메뉴 건너뛰기




Volumn 20, Issue 2, 1999, Pages 187-197

Alpha actinin-CapZ, an anchoring complex for thin filaments in Z-line

Author keywords

Alpha actinin; CapZ; Fish striated muscle; Titin; Z disc

Indexed keywords

ACTIN; ALPHA ACTININ; CAPZ; CONNECTIN; MUSCLE PROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; UNCLASSIFIED DRUG;

EID: 0032997340     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005489319058     Document Type: Article
Times cited : (77)

References (64)
  • 2
    • 0027419031 scopus 로고
    • Effects of different enzymatic treatments on the release of titin fragments from rabbit skeletal myofibrils Purification of an 800 kDa titin polypeptide
    • Astier C, Labbe JP, Roustan C and Benjamin Y (1993) Effects of different enzymatic treatments on the release of titin fragments from rabbit skeletal myofibrils Purification of an 800 kDa titin polypeptide. Biochem J 290: 731-734.
    • (1993) Biochem J , vol.290 , pp. 731-734
    • Astier, C.1    Labbe, J.P.2    Roustan, C.3    Benjamin, Y.4
  • 5
    • 0022645234 scopus 로고
    • Anti-actin antibodies. Chemical modification allows the selective production of antibodies to the N-terminal region
    • Benyamin Y, Roustan C and Boyer M (1986) Anti-actin antibodies. Chemical modification allows the selective production of antibodies to the N-terminal region. J Immunol Methods 86: 21-29.
    • (1986) J Immunol Methods , vol.86 , pp. 21-29
    • Benyamin, Y.1    Roustan, C.2    Boyer, M.3
  • 6
    • 0025329444 scopus 로고
    • Digestion of proteins associated with the Z-disc by calpain
    • Bullard B. Sainsbury G and Miller N (1990) Digestion of proteins associated with the Z-disc by calpain. J Muscle Res Cell Motil 11: 271-279.
    • (1990) J Muscle Res Cell Motil , vol.11 , pp. 271-279
    • Bullard, B.1    Sainsbury, G.2    Miller, N.3
  • 7
    • 0023372284 scopus 로고
    • (36,32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
    • (36,32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle. J Cell Biol 105: 371-379.
    • (1987) J Cell Biol , vol.105 , pp. 371-379
    • Casella, J.F.1    Craig, S.W.2    Maack, D.J.3    Brown, A.E.4
  • 8
    • 0025764370 scopus 로고
    • Purification of CapZ from chick skeletal muscle
    • Casella JF and Cooper JA (1991) Purification of CapZ from chick skeletal muscle. Meth in Enzymol 193: 140-154.
    • (1991) Meth in Enzymol , vol.193 , pp. 140-154
    • Casella, J.F.1    Cooper, J.A.2
  • 9
    • 0028173631 scopus 로고
    • 2-terminal domains of the al-and b-subunits are not required for actin capping, and alb and a2b heterodimers bind differentially to actin
    • 2-terminal domains of the al-and b-subunits are not required for actin capping, and alb and a2b heterodimers bind differentially to actin. J Biol Chem 269: 6992-6998.
    • (1994) J Biol Chem , vol.269 , pp. 6992-6998
    • Casella, J.F.1    Torres, M.A.2
  • 10
    • 0018848094 scopus 로고
    • Enzyme immunoassay ELISA and EMIT
    • Neufeld EF and Ginsberg V (eds) Academic Press, New York
    • Engvall E (1980) Enzyme immunoassay ELISA and EMIT. In: Neufeld EF and Ginsberg V (eds) Methods in Enzymology. Vol. 70 (pp. 419-439) Academic Press, New York.
    • (1980) Methods in Enzymology , vol.70 , pp. 419-439
    • Engvall, E.1
  • 12
    • 0015894257 scopus 로고
    • The structure of a simple Z-line
    • Franzini-Armstrong C (1973) The structure of a simple Z-line. J Cell Biol 58: 630-642.
    • (1973) J Cell Biol , vol.58 , pp. 630-642
    • Franzini-Armstrong, C.1
  • 13
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-biphosphate for alpha-actinin function
    • Fukami K, Furuhashi K, Inagaki M, Endo T, Hatano S and Takanawa T (1992) Requirement of phosphatidylinositol 4,5-biphosphate for alpha-actinin function. Nature 359: 150-152.
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takanawa, T.6
  • 15
    • 0023924769 scopus 로고
    • The organisation of titin filaments in the half sarcomere revealed by monoclonal antibodies in immunoelectronic microscopy: A map of ten nonrepetitive epitopes starting at the Z-line extends to the M-line
    • Fürst D, Nave R, Osborn R and Weber K (1988) The organisation of titin filaments in the half sarcomere revealed by monoclonal antibodies in immunoelectronic microscopy: a map of ten nonrepetitive epitopes starting at the Z-line extends to the M-line. J Cell Biol 160: 1563-1572.
    • (1988) J Cell Biol , vol.160 , pp. 1563-1572
    • Fürst, D.1    Nave, R.2    Osborn, R.3    Weber, K.4
  • 16
    • 0026683647 scopus 로고
    • Inositol phospholipid-induced suppression of F-actin-gelat-ing activity of smooth muscle filamin
    • Furuhashi K, Inagaki M, Hatano S, Fukami K and Takenawa T (1992) Inositol phospholipid-induced suppression of F-actin-gelat-ing activity of smooth muscle filamin. Biochem Biophys Res Commun 184: 1261-1265.
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 1261-1265
    • Furuhashi, K.1    Inagaki, M.2    Hatano, S.3    Fukami, K.4    Takenawa, T.5
  • 17
    • 0027246620 scopus 로고
    • Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts
    • Gautel M, Leonard K and Labeit S (1993) Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts. EMBO J 12: 3827-3834.
    • (1993) EMBO J , vol.12 , pp. 3827-3834
    • Gautel, M.1    Leonard, K.2    Labeit, S.3
  • 18
    • 0029859276 scopus 로고    scopus 로고
    • The central Z-disc region of titin is assembled from a novel repeat in variable copy numbers
    • Gautel M, Goulding D, Bullard B, Weber K, and Furst DO (1996) The central Z-disc region of titin is assembled from a novel repeat in variable copy numbers. J Cell Sci 109: 2747-2754.
    • (1996) J Cell Sci , vol.109 , pp. 2747-2754
    • Gautel, M.1    Goulding, D.2    Bullard, B.3    Weber, K.4    Furst, D.O.5
  • 19
    • 0031918680 scopus 로고    scopus 로고
    • A six-module human nebulin fragment bundles actin filaments and induces actin polymerization
    • Gonsior SM, Gautel M and Hinssen H (1998) A six-module human nebulin fragment bundles actin filaments and induces actin polymerization. J Muscle Res Cell Motil 19: 225-235.
    • (1998) J Muscle Res Cell Motil , vol.19 , pp. 225-235
    • Gonsior, S.M.1    Gautel, M.2    Hinssen, H.3
  • 21
    • 0025748580 scopus 로고
    • Regulation of CapZ, an actin capping protein of chicken muscle, by anionic phospholipids
    • Heiss SG and Cooper JA (1991) Regulation of CapZ, an actin capping protein of chicken muscle, by anionic phospholipids. Biochemistry 30: 8753-8758.
    • (1991) Biochemistry , vol.30 , pp. 8753-8758
    • Heiss, S.G.1    Cooper, J.A.2
  • 22
    • 0029664528 scopus 로고    scopus 로고
    • Interaction of S100a(0) protein with the actin capping protein CapZ. Characterization of a S100a(0) putative binding site in CapZ a subunit
    • Ivanenkov V, Dimlich R and Jamieson G (1996) Interaction of S100a(0) protein with the actin capping protein CapZ. Characterization of a S100a(0) putative binding site in CapZ a subunit. Biochem Biophys Res Commun 221: 46-50.
    • (1996) Biochem Biophys Res Commun , vol.221 , pp. 46-50
    • Ivanenkov, V.1    Dimlich, R.2    Jamieson, G.3
  • 25
    • 0024567044 scopus 로고
    • Gelsolin-polyphosphoinositides interaction. Full expression of gelsolin inhibiting function by polyphosphoinositides in vesicular form and inactivation by dilution, aggregation or masking of the inositol
    • Janmey PA and Stossel TP (1989) Gelsolin-polyphosphoinositides interaction. Full expression of gelsolin inhibiting function by polyphosphoinositides in vesicular form and inactivation by dilution, aggregation or masking of the inositol. J Biol Chem 264: 4825-4831.
    • (1989) J Biol Chem , vol.264 , pp. 4825-4831
    • Janmey, P.A.1    Stossel, T.P.2
  • 27
    • 0025603713 scopus 로고
    • Localization of a new α-actinin binding site on the COOH-terminal part of the actin sequence
    • Lebart MC, Mejean C, Boyer M, Roustan C and Benyamin Y (1990) Localization of a new α-actinin binding site on the COOH-terminal part of the actin sequence. Biochem Biophys Res Commun 173: 120-126.
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 120-126
    • Lebart, M.C.1    Mejean, C.2    Boyer, M.3    Roustan, C.4    Benyamin, Y.5
  • 28
    • 0027416724 scopus 로고
    • Further characterization of the α-actinin - actin interface and comparison with filamin binding sites
    • Lebart MC, Mejean C, Roustan C and Benjamin Y (1993) Further characterization of the α-actinin - actin interface and comparison with filamin binding sites. J Biol Chem 268: 5642-5648.
    • (1993) J Biol Chem , vol.268 , pp. 5642-5648
    • Lebart, M.C.1    Mejean, C.2    Roustan, C.3    Benjamin, Y.4
  • 31
    • 0025720064 scopus 로고
    • Three-dimensional reconstruction of a simple Z-band in fish muscle
    • Luther PK (1991) Three-dimensional reconstruction of a simple Z-band in fish muscle. J Cell Biol 113: 1043-1055.
    • (1991) J Cell Biol , vol.113 , pp. 1043-1055
    • Luther, P.K.1
  • 32
    • 0029566023 scopus 로고
    • Symmetry of a vertebrate muscle basketweave Z-band
    • Luther PK (1995) Symmetry of a vertebrate muscle basketweave Z-band. J Struct Biol 115(3): 275-282.
    • (1995) J Struct Biol , vol.115 , Issue.3 , pp. 275-282
    • Luther, P.K.1
  • 34
    • 0028863184 scopus 로고
    • Molecular model of an actin filament capped by a severing protein
    • McGough A, and Way M (1995) Molecular model of an actin filament capped by a severing protein. J Struct Biol 115: 144-150.
    • (1995) J Struct Biol , vol.115 , pp. 144-150
    • McGough, A.1    Way, M.2
  • 35
    • 0026774746 scopus 로고
    • Localization and identification of actin structures involved in the filamin-actin interaction
    • Mejean C, Lebart MC, Boyer M, Roustan C and Benyamin Y (1992) Localization and identification of actin structures involved in the filamin-actin interaction. Eur J Biochem 209: 555-562.
    • (1992) Eur J Biochem , vol.209 , pp. 555-562
    • Mejean, C.1    Lebart, M.C.2    Boyer, M.3    Roustan, C.4    Benyamin, Y.5
  • 37
    • 0022973726 scopus 로고
    • Isolation and characterization of a conserved actin binding domain from rat hepatic actinogelin, rat skeletal muscle, and chicken gizzard α-actinin
    • Mimura N, and Asano A (1986) Isolation and characterization of a conserved actin binding domain from rat hepatic actinogelin, rat skeletal muscle, and chicken gizzard α-actinin. J Biol Chem 261: 10680-10687.
    • (1986) J Biol Chem , vol.261 , pp. 10680-10687
    • Mimura, N.1    Asano, A.2
  • 38
    • 0025100156 scopus 로고
    • Interaction of alpha-actinin and nebulin in vitro. Support for the existence of a fourth filament system in skeletal muscle
    • Nave R, Furst DO and Weber K (1990) Interaction of alpha-actinin and nebulin in vitro. Support for the existence of a fourth filament system in skeletal muscle. FEBS Lett 269: 163-166.
    • (1990) FEBS Lett , vol.269 , pp. 163-166
    • Nave, R.1    Furst, D.O.2    Weber, K.3
  • 39
    • 0031596986 scopus 로고    scopus 로고
    • 2- exchange on the flexibility and/or conformation of the small domain in monomeric actin
    • 2- exchange on the flexibility and/or conformation of the small domain in monomeric actin. Biophys J 74: 2474-2481.
    • (1998) Biophys J , vol.74 , pp. 2474-2481
    • Nyitrai, M.1    Hild, G.2    Lakos, Z.3    Somogyi, B.4
  • 40
    • 0031560933 scopus 로고    scopus 로고
    • The N-terminal Z repeat 5 of connectin/titin binds to the C-terminal region of alpha-actinin
    • Ohtsuka H, Yajima H, Maruyama K and Kimura S (1997). The N-terminal Z repeat 5 of connectin/titin binds to the C-terminal region of alpha-actinin. Biochem Biophys Res Com 235: 1-3.
    • (1997) Biochem Biophys Res Com , vol.235 , pp. 1-3
    • Ohtsuka, H.1    Yajima, H.2    Maruyama, K.3    Kimura, S.4
  • 41
    • 0031027371 scopus 로고    scopus 로고
    • Binding of th N-terminal 63 kDa portion of connectin/titin to α-actinin as revealed by the yeast two-hybrid system
    • Ohtsuka HO, Yajima H, Maruyama K and Kimura S (1997) Binding of th N-terminal 63 kDa portion of connectin/titin to α-actinin as revealed by the yeast two-hybrid system. FEBS Lett 401: 65-67.
    • (1997) FEBS Lett , vol.401 , pp. 65-67
    • Ohtsuka, H.O.1    Yajima, H.2    Maruyama, K.3    Kimura, S.4
  • 43
    • 0027178964 scopus 로고
    • Localization of CapZ during myofibrillogenesis in cultured chicken muscle
    • Schafer DA, Waddle JA and Cooper JA (1993) Localization of CapZ during myofibrillogenesis in cultured chicken muscle. Cell Motil Cytoskelet 25: 317-35.
    • (1993) Cell Motil Cytoskelet , vol.25 , pp. 317-335
    • Schafer, D.A.1    Waddle, J.A.2    Cooper, J.A.3
  • 44
    • 0028891855 scopus 로고
    • Inhibition of CapZ during myofibrillogenesis alters assembly of actin filaments
    • Schafer DA, Hug C and Cooper JA (1995) Inhibition of CapZ during myofibrillogenesis alters assembly of actin filaments. J Cell Biol 128: 61-70.
    • (1995) J Cell Biol , vol.128 , pp. 61-70
    • Schafer, D.A.1    Hug, C.2    Cooper, J.A.3
  • 45
    • 0029795850 scopus 로고    scopus 로고
    • Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by phosphoinositides
    • Schafer D, Jennings P and Cooper J (1996) Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by phosphoinositides. J Cell Biol 135: 169-179.
    • (1996) J Cell Biol , vol.135 , pp. 169-179
    • Schafer, D.1    Jennings, P.2    Cooper, J.3
  • 46
    • 0029952579 scopus 로고    scopus 로고
    • Three dimensional structure of the Z-band in a normal mammalian skeletal muscle
    • Schroeter JP, Bretaudiere JP, Sass R and Goldstein M (1996) Three dimensional structure of the Z-band in a normal mammalian skeletal muscle. J Cell Biol 133: 571-583.
    • (1996) J Cell Biol , vol.133 , pp. 571-583
    • Schroeter, J.P.1    Bretaudiere, J.P.2    Sass, R.3    Goldstein, M.4
  • 48
    • 0024560073 scopus 로고
    • Alpha-actinin is a component of the Z-filament, a structural backbone of skeletal muscle Z-discs
    • Takahashi K and Hattori A (1989) Alpha-actinin is a component of the Z-filament, a structural backbone of skeletal muscle Z-discs. J Biochem 105: 529-536.
    • (1989) J Biochem , vol.105 , pp. 529-536
    • Takahashi, K.1    Hattori, A.2
  • 50
    • 0025877737 scopus 로고
    • Elastic filaments and giant proteins in muscle
    • Trinick J (1991) Elastic filaments and giant proteins in muscle. Curr Op Cell Biol 3: 112-119.
    • (1991) Curr Op Cell Biol , vol.3 , pp. 112-119
    • Trinick, J.1
  • 51
    • 0028091960 scopus 로고
    • Titin and nebulin: Protein rulers in muscle?
    • Trinick J (1994) Titin and nebulin: protein rulers in muscle? TIBS 19: 405-408.
    • (1994) TIBS , vol.19 , pp. 405-408
    • Trinick, J.1
  • 52
    • 0027313537 scopus 로고
    • Elastic properties of the titin filament in the Z line region of vertebrate striated muscle
    • Trombitas K and Pollack G (1993) Elastic properties of the titin filament in the Z line region of vertebrate striated muscle. J Muscle Res Cell Motil Res 14: 416-422.
    • (1993) J Muscle Res Cell Motil Res , vol.14 , pp. 416-422
    • Trombitas, K.1    Pollack, G.2
  • 53
    • 0025744006 scopus 로고
    • Vertebrate muscle Z-line structure: An electron microscopic study of negatively-stained myofibrils
    • Tskhovrebova LA (1991) Vertebrate muscle Z-line structure: an electron microscopic study of negatively-stained myofibrils. J Muscle Res Cell Motil 12: 425-438.
    • (1991) J Muscle Res Cell Motil , vol.12 , pp. 425-438
    • Tskhovrebova, L.A.1
  • 54
    • 0030662160 scopus 로고    scopus 로고
    • Analysis of long range structural effects induced by DNase-I interaction with actin monomeric form or complexed to CapZ
    • Usmanova A, Astier C, Lebart MC, Kwiatek O, Papa I, Boyer M, Roustan C and Benyamin Y (1997) Analysis of long range structural effects induced by DNase-I interaction with actin monomeric form or complexed to CapZ. Biochimie 79: 485-492.
    • (1997) Biochimie , vol.79 , pp. 485-492
    • Usmanova, A.1    Astier, C.2    Lebart, M.C.3    Kwiatek, O.4    Papa, I.5    Boyer, M.6    Roustan, C.7    Benyamin, Y.8
  • 56
    • 0028283285 scopus 로고
    • The muscle Z band: Lessons in stress management
    • Vigoreaux JO (1994) The muscle Z band: lessons in stress management. J Muscle Res Cell Motil 15: 237-255.
    • (1994) J Muscle Res Cell Motil , vol.15 , pp. 237-255
    • Vigoreaux, J.O.1
  • 57
    • 0024226674 scopus 로고
    • Architecture of the sarcomere matrix of skeletal muscle: Immunoelectronic microscopy evidence suggests that a set of parallel inextensible nebulin filaments anchored at the Z-line
    • Wang K and Wright J (1988) Architecture of the sarcomere matrix of skeletal muscle: immunoelectronic microscopy evidence suggests that a set of parallel inextensible nebulin filaments anchored at the Z-line. J Cell Biol 107: 2199-2212.
    • (1988) J Cell Biol , vol.107 , pp. 2199-2212
    • Wang, K.1    Wright, J.2
  • 58
    • 0026741734 scopus 로고
    • Interaction between titin and alpha-actinin
    • Wang SM and Jeng CJ (1992) Interaction between titin and alpha-actinin. Biomedical Res 13: 197-202.
    • (1992) Biomedical Res , vol.13 , pp. 197-202
    • Wang, S.M.1    Jeng, C.J.2
  • 59
    • 0029805084 scopus 로고    scopus 로고
    • Titin/connectin and nebulin: Giant protein rulers of muscle structure and function
    • Wang K (1996) Titin/connectin and nebulin: giant protein rulers of muscle structure and function. Adv Biophys 33: 123-134.
    • (1996) Adv Biophys , vol.33 , pp. 123-134
    • Wang, K.1
  • 60
    • 0030740644 scopus 로고    scopus 로고
    • Flexibility and fine structure of smooth-muscle α-actinin
    • Winkler J, Lünsdorf H and Jockusch BM (1997) Flexibility and fine structure of smooth-muscle α-actinin. Eur J Biochem 248: 193-199.
    • (1997) Eur J Biochem , vol.248 , pp. 193-199
    • Winkler, J.1    Lünsdorf, H.2    Jockusch, B.M.3
  • 61
    • 0022259764 scopus 로고
    • Fine structure of wide and narrow vertebrate muscle Z-lines. A proposed model and computer simulation of Z-line architecture
    • Yamaguchi M, Izumimoto M, Robson RM and Stromer MH (1985) Fine structure of wide and narrow vertebrate muscle Z-lines. A proposed model and computer simulation of Z-line architecture. J Mol Biol 184: 621-643.
    • (1985) J Mol Biol , vol.184 , pp. 621-643
    • Yamaguchi, M.1    Izumimoto, M.2    Robson, R.M.3    Stromer, M.H.4
  • 63
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disc: Two types of titin interactions lead to an asymmetrical sorting of α-actinin
    • Young P, Ferguson C, Banuelos S and Gautel M (1998) Molecular structure of the sarcomeric Z-disc: two types of titin interactions lead to an asymmetrical sorting of α-actinin. EMBO J 17: 1614-1624.
    • (1998) EMBO J , vol.17 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Banuelos, S.3    Gautel, M.4
  • 64
    • 0025651999 scopus 로고
    • gCap39, a calcium ion- and polyphosphoinositide regulated actin capping protein
    • Yu FX, Johnston PA, Sudhof TC and Yin HL (1990) gCap39, a calcium ion-and polyphosphoinositide regulated actin capping protein. Science 250: 1413-1415.
    • (1990) Science , vol.250 , pp. 1413-1415
    • Yu, F.X.1    Johnston, P.A.2    Sudhof, T.C.3    Yin, H.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.