메뉴 건너뛰기




Volumn 4, Issue I, 2002, Pages

Z-line proteins: Implications for additional functions

Author keywords

Cytoskeleton; DCM; Heart failure; Z line

Indexed keywords

ALPHA ACTININ; CELL PROTEIN; LIM PROTEIN; MUSCLE PROTEIN; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG; Z LINE PROTEIN;

EID: 0036898997     PISSN: 1520765X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1520-765X(02)90105-7     Document Type: Conference Paper
Times cited : (8)

References (41)
  • 1
    • 0037178779 scopus 로고    scopus 로고
    • Converging pathways for heart development and disease: CV@CSH
    • Chien K, Olson E. Converging pathways for heart development and disease: CV@CSH. Cell 2002; 110: 153-62.
    • (2002) Cell , vol.110 , pp. 153-162
    • Chien, K.1    Olson, E.2
  • 2
    • 0034648805 scopus 로고    scopus 로고
    • Genomic circuits and the integrative biology of cardiac diseases
    • Chien KR. Genomic circuits and the integrative biology of cardiac diseases. Nature 2000; 407: 227-32.
    • (2000) Nature , vol.407 , pp. 227-232
    • Chien, K.R.1
  • 3
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the alpha-actinin rod: Molecular basis for cross-linking of actin filaments
    • Djinovic-Carugo K, Young P, Gautel M, Saraste M. Structure of the alpha-actinin rod: Molecular basis for cross-linking of actin filaments. Cell 1999; 98: 537-46.
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 5
    • 0032948848 scopus 로고    scopus 로고
    • A common nonsense mutation results in alpha-actinin-3 deficiency in the general population
    • North KN, Yang N, Wattanasirichaigoon D, et al. A common nonsense mutation results in alpha-actinin-3 deficiency in the general population. Nat Genet 1999; 21: 353-4.
    • (1999) Nat Genet , vol.21 , pp. 353-354
    • North, K.N.1    Yang, N.2    Wattanasirichaigoon, D.3
  • 6
    • 0032434538 scopus 로고    scopus 로고
    • Characterization of lethal Drosophila melanogaster alpha-actinin mutants
    • Fyrberg C, Ketchum A, Ball E, Fyrberg E. Characterization of lethal Drosophila melanogaster alpha-actinin mutants. Biochem Genet 1998; 36: 299-310.
    • (1998) Biochem Genet , vol.36 , pp. 299-310
    • Fyrberg, C.1    Ketchum, A.2    Ball, E.3    Fyrberg, E.4
  • 7
    • 0034004352 scopus 로고    scopus 로고
    • The LIM domain: Regulation by association
    • Bach I. The LIM domain: Regulation by association. Mech Dev 2000; 91: 5-17.
    • (2000) Mech Dev , vol.91 , pp. 5-17
    • Bach, I.1
  • 8
  • 9
    • 0030871066 scopus 로고    scopus 로고
    • Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression
    • Louis HA, Pino JD, Schmeichel KL, et al. Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression. J Biol Chem 1997; 272: 27484-91.
    • (1997) J Biol Chem , vol.272 , pp. 27484-27491
    • Louis, H.A.1    Pino, J.D.2    Schmeichel, K.L.3
  • 10
    • 0033520388 scopus 로고    scopus 로고
    • Stress pathways and heart failure
    • Chien KR. Stress pathways and heart failure. Cell 1999; 98: 555-8.
    • (1999) Cell , vol.98 , pp. 555-558
    • Chien, K.R.1
  • 11
    • 0030933063 scopus 로고    scopus 로고
    • MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure
    • Arber S, Hunter JJ, Ross J Jr, et al. MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure. Cell 1997; 88: 393-403.
    • (1997) Cell , vol.88 , pp. 393-403
    • Arber, S.1    Hunter, J.J.2    Ross J., Jr.3
  • 12
    • 0029864693 scopus 로고    scopus 로고
    • Report of the 1995 World Health Organization/International Society and Federation of Cardiology Task Force on the Definition and Classification of cardiomyopathies
    • Richardson P, McKenna W, Bristow M, et al. Report of the 1995 World Health Organization/International Society and Federation of Cardiology Task Force on the Definition and Classification of cardiomyopathies. Circulation 1996; 93: 841-2.
    • (1996) Circulation , vol.93 , pp. 841-842
    • Richardson, P.1    McKenna, W.2    Bristow, M.3
  • 13
    • 0034643946 scopus 로고    scopus 로고
    • Decreased expression of the cardiac LIM domain protein MLP in chronic human heart failure
    • Zolk O, Caroni P, Bohm M. Decreased expression of the cardiac LIM domain protein MLP in chronic human heart failure. Circulation 2000; 101: 2674-7.
    • (2000) Circulation , vol.101 , pp. 2674-2677
    • Zolk, O.1    Caroni, P.2    Bohm, M.3
  • 14
    • 0034509337 scopus 로고    scopus 로고
    • Down-regulation and nuclear relocation of MLP during the progression of right ventricular hypertrophy induced by chronic pressure overload
    • Ecamot-Laubriet A, De Luca K, Vandroux D, et al. Down-regulation and nuclear relocation of MLP during the progression of right ventricular hypertrophy induced by chronic pressure overload. J Mol Cell Cardiol 2000; 32: 2385-95.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 2385-2395
    • Ecamot-Laubriet, A.1    De Luca, K.2    Vandroux, D.3
  • 15
    • 0035858885 scopus 로고    scopus 로고
    • Alterations at the intercalated disk associated with the absence of muscle lim protein
    • Ehler E, Horowits R, Zuppinger C, et al. Alterations at the intercalated disk associated with the absence of muscle lim protein. J Cell Biol 2001; 153: 763-72.
    • (2001) J Cell Biol , vol.153 , pp. 763-772
    • Ehler, E.1    Horowits, R.2    Zuppinger, C.3
  • 16
    • 0041042154 scopus 로고    scopus 로고
    • FHL2, a novel tissue-specific coactivator of the androgen receptor
    • Muller JM, Isele U, Metzger E, et al. FHL2, a novel tissue-specific coactivator of the androgen receptor. EMBO J 2000; 19: 359-69.
    • (2000) EMBO J , vol.19 , pp. 359-369
    • Muller, J.M.1    Isele, U.2    Metzger, E.3
  • 17
    • 0031983193 scopus 로고    scopus 로고
    • LIM protein KyoT2 negatively regulates transcription by association with the RBP-J DNA-binding protein
    • Taniguchi Y, Furukawa T, Tun T, et al. LIM protein KyoT2 negatively regulates transcription by association with the RBP-J DNA-binding protein. Mol Cell Biol 1998; 18: 644-54.
    • (1998) Mol Cell Biol , vol.18 , pp. 644-654
    • Taniguchi, Y.1    Furukawa, T.2    Tun, T.3
  • 18
    • 0031005095 scopus 로고    scopus 로고
    • Subtractive cloning and characterization of DRAL, a novel LIM-domain protein down-regulated in rhabdomyosarcoma
    • Genini M, Schwalbe P, Scholl FA, et al. Subtractive cloning and characterization of DRAL, a novel LIM-domain protein down-regulated in rhabdomyosarcoma. DNA Cell Biol 1997; 16: 433-42.
    • (1997) DNA Cell Biol , vol.16 , pp. 433-442
    • Genini, M.1    Schwalbe, P.2    Scholl, F.A.3
  • 19
    • 0034735595 scopus 로고    scopus 로고
    • DRAL is a p53-responsive gene whose four and a half LIM domain protein product induces apoptosis
    • Scholl FA, McLoughlin P, Ehler E, et al. DRAL is a p53-responsive gene whose four and a half LIM domain protein product induces apoptosis. J Cell Biol 2000; 151: 495-506.
    • (2000) J Cell Biol , vol.151 , pp. 495-506
    • Scholl, F.A.1    McLoughlin, P.2    Ehler, E.3
  • 20
    • 0035173456 scopus 로고    scopus 로고
    • Translocation of a human focal adhesion LIM-only protein, FHL2, during myofibrillogenesis and identification of LIM2 as the principal determinants of FHL2 focal adhesion localization
    • Li HY, Kotaka M, Kostin S, et al. Translocation of a human focal adhesion LIM-only protein, FHL2, during myofibrillogenesis and identification of LIM2 as the principal determinants of FHL2 focal adhesion localization. Cell Motil Cytoskeleton 2001; 48: 11-23.
    • (2001) Cell Motil Cytoskeleton , vol.48 , pp. 11-23
    • Li, H.Y.1    Kotaka, M.2    Kostin, S.3
  • 21
    • 0033805096 scopus 로고    scopus 로고
    • FHL2 (SLIM3) is not essential for cardiac development and function
    • Chu PH, Bardwell WM, Gu Y, et al. FHL2 (SLIM3) is not essential for cardiac development and function. Mol Cell Biol 2000; 20: 7460-2.
    • (2000) Mol Cell Biol , vol.20 , pp. 7460-7462
    • Chu, P.H.1    Bardwell, W.M.2    Gu, Y.3
  • 22
    • 0035811023 scopus 로고    scopus 로고
    • Cardiac-specific LIM protein FHL2 modifies the hypertrophic response to beta-adrenergic stimulation
    • Kong Y, Shelton JM, Rothermel B, et al. Cardiac-specific LIM protein FHL2 modifies the hypertrophic response to beta-adrenergic stimulation. Circulation 2001; 103: 2731-8.
    • (2001) Circulation , vol.103 , pp. 2731-2738
    • Kong, Y.1    Shelton, J.M.2    Rothermel, B.3
  • 23
    • 0033018828 scopus 로고    scopus 로고
    • The PDZ domain of the LIM protein enigma binds to beta-tropomyosin
    • Guy PM, Kenny DA, Gill GN. The PDZ domain of the LIM protein enigma binds to beta-tropomyosin. Mol Biol Cell 1999; 10: 1973-84.
    • (1999) Mol Biol Cell , vol.10 , pp. 1973-1984
    • Guy, P.M.1    Kenny, D.A.2    Gill, G.N.3
  • 24
    • 0035033212 scopus 로고    scopus 로고
    • Adult mice deficient in actinin-associated LIM-domain protein reveal a developmental pathway for right ventricular cardiomyopathy
    • Pashmforoush M, Pomies P, Peterson KL, et al. Adult mice deficient in actinin-associated LIM-domain protein reveal a developmental pathway for right ventricular cardiomyopathy. Nat Med 2001; 7: 591-7.
    • (2001) Nat Med , vol.7 , pp. 591-597
    • Pashmforoush, M.1    Pomies, P.2    Peterson, K.L.3
  • 25
    • 0029962498 scopus 로고    scopus 로고
    • Protein-protein interaction of zinc finger LIM domains with protein kinase C
    • Kuroda S, Tokunaga C, Kiyohara Y, et al. Protein-protein interaction of zinc finger LIM domains with protein kinase C. J Biol Chem 1996; 271: 31029-32.
    • (1996) J Biol Chem , vol.271 , pp. 31029-31032
    • Kuroda, S.1    Tokunaga, C.2    Kiyohara, Y.3
  • 26
    • 84924110084 scopus 로고    scopus 로고
    • Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy
    • Zhou Q, Chu PH, Huang C, et al. Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy. J Cell Biol 2001; 155: 605-12.
    • (2001) J Cell Biol , vol.155 , pp. 605-612
    • Zhou, Q.1    Chu, P.H.2    Huang, C.3
  • 27
    • 17544369411 scopus 로고    scopus 로고
    • Mitogenic signaling by Ret/ptc2 requires association with enigma via a LIM domain
    • Durick K, Wu RY, Gill GN, Taylor SS. Mitogenic signaling by Ret/ptc2 requires association with enigma via a LIM domain. J Biol Chem 1996; 271: 12691-4.
    • (1996) J Biol Chem , vol.271 , pp. 12691-12694
    • Durick, K.1    Wu, R.Y.2    Gill, G.N.3    Taylor, S.S.4
  • 28
    • 0028061406 scopus 로고
    • LIM domain recognition of a tyrosine-containing tight turn
    • Wu RY, Gill GN. LIM domain recognition of a tyrosine-containing tight turn. J Biol Chem 1994; 269: 25085-90.
    • (1994) J Biol Chem , vol.269 , pp. 25085-25090
    • Wu, R.Y.1    Gill, G.N.2
  • 29
    • 0034679297 scopus 로고    scopus 로고
    • Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease)
    • McKoy G, Protonotarios N, Crosby A, et al. Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease). Lancet 2000; 355: 2119-24.
    • (2000) Lancet , vol.355 , pp. 2119-2124
    • McKoy, G.1    Protonotarios, N.2    Crosby, A.3
  • 30
    • 0034731460 scopus 로고    scopus 로고
    • FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle
    • Faulkner G, Pallavicini A, Comelli A, et al. FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. J Biol Chem 2000; 275: 41234-42.
    • (2000) J Biol Chem , vol.275 , pp. 41234-41242
    • Faulkner, G.1    Pallavicini, A.2    Comelli, A.3
  • 31
    • 0034687814 scopus 로고    scopus 로고
    • Calsarcins, a novel family of sarcomeric calcineurin-binding proteins
    • Frey N, Richardson JA, Olson EN. Calsarcins, a novel family of sarcomeric calcineurin-binding proteins. Proc Natl Acad Sci USA 2000; 97: 14632-7.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14632-14637
    • Frey, N.1    Richardson, J.A.2    Olson, E.N.3
  • 32
    • 0035852783 scopus 로고    scopus 로고
    • Myozenin: An alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines
    • Takada F, Vander Woude DL, Tong HQ, et al. Myozenin: An alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines. Proc Natl Acad Sci USA 2001; 98: 1595-600.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1595-1600
    • Takada, F.1    Vander Woude, D.L.2    Tong, H.Q.3
  • 33
    • 0037134462 scopus 로고    scopus 로고
    • Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins
    • Frey N, Olson EN. Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins. J Biol Chem 2002; 277: 13998-4004.
    • (2002) J Biol Chem , vol.277 , pp. 13998-14004
    • Frey, N.1    Olson, E.N.2
  • 34
    • 0035897410 scopus 로고    scopus 로고
    • Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies
    • Bang ML, Mudry RE, McElhinny AS, et al. Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies. J Cell Biol 2001; 153: 413-27.
    • (2001) J Cell Biol , vol.153 , pp. 413-427
    • Bang, M.L.1    Mudry, R.E.2    McElhinny, A.S.3
  • 35
    • 0028944298 scopus 로고
    • Identification and characterization of a novel cytokine-inducible nuclear protein from human endothelial cells
    • Chu W, Bums DK, Swerlick RA, Presky DH. Identification and characterization of a novel cytokine-inducible nuclear protein from human endothelial cells. J Biol Chem 1995; 270: 10236-45.
    • (1995) J Biol Chem , vol.270 , pp. 10236-10245
    • Chu, W.1    Bums, D.K.2    Swerlick, R.A.3    Presky, D.H.4
  • 36
    • 0031029447 scopus 로고    scopus 로고
    • CARP, a cardiac ankyrin repeat protein, is downstream in the Nkx2-5 homeobox gene pathway
    • Zou Y, Evans S, Chen J, et al. CARP, a cardiac ankyrin repeat protein, is downstream in the Nkx2-5 homeobox gene pathway. Development 1997; 124: 793-804.
    • (1997) Development , vol.124 , pp. 793-804
    • Zou, Y.1    Evans, S.2    Chen, J.3
  • 37
    • 0031590316 scopus 로고    scopus 로고
    • Telethonin, a novel sarcomeric protein of heart and skeletal muscle
    • Valle G, Faulkner G, De Antoni A, et al. Telethonin, a novel sarcomeric protein of heart and skeletal muscle. FEBS Lett 1997; 415: 163-8.
    • (1997) FEBS Lett , vol.415 , pp. 163-168
    • Valle, G.1    Faulkner, G.2    De Antoni, A.3
  • 38
    • 0032538660 scopus 로고    scopus 로고
    • The NH2 terminus of titin spans the Z-disc: Its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity
    • Gregorio CC, Trombitas K, Centner T, et al. The NH2 terminus of titin spans the Z-disc: Its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity. J Cell Biol 1998; 143: 1013-27.
    • (1998) J Cell Biol , vol.143 , pp. 1013-1027
    • Gregorio, C.C.1    Trombitas, K.2    Centner, T.3
  • 39
    • 0032578901 scopus 로고    scopus 로고
    • Structural basis for activation of the titin kinase domain during myofibrillogenesis
    • Mayans O, van der Ven PF, Wilm M, et al. Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature 1998; 395: 863-9.
    • (1998) Nature , vol.395 , pp. 863-869
    • Mayans, O.1    Van der Ven, P.F.2    Wilm, M.3
  • 40
    • 0033954004 scopus 로고    scopus 로고
    • Limb-girdle muscular dystrophy type 2G is caused by mutations in the gene encoding the sarcomeric protein telethonin
    • Moreira ES, Wiltshire TJ, Faulkner G, et al. Limb-girdle muscular dystrophy type 2G is caused by mutations in the gene encoding the sarcomeric protein telethonin. Nat Genet 2000; 24: 163-6.
    • (2000) Nat Genet , vol.24 , pp. 163-166
    • Moreira, E.S.1    Wiltshire, T.J.2    Faulkner, G.3
  • 41
    • 0035798418 scopus 로고    scopus 로고
    • Specific interaction of the potassium channel beta-subunit mink with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system
    • Furukawa T, Ono Y, Tsuchiya H, et al. Specific interaction of the potassium channel beta-subunit mink with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system. J Mol Biol 2001; 313: 775-84.
    • (2001) J Mol Biol , vol.313 , pp. 775-784
    • Furukawa, T.1    Ono, Y.2    Tsuchiya, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.