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Volumn 27, Issue 1, 2006, Pages 45-51

Smooth muscle α-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; ALPHA ACTININ; FESSELIN; SPECTRIN; UNCLASSIFIED DRUG;

EID: 33746053239     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-005-9053-2     Document Type: Article
Times cited : (11)

References (25)
  • 1
    • 18244384042 scopus 로고    scopus 로고
    • Synaptopodin regulates the actin-bundling activity of α-actinin in an isoform-specific manner
    • Asanuma K, Kim K, Oh J, Giardino L, Chabanis S, Faul C, Reiser J and Mundel P (2005) Synaptopodin regulates the actin-bundling activity of α-actinin in an isoform-specific manner. J Clin Invest 115: 1188-1198.
    • (2005) J Clin Invest , vol.115 , pp. 1188-1198
    • Asanuma, K.1    Kim, K.2    Oh, J.3    Giardino, L.4    Chabanis, S.5    Faul, C.6    Reiser, J.7    Mundel, P.8
  • 2
    • 0023632004 scopus 로고
    • The sequence of chick alpha actinin reveals homologies to spectrin and calmodulin
    • Baron MD, Davison MD, Jones P and Critchley DR (1987) The sequence of chick alpha actinin reveals homologies to spectrin and calmodulin. J Biol Chem 262: 17623-17629.
    • (1987) J Biol Chem , vol.262 , pp. 17623-17629
    • Baron, M.D.1    Davison, M.D.2    Jones, P.3    Critchley, D.R.4
  • 3
    • 0035960656 scopus 로고    scopus 로고
    • Fesselin a synaptopodin-like protein, stimulates actin nucleation and polymerization
    • Beall B and Chalovich JM (2001) Fesselin a synaptopodin-like protein, stimulates actin nucleation and polymerization. Biochemistry 40: 14252-14259.
    • (2001) Biochemistry , vol.40 , pp. 14252-14259
    • Beall, B.1    Chalovich, J.M.2
  • 5
    • 0021111905 scopus 로고
    • On the mechanism of actin monomer-polymer subunit exchange at steady state
    • Brenner SL and Korn ED (1983) On the mechanism of actin monomer-polymer subunit exchange at steady state. J Biol Chem 258: 5013-5020.
    • (1983) J Biol Chem , vol.258 , pp. 5013-5020
    • Brenner, S.L.1    Korn, E.D.2
  • 7
    • 0001672080 scopus 로고
    • Evidence for a refractory state of heavy meromyosin and subfragment-1 unable to bind to actin in the presence of ATP
    • Eisenberg E and Kielley WW (1972) Evidence for a refractory state of heavy meromyosin and subfragment-1 unable to bind to actin in the presence of ATP. Cold Spring Harbor Symp Quant Biol 37: 145-152.
    • (1972) Cold Spring Harbor Symp Quant Biol , vol.37 , pp. 145-152
    • Eisenberg, E.1    Kielley, W.W.2
  • 8
    • 0019320755 scopus 로고
    • A rapid purification of A-actinin, filamin, and a 130,000-dalton protein from smooth muscle
    • Feramisco JR and Burridge K (1980) A rapid purification of A-actinin, filamin, and a 130,000-dalton protein from smooth muscle. J Biol Chem 255: 1194-1199.
    • (1980) J Biol Chem , vol.255 , pp. 1194-1199
    • Feramisco, J.R.1    Burridge, K.2
  • 10
    • 0024278676 scopus 로고
    • Substructure and higher structure of chicken smooth muscle alpha-actinin molecule
    • Imamura M, Endo T, Kuroda M, Tanaka T and Masaki T (1988) Substructure and higher structure of chicken smooth muscle alpha-actinin molecule. J Biol Chem 263: 7800-7805.
    • (1988) J Biol Chem , vol.263 , pp. 7800-7805
    • Imamura, M.1    Endo, T.2    Kuroda, M.3    Tanaka, T.4    Masaki, T.5
  • 11
    • 4644363346 scopus 로고    scopus 로고
    • Fesselin is a target protein for calmodulin in a calcium-dependent manner
    • Kolakowski J, Wrzosek A and Dabrowska R (2004) Fesselin is a target protein for calmodulin in a calcium-dependent manner. Biochem Biophys Res Commun 323: 1251-1256.
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 1251-1256
    • Kolakowski, J.1    Wrzosek, A.2    Dabrowska, R.3
  • 12
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labeled F-actin: Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama T and Mihashi K (1981) Fluorimetry study of N-(1-pyrenyl) iodoacetamide-labeled F-actin: local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur J Biochem 114: 33-38.
    • (1981) Eur J Biochem , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 13
    • 13244265661 scopus 로고    scopus 로고
    • Synaptopodin, a molecule involved in the formation of the dendritic spine apparatus, is a dual actin/α-actinin binding protein
    • Kremerskothen J, Plaas C, Kindler S, Frotscher M and Barnekow A (2005) Synaptopodin, a molecule involved in the formation of the dendritic spine apparatus, is a dual actin/α-actinin binding protein. J Neurochem 92: 597-606.
    • (2005) J Neurochem , vol.92 , pp. 597-606
    • Kremerskothen, J.1    Plaas, C.2    Kindler, S.3    Frotscher, M.4    Barnekow, A.5
  • 14
    • 0028208411 scopus 로고
    • Conformational change of skeletal muscle alpha-actinin induced by salt
    • Kuroda M, Kohira Y and Sasaki M (1994) Conformational change of skeletal muscle alpha-actinin induced by salt. Biochim Biophys Acta 1205: 97-104.
    • (1994) Biochim Biophys Acta , vol.1205 , pp. 97-104
    • Kuroda, M.1    Kohira, Y.2    Sasaki, M.3
  • 17
    • 0032786904 scopus 로고    scopus 로고
    • Calponin interaction with α-actinin-actin: Evidence for a structural role for calponin
    • Leinweber B, Tang JX, Stafford WF and Chalovich JM (1999) Calponin interaction with α-actinin-actin: Evidence for a structural role for calponin. Biophys J 77: 3208-3217.
    • (1999) Biophys J , vol.77 , pp. 3208-3217
    • Leinweber, B.1    Tang, J.X.2    Stafford, W.F.3    Chalovich, J.M.4
  • 18
    • 0030816323 scopus 로고    scopus 로고
    • Synaptopodin: An actin-associated protein in telencephalic dendrites and renal podocytes
    • Mundel P, Heid HW, Mundel TM, Krüger M, Reiser J and Kriz W (1997) Synaptopodin: An actin-associated protein in telencephalic dendrites and renal podocytes. J Cell Biol 139: 193-204.
    • (1997) J Cell Biol , vol.139 , pp. 193-204
    • Mundel, P.1    Heid, H.W.2    Mundel, T.M.3    Krüger, M.4    Reiser, J.5    Kriz, W.6
  • 19
    • 2442481067 scopus 로고    scopus 로고
    • α-Actinin revisited: A fresh look at an old player
    • Otey CA and Carpen O (2004) α-Actinin revisited: a fresh look at an old player. Cell Motil Cytoskel 58: 104-111.
    • (2004) Cell Motil Cytoskel , vol.58 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 20
    • 0037119361 scopus 로고    scopus 로고
    • Interaction of two actin-binding proteins, synaptopodin and α-actinin-4, with the tight junction protein MAGI-1
    • Patrie KM, Drescher AJ, Welihinda A, Mundel P and Margolis B (2002) Interaction of two actin-binding proteins, synaptopodin and α-actinin-4, with the tight junction protein MAGI-1,. J Biol Chem 277: 30183-30190.
    • (2002) J Biol Chem , vol.277 , pp. 30183-30190
    • Patrie, K.M.1    Drescher, A.J.2    Welihinda, A.3    Mundel, P.4    Margolis, B.5
  • 21
    • 0020012723 scopus 로고
    • Methods to characterize actin filament networks
    • Pollard TD and Cooper JA (1982) Methods to characterize actin filament networks. Method Enzymol 85: 211-233.
    • (1982) Method Enzymol , vol.85 , pp. 211-233
    • Pollard, T.D.1    Cooper, J.A.2
  • 22
    • 7244245361 scopus 로고    scopus 로고
    • 2+-calmodulin regulates fesselin-induced actin polymerization
    • 2+-calmodulin regulates fesselin-induced actin polymerization. Biochemistry 43: 13875-13882.
    • (2004) Biochemistry , vol.43 , pp. 13875-13882
    • Schroeter, M.1    Chalovich, J.M.2
  • 23
    • 28444478088 scopus 로고    scopus 로고
    • Fesselin binds to actin and myosin and inhibits actin activated ATPase activity
    • Schroeter MM and Chalovich JM (2005) Fesselin binds to actin and myosin and inhibits actin activated ATPase activity. J Muscle Res Cell Motil 26: 183-189.
    • (2005) J Muscle Res Cell Motil , vol.26 , pp. 183-189
    • Schroeter, M.M.1    Chalovich, J.M.2
  • 24
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA and Watt S (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246: 4866-4871.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 25
    • 0035851920 scopus 로고    scopus 로고
    • Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein
    • Weins A, Schwarz K, Faul C, Barisoni L, Linke WA and Mundel P (2001) Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein. J Cell Biol 155: 393-404.
    • (2001) J Cell Biol , vol.155 , pp. 393-404
    • Weins, A.1    Schwarz, K.2    Faul, C.3    Barisoni, L.4    Linke, W.A.5    Mundel, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.