메뉴 건너뛰기




Volumn 123, Issue 18, 2010, Pages 3136-3145

Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle

Author keywords

Cardiomyocytes; Leiomodin; Lmod2; Thin filament; Tropomodulin; WH2 domain

Indexed keywords

ACTIN BINDING PROTEIN; ALPHA ACTININ; F ACTIN; GREEN FLUORESCENT PROTEIN; LEIOMODIN 2; TROPOMODULIN; TROPOMODULIN 1; TROPOMYOSIN; UNCLASSIFIED DRUG;

EID: 77956930753     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.071837     Document Type: Article
Times cited : (81)

References (42)
  • 1
    • 0033214493 scopus 로고    scopus 로고
    • Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle
    • Almenar-Queralt, A., Lee, A., Conley, C. A., Ribas de Pouplana, L. and Fowler, V. M. (1999). Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle. J. Biol. Chem. 274, 28466-28475.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28466-28475
    • Almenar-Queralt, A.1    Lee, A.2    Conley, C.A.3    Ribas De Pouplana, L.4    Fowler, V.M.5
  • 2
    • 0028116302 scopus 로고
    • Isoform-specific interaction of tropomodulin with skeletal muscle and erythrocyte tropomyosins
    • Babcock, G. G. and Fowler, V. M. (1994). Isoform-specific interaction of tropomodulin with skeletal muscle and erythrocyte tropomyosins. J. Biol. Chem. 269, 27510-27518.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27510-27518
    • Babcock, G.G.1    Fowler, V.M.2
  • 3
    • 36448942505 scopus 로고    scopus 로고
    • SALS, a WH2-domain-containing protein, promotes sarcomeric actin filament elongation from pointed ends during Drosophila muscle growth
    • Bai, J., Hartwig, J. H. and Perrimon, N. (2007). SALS, a WH2-domain-containing protein, promotes sarcomeric actin filament elongation from pointed ends during Drosophila muscle growth. Dev. Cell 13, 828-842.
    • (2007) Dev. Cell , vol.13 , pp. 828-842
    • Bai, J.1    Hartwig, J.H.2    Perrimon, N.3
  • 4
    • 0041857887 scopus 로고    scopus 로고
    • Ephs and ephrins during early stages of chick embryogenesis
    • Baker, R. K. and Antin, P. B. (2003). Ephs and ephrins during early stages of chick embryogenesis. Dev. Dyn. 228, 128-142.
    • (2003) Dev. Dyn. , vol.228 , pp. 128-142
    • Baker, R.K.1    Antin, P.B.2
  • 5
    • 0020025754 scopus 로고
    • Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF)
    • Bernstein, B. W. and Bamburg, J. R. (1982). Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil. 2, 1-8.
    • (1982) Cell Motil. , vol.2 , pp. 1-8
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 7
    • 0025613855 scopus 로고
    • Tropomyosin prevents depolymerization of actin filaments from the pointed end
    • Broschat, K. O. (1990). Tropomyosin prevents depolymerization of actin filaments from the pointed end. J. Biol. Chem. 265, 21323-21329.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21323-21329
    • Broschat, K.O.1
  • 8
    • 0024421755 scopus 로고
    • Effects of CapZ, an actin capping protein of muscle, on the polymerization of actin
    • Caldwell, J. E., Heiss, S. G., Mermall, V. and Cooper, J. A. (1989). Effects of CapZ, an actin capping protein of muscle, on the polymerization of actin. Biochemistry 28, 8506-8514.
    • (1989) Biochemistry , vol.28 , pp. 8506-8514
    • Caldwell, J.E.1    Heiss, S.G.2    Mermall, V.3    Cooper, J.A.4
  • 10
    • 0344406087 scopus 로고    scopus 로고
    • E-Tmod capping of actin filaments at the slow-growing end is required to establish mouse embryonic circulation
    • Chu, X., Chen, J., Reedy, M. C., Vera, C., Sung, K. L. and Sung, L. A. (2003). E-Tmod capping of actin filaments at the slow-growing end is required to establish mouse embryonic circulation. Am. J. Physiol. Heart Circ. Physiol. 284, H1827-H1838.
    • (2003) Am. J. Physiol. Heart Circ. Physiol. , vol.284
    • Chu, X.1    Chen, J.2    Reedy, M.C.3    Vera, C.4    Sung, K.L.5    Sung, L.A.6
  • 11
    • 0034984739 scopus 로고    scopus 로고
    • Leiomodin and tropomodulin in smooth muscle
    • Conley, C. A. (2001). Leiomodin and tropomodulin in smooth muscle. Am. J. Physiol. Cell Physiol. 280, C1645-C1656.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280
    • Conley, C.A.1
  • 12
    • 0035870762 scopus 로고    scopus 로고
    • Leiomodins: Larger members of the tropomodulin (Tmod) gene family
    • Conley, C. A., Fritz-Six, K. L., Almenar-Queralt, A. and Fowler, V. M. (2001). Leiomodins: larger members of the tropomodulin (Tmod) gene family. Genomics 73, 127-139.
    • (2001) Genomics , vol.73 , pp. 127-139
    • Conley, C.A.1    Fritz-Six, K.L.2    Almenar-Queralt, A.3    Fowler, V.M.4
  • 13
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967). Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 15
    • 0020600552 scopus 로고
    • Isolation and some structural and functional properties of macrophage tropomyosin
    • Fattoum, A., Hartwig, J. H. and Stossel, T. P. (1983). Isolation and some structural and functional properties of macrophage tropomyosin. Biochemistry 22, 1187-1193. (Pubitemid 13126376)
    • (1983) Biochemistry , vol.22 , Issue.5 , pp. 1187-1193
    • Fattoum, A.1    Hartwig, J.H.2    Stossel, T.P.3
  • 16
    • 0141809370 scopus 로고    scopus 로고
    • Tropomodulin contains two actin filament pointed end-capping domains
    • Fowler, V. M., Greenfield, N. J. and Moyer, J. (2003). Tropomodulin contains two actin filament pointed end-capping domains. J. Biol. Chem. 278, 40000-40009.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40000-40009
    • Fowler, V.M.1    Greenfield, N.J.2    Moyer, J.3
  • 17
    • 0347480271 scopus 로고    scopus 로고
    • Aberrant myofibril assembly in tropomodulin1 null mice leads to aborted heart development and embryonic lethality
    • Fritz-Six, K. L., Cox, P. R., Fischer, R. S., Xu, B., Gregorio, C. C., Zoghbi, H. Y. and Fowler, V. M. (2003). Aberrant myofibril assembly in tropomodulin1 null mice leads to aborted heart development and embryonic lethality. J. Cell Biol. 163, 1033-1044.
    • (2003) J. Cell Biol. , vol.163 , pp. 1033-1044
    • Fritz-Six, K.L.1    Cox, P.R.2    Fischer, R.S.3    Xu, B.4    Gregorio, C.C.5    Zoghbi, H.Y.6    Fowler, V.M.7
  • 18
    • 0028914944 scopus 로고
    • Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: Tropomodulin requires tropomyosin for assembly
    • Gregorio, C. C. and Fowler, V. M. (1995). Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: tropomodulin requires tropomyosin for assembly. J. Cell Biol. 129, 683-695.
    • (1995) J. Cell Biol. , vol.129 , pp. 683-695
    • Gregorio, C.C.1    Fowler, V.M.2
  • 19
    • 0029166140 scopus 로고
    • Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes
    • Gregorio, C. C., Weber, A., Bondad, M., Pennise, C. R. and Fowler, V. M. (1995). Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes. Nature 377, 83-86.
    • (1995) Nature , vol.377 , pp. 83-86
    • Gregorio, C.C.1    Weber, A.2    Bondad, M.3    Pennise, C.R.4    Fowler, V.M.5
  • 20
    • 0033058418 scopus 로고    scopus 로고
    • Nonmuscle tropomyosin-4 requires coexpression with other low molecular weight isoforms for binding to thin filaments in cardiomyocytes
    • Helfman, D. M., Berthier, C., Grossman, J., Leu, M., Ehler, E., Perriard, E. and Perriard, J. C. (1999). Nonmuscle tropomyosin-4 requires coexpression with other low molecular weight isoforms for binding to thin filaments in cardiomyocytes. J. Cell Sci. 112, 371-380.
    • (1999) J. Cell Sci. , vol.112 , pp. 371-380
    • Helfman, D.M.1    Berthier, C.2    Grossman, J.3    Leu, M.4    Ehler, E.5    Perriard, E.6    Perriard, J.C.7
  • 21
    • 0017124861 scopus 로고
    • Depolymerization of F-actin by deoxyribonuclease I
    • Hitchcock, S. E., Carisson, L. and Lindberg, U. (1976). Depolymerization of F-actin by deoxyribonuclease I. Cell 7, 531-542.
    • (1976) Cell , vol.7 , pp. 531-542
    • Hitchcock, S.E.1    Carisson, L.2    Lindberg, U.3
  • 22
    • 0033565351 scopus 로고    scopus 로고
    • Tropomodulin isolated from rabbit skeletal muscle inhibits filament formation of actin in the presence of tropomyosin and troponin
    • Kimura, S., Ichikawa, A., Ishizuka, J., Ohkouchi, S., Kake, T. and Maruyama, K. (1999). Tropomodulin isolated from rabbit skeletal muscle inhibits filament formation of actin in the presence of tropomyosin and troponin. Eur. J. Biochem. 263, 396-401.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 396-401
    • Kimura, S.1    Ichikawa, A.2    Ishizuka, J.3    Ohkouchi, S.4    Kake, T.5    Maruyama, K.6
  • 23
    • 34548017691 scopus 로고    scopus 로고
    • Leiomodin/tropomyosin interactions are isoform specific
    • Kostyukova, A. S. (2007). Leiomodin/tropomyosin interactions are isoform specific. Arch. Biochem. Biophys. 465, 227-230.
    • (2007) Arch. Biochem. Biophys. , vol.465 , pp. 227-230
    • Kostyukova, A.S.1
  • 24
    • 39749176245 scopus 로고    scopus 로고
    • Tropomodulins and tropomodulin/tropomyosin interactions
    • Kostyukova, A. S. (2008). Tropomodulins and tropomodulin/tropomyosin interactions. Cell. Mol. Life Sci. 65, 563-569.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 563-569
    • Kostyukova, A.S.1
  • 25
    • 1242294519 scopus 로고    scopus 로고
    • Effect of the structure of the N terminus of tropomyosin on tropomodulin function
    • Kostyukova, A. S. and Hitchcock-DeGregori, S. E. (2004). Effect of the structure of the N terminus of tropomyosin on tropomodulin function. J. Biol. Chem. 279, 5066-5071.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5066-5071
    • Kostyukova, A.S.1    Hitchcock-DeGregori, S.E.2
  • 26
    • 0033756332 scopus 로고    scopus 로고
    • Domain structure of tropomodulin: Distinct properties of the N-terminal and C-terminal halves
    • Kostyukova, A., Maeda, K., Yamauchi, E., Krieger, I. and Maeda, Y. (2000). Domain structure of tropomodulin: distinct properties of the N-terminal and C-terminal halves. Eur. J. Biochem. 267, 6470-6475.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6470-6475
    • Kostyukova, A.1    Maeda, K.2    Yamauchi, E.3    Krieger, I.4    Maeda, Y.5
  • 27
    • 0034950529 scopus 로고    scopus 로고
    • Folding properties of functional domains of tropomodulin
    • Kostyukova, A. S., Tiktopulo, E. I. and Maeda, Y. (2001). Folding properties of functional domains of tropomodulin. Biophys. J. 81, 345-351.
    • (2001) Biophys. J. , vol.81 , pp. 345-351
    • Kostyukova, A.S.1    Tiktopulo, E.I.2    Maeda, Y.3
  • 28
    • 33749345764 scopus 로고    scopus 로고
    • Tropomodulin binds two tropomyosins: A novel model for actin filament capping
    • Kostyukova, A. S., Choy, A. and Rapp, B. A. (2006). Tropomodulin binds two tropomyosins: a novel model for actin filament capping. Biochemistry 45, 12068-12075.
    • (2006) Biochemistry , vol.45 , pp. 12068-12075
    • Kostyukova, A.S.1    Choy, A.2    Rapp, B.A.3
  • 29
    • 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
  • 30
    • 0034976418 scopus 로고    scopus 로고
    • Actin dynamics at pointed ends regulates thin filament length in striated muscle
    • Littlefield, R., Almenar-Queralt, A. and Fowler, V. M. (2001). Actin dynamics at pointed ends regulates thin filament length in striated muscle. Nat. Cell Biol. 3, 544-551.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 544-551
    • Littlefield, R.1    Almenar-Queralt, A.2    Fowler, V.M.3
  • 31
    • 24944524470 scopus 로고    scopus 로고
    • Nebulin regulates the assembly and lengths of the thin filaments in striated muscle
    • McElhinny, A. S., Schwach, C., Valichnac, M., Mount-Patrick, S. and Gregorio, C. C. (2005). Nebulin regulates the assembly and lengths of the thin filaments in striated muscle. J. Cell Biol. 170, 947-957.
    • (2005) J. Cell Biol. , vol.170 , pp. 947-957
    • McElhinny, A.S.1    Schwach, C.2    Valichnac, M.3    Mount-Patrick, S.4    Gregorio, C.C.5
  • 32
    • 58149326918 scopus 로고    scopus 로고
    • Tropomodulin1 is required in the heart but not the yolk sac for mouse embryonic development
    • McKeown, C. R., Nowak, R. B., Moyer, J., Sussman, M. A. and Fowler, V. M. (2008). Tropomodulin1 is required in the heart but not the yolk sac for mouse embryonic development. Circ. Res. 103, 1241-1248.
    • (2008) Circ. Res. , vol.103 , pp. 1241-1248
    • McKeown, C.R.1    Nowak, R.B.2    Moyer, J.3    Sussman, M.A.4    Fowler, V.M.5
  • 33
    • 0141545016 scopus 로고    scopus 로고
    • The interaction of tropomodulin with tropomyosin stabilizes thin filaments in cardiac myocytes
    • Mudry, R. E., Perry, C. N., Richards, M., Fowler, V. M. and Gregorio, C. C. (2003). The interaction of tropomodulin with tropomyosin stabilizes thin filaments in cardiac myocytes. J. Cell Biol. 162, 1057-1068.
    • (2003) J. Cell Biol. , vol.162 , pp. 1057-1068
    • Mudry, R.E.1    Perry, C.N.2    Richards, M.3    Fowler, V.M.4    Gregorio, C.C.5
  • 34
    • 0029692152 scopus 로고    scopus 로고
    • In situ hybridization analysis of chick embryos in whole mount and tissue sections
    • Nieto, M. A., Patel, K. and Wilkinson, D. G. (1996). In situ hybridization analysis of chick embryos in whole mount and tissue sections. Methods Cell Biol. 51, 219-235.
    • (1996) Methods Cell Biol. , vol.51 , pp. 219-235
    • Nieto, M.A.1    Patel, K.2    Wilkinson, D.G.3
  • 35
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics
    • DOI 10.1083/jcb.200110013
    • Ono, S. and Ono, K. (2002). Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics. J. Cell Biol. 156, 1065-1076. (Pubitemid 34839855)
    • (2002) Journal of Cell Biology , vol.156 , Issue.6 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 36
    • 20444417053 scopus 로고    scopus 로고
    • Disruption in the tropomodulin1 (Tmod1) gene compromises cardiomyocyte development in murine embryonic stem cells by arresting myofibril maturation
    • Ono, Y., Schwach, C., Antin, P. B. and Gregorio, C. C. (2005). Disruption in the tropomodulin1 (Tmod1) gene compromises cardiomyocyte development in murine embryonic stem cells by arresting myofibril maturation. Dev. Biol. 282, 336-348.
    • (2005) Dev. Biol. , vol.282 , pp. 336-348
    • Ono, Y.1    Schwach, C.2    Antin, P.B.3    Gregorio, C.C.4
  • 37
    • 48249127189 scopus 로고    scopus 로고
    • Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc
    • Pappas, C. T., Bhattacharya, N., Cooper, J. A. and Gregorio, C. C. (2008). Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc. Mol. Biol. Cell 19, 1837-1847.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1837-1847
    • Pappas, C.T.1    Bhattacharya, N.2    Cooper, J.A.3    Gregorio, C.C.4
  • 38
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard, T. D. (1986). Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 103, 2747-2754.
    • (1986) J. Cell Biol. , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 40
  • 41
    • 0028099996 scopus 로고
    • Tropomodulin caps the pointed ends of actin filaments
    • Weber, A., Pennise, C. R., Babcock, G. G. and Fowler, V. M. (1994). Tropomodulin caps the pointed ends of actin filaments. J. Cell Biol. 127, 1627-1635.
    • (1994) J. Cell Biol. , vol.127 , pp. 1627-1635
    • Weber, A.1    Pennise, C.R.2    Babcock, G.G.3    Fowler, V.M.4
  • 42
    • 45149141240 scopus 로고
    • Tropomyosin-troponin complex stabilizes the pointed ends of actin filaments against polymerization and depolymerization
    • DOI 10.1016/0014-5793(90)80118-3
    • Weigt, C., Schoepper, B. and Wegner, A. (1990). Tropomyosin-troponin complex stabilizes the pointed ends of actin filaments against polymerization and depolymerization. FEBS Lett. 260, 266-268. (Pubitemid 20042383)
    • (1990) FEBS Letters , vol.260 , Issue.2 , pp. 266-268
    • Weigt, C.1    Shoepper, B.2    Wegner, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.