Biol. Chem. 267, 12845-12850
    • (1992) J. Biol. Chem , vol.267 , pp. 12845-12850
    • Byrne, B.J.1    Kaczorowski, Y.J.2    Coutu, M.D.3    Craig, S.W.4
  • 33
    • 0035808418 scopus 로고    scopus 로고
    • The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments
    • McElhinny, A. S., Kolmerer, B., Fowler, V. M., Labeit, S. and Gregorio, C. C. (2001) The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments. J. Biol. Chem. 276, 583-592
    • (2001) J. Biol. Chem , vol.276 , pp. 583-592
    • McElhinny, A.S.1    Kolmerer, B.2    Fowler, V.M.3    Labeit, S.4    Gregorio, C.C.5
  • 34
    • 0032559997 scopus 로고    scopus 로고
    • The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate
    • Huttelmaier, S., Mayboroda, O., Harbeck, B., Jarchau, T., Jockusch, B. M. and Rudiger, M. (1998) The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate. Curr. Biol. 8, 479-488
    • (1998) Curr. Biol , vol.8 , pp. 479-488
    • Huttelmaier, S.1    Mayboroda, O.2    Harbeck, B.3    Jarchau, T.4    Jockusch, B.M.5    Rudiger, M.6
  • 36
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • Johnson, R. P. and Craig, S. W. (1995) F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 373, 261-264
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 37
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson, R. P. and Craig, S. W. (1994) An intramolecular association between the head and tail domains of vinculin modulates talin binding. J. Biol. Chem. 269, 12611-12619
    • (1994) J. Biol. Chem , vol.269 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 39
    • 0027943345 scopus 로고
    • Intramolecular interactions in vinculin control α-actinin binding to the vinculin head
    • Kroemker, M., Rudiger, A. H., Jockusch, B. M. and Rudiger, M. (1994) Intramolecular interactions in vinculin control α-actinin binding to the vinculin head. FEBS Lett. 355, 259-262
    • (1994) FEBS Lett , vol.355 , pp. 259-262
    • Kroemker, M.1    Rudiger, A.H.2    Jockusch, B.M.3    Rudiger, M.4
  • 40
    • 0030805718 scopus 로고    scopus 로고
    • Characterization of two F-actin-binding and oligomerization sites in the cell-contact protein vinculin
    • Huttelmaier, S., Bubeck, P., Rudiger, M. and Jockusch, B. M. (1997) Characterization of two F-actin-binding and oligomerization sites in the cell-contact protein vinculin. Eur. J. Biochem. 247, 1136-1142
    • (1997) Eur. J. Biochem , vol.247 , pp. 1136-1142
    • Huttelmaier, S.1    Bubeck, P.2    Rudiger, M.3    Jockusch, B.M.4
  • 41
    • 0029918344 scopus 로고    scopus 로고
    • Acidic phospholipids inhibit the intramolecular association between the N- and C-terminal regions of vinculin, exposing actin-binding and protein kinase C phosphorylation sites
    • Weekes, J., Barry, S. T. and Critchley, D. R. (1996) Acidic phospholipids inhibit the intramolecular association between the N- and C-terminal regions of vinculin, exposing actin-binding and protein kinase C phosphorylation sites. Biochem. J. 314, 827-832
    • (1996) Biochem. J , vol.314 , pp. 827-832
    • Weekes, J.1    Barry, S.T.2    Critchley, D.R.3
  • 42
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate
    • Gilmore, A. P. and Burridge, K. (1996) Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Nature 381, 531-535
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 44
    • 3242671425 scopus 로고    scopus 로고
    • The mouse synemin gene encodes three intermediate filament proteins generated by alternative exon usage and different open reading frames
    • Xue, Z. G., Cheraud, Y., Brocheriou, V., Izmiryan, A., Titeux, M., Paulin, D. and Li, Z. (2004) The mouse synemin gene encodes three intermediate filament proteins generated by alternative exon usage and different open reading frames. Exp. Cell Res. 298, 431-444
    • (2004) Exp. Cell Res , vol.298 , pp. 431-444
    • Xue, Z.G.1    Cheraud, Y.2    Brocheriou, V.3    Izmiryan, A.4    Titeux, M.5    Paulin, D.6    Li, Z.7
  • 45
    • 0026706734 scopus 로고
    • Assembly of a tail-less mutant of the intermediate filament protein, vimentin, in vitro and in vivo
    • Eckelt, A., Herrmann, H. and Franke, W. W. (1992) Assembly of a tail-less mutant of the intermediate filament protein, vimentin, in vitro and in vivo. Eur. J. Cell Biol. 58, 319-330
    • (1992) Eur. J. Cell Biol , vol.58 , pp. 319-330
    • Eckelt, A.1    Herrmann, H.2    Franke, W.W.3
  • 47
    • 0027936160 scopus 로고
    • The endless story of the glial fibrillary acidic protein
    • Chen, W. J. and Liem, R. K. (1994) The endless story of the glial fibrillary acidic protein. J. Cell Sci. 107, 2299-2311
    • (1994) J. Cell Sci , vol.107 , pp. 2299-2311
    • Chen, W.J.1    Liem, R.K.2
  • 48
    • 18844369343 scopus 로고    scopus 로고
    • Spatial distribution and functional significance of activated vinculin in living cells
    • Chen, H., Cohen, D. M., Choudhury, D. M., Kioka, N. and Craig, S. W. (2005) Spatial distribution and functional significance of activated vinculin in living cells. J. Cell Biol. 169, 459-470
    • (2005) J. Cell Biol , vol.169 , pp. 459-470
    • Chen, H.1    Cohen, D.M.2    Choudhury, D.M.3    Kioka, N.4    Craig, S.W.5
  • 49
    • 0347513188 scopus 로고    scopus 로고
    • The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress
    • Tsuruta, D. and Jones, J. C. (2003) The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress. J. Cell Sci. 116, 4977-4984
    • (2003) J. Cell Sci , vol.116 , pp. 4977-4984
    • Tsuruta, D.1    Jones, J.C.2
  • 50
    • 33646433420 scopus 로고    scopus 로고
    • Focal adhesions are hotspots for keratin filament precursor formation
    • Windoffer, R., Kolsch, A., Woll, S. and Leube, R. E. (2006) Focal adhesions are hotspots for keratin filament precursor formation. J. Cell Biol. 173, 341-348
    • (2006) J. Cell Biol , vol.173 , pp. 341-348
    • Windoffer, R.1    Kolsch, A.2    Woll, S.3    Leube, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.