메뉴 건너뛰기




Volumn 158, Issue 1, 2007, Pages 107-115

Assembly defects of desmin disease mutants carrying deletions in the α-helical rod domain are rescued by wild type protein

Author keywords

Assembly; Deletion mutation; Desmin; Intermediate filament disease; Myofibrillar myopathy

Indexed keywords

DESMIN;

EID: 33947307160     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.10.029     Document Type: Article
Times cited : (17)

References (43)
  • 3
    • 5144228375 scopus 로고    scopus 로고
    • The biology of desmin filaments: how do mutations affect their structure, assembly, and organisation?
    • Bär H., Strelkov S.V., Sjöberg G., Aebi U., and Herrmann H. The biology of desmin filaments: how do mutations affect their structure, assembly, and organisation?. J. Struct. Biol. 148 (2004) 137-152
    • (2004) J. Struct. Biol. , vol.148 , pp. 137-152
    • Bär, H.1    Strelkov, S.V.2    Sjöberg, G.3    Aebi, U.4    Herrmann, H.5
  • 4
    • 27244439232 scopus 로고    scopus 로고
    • Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages
    • Bär H., Mücke N., Kostareva A., Sjöberg G., Aebi U., and Herrmann H. Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages. Proc. Natl. Acad. Sci. USA 102 (2005) 15099-15104
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15099-15104
    • Bär, H.1    Mücke, N.2    Kostareva, A.3    Sjöberg, G.4    Aebi, U.5    Herrmann, H.6
  • 5
    • 33646144211 scopus 로고    scopus 로고
    • Forced expression of desmin and desmin mutants in cultured cells: impact of myopathic missense mutations in the central coiled-coil domain on network formation
    • Bär H., Kostareva A., Sjöberg G., Sejersen T., Katus H.A., and Herrmann H. Forced expression of desmin and desmin mutants in cultured cells: impact of myopathic missense mutations in the central coiled-coil domain on network formation. Exp. Cell Res. 312 (2006) 1554-1565
    • (2006) Exp. Cell Res. , vol.312 , pp. 1554-1565
    • Bär, H.1    Kostareva, A.2    Sjöberg, G.3    Sejersen, T.4    Katus, H.A.5    Herrmann, H.6
  • 7
    • 19744363995 scopus 로고    scopus 로고
    • Pathogenic effects of a novel heterozygous R350P desmin mutation on the assembly of desmin intermediate filaments in vivo and in vitro
    • Bär H., Fischer D., Goudeau B., Kley R.A., Clemen C.S., Vicart P., Herrmann H., Vorgerd M., and Schröder R. Pathogenic effects of a novel heterozygous R350P desmin mutation on the assembly of desmin intermediate filaments in vivo and in vitro. Hum. Mol. Genet. 14 (2005) 1251-1260
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1251-1260
    • Bär, H.1    Fischer, D.2    Goudeau, B.3    Kley, R.A.4    Clemen, C.S.5    Vicart, P.6    Herrmann, H.7    Vorgerd, M.8    Schröder, R.9
  • 9
    • 0018141798 scopus 로고
    • The intermediate-sized filaments in rat kangaroo PtK2 cells. II. Structure and composition of isolated filaments
    • Franke W.W., Schmid E., Osborn M., and Weber K. The intermediate-sized filaments in rat kangaroo PtK2 cells. II. Structure and composition of isolated filaments. Cytobiologie 17 (1978) 392-411
    • (1978) Cytobiologie , vol.17 , pp. 392-411
    • Franke, W.W.1    Schmid, E.2    Osborn, M.3    Weber, K.4
  • 12
    • 30044434950 scopus 로고    scopus 로고
    • A-type lamin complexes and regenerative potential: a step towards understanding laminopathic diseases?
    • Gotzmann J., and Foisner R. A-type lamin complexes and regenerative potential: a step towards understanding laminopathic diseases?. Histochem. Cell Biol. 125 (2006) 33-41
    • (2006) Histochem. Cell Biol. , vol.125 , pp. 33-41
    • Gotzmann, J.1    Foisner, R.2
  • 13
    • 0022538727 scopus 로고
    • Absence of intermediate filaments in a human adrenal cortex carcinoma-derived cell line
    • Hedberg K.K., and Chen L.B. Absence of intermediate filaments in a human adrenal cortex carcinoma-derived cell line. Exp. Cell Res. 163 (1986) 509-517
    • (1986) Exp. Cell Res. , vol.163 , pp. 509-517
    • Hedberg, K.K.1    Chen, L.B.2
  • 14
    • 0033618848 scopus 로고    scopus 로고
    • Intermediate filament assembly: temperature sensitivity and polymorphism
    • Herrmann H., and Aebi U. Intermediate filament assembly: temperature sensitivity and polymorphism. Cell Mol. Life Sci. 55 (1999) 1416-1431
    • (1999) Cell Mol. Life Sci. , vol.55 , pp. 1416-1431
    • Herrmann, H.1    Aebi, U.2
  • 15
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann H., and Aebi U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 73 (2004) 749-789
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 16
    • 0026559105 scopus 로고
    • Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly
    • Herrmann H., Hofmann I., and Franke W.W. Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly. J. Mol. Biol. 223 (1992) 637-650
    • (1992) J. Mol. Biol. , vol.223 , pp. 637-650
    • Herrmann, H.1    Hofmann, I.2    Franke, W.W.3
  • 17
    • 14244253598 scopus 로고    scopus 로고
    • Isolation, characterization, and in vitro assembly of intermediate filaments
    • Herrmann H., Kreplak L., and Aebi U. Isolation, characterization, and in vitro assembly of intermediate filaments. Method Cell Biol. 78 (2004) 3-24
    • (2004) Method Cell Biol. , vol.78 , pp. 3-24
    • Herrmann, H.1    Kreplak, L.2    Aebi, U.3
  • 18
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • Herrmann H., Haner M., Brettel M., Ku N.O., and Aebi U. Characterization of distinct early assembly units of different intermediate filament proteins. J. Mol. Biol. 286 (1999) 1403-1420
    • (1999) J. Mol. Biol. , vol.286 , pp. 1403-1420
    • Herrmann, H.1    Haner, M.2    Brettel, M.3    Ku, N.O.4    Aebi, U.5
  • 19
    • 0037282536 scopus 로고    scopus 로고
    • Functional complexity of intermediate filament cytoskeletons: from structure to assembly to gene ablation
    • Herrmann H., Hesse M., Reichenzeller M., Aebi U., and Magin T.M. Functional complexity of intermediate filament cytoskeletons: from structure to assembly to gene ablation. Int. Rev. Cytol. 223 (2003) 83-175
    • (2003) Int. Rev. Cytol. , vol.223 , pp. 83-175
    • Herrmann, H.1    Hesse, M.2    Reichenzeller, M.3    Aebi, U.4    Magin, T.M.5
  • 20
    • 0030596170 scopus 로고    scopus 로고
    • Structure and assembly properties of the intermediate filament protein vimentin: the role of its head, rod and tail domains
    • Herrmann H., Haner M., Brettel M., Müller S.A., Goldie K.N., Fedtke B., Lustig A., Franke W.W., and Aebi U. Structure and assembly properties of the intermediate filament protein vimentin: the role of its head, rod and tail domains. J. Mol. Biol. 264 (1996) 933-953
    • (1996) J. Mol. Biol. , vol.264 , pp. 933-953
    • Herrmann, H.1    Haner, M.2    Brettel, M.3    Müller, S.A.4    Goldie, K.N.5    Fedtke, B.6    Lustig, A.7    Franke, W.W.8    Aebi, U.9
  • 21
    • 0026343580 scopus 로고
    • Assembly and structure of calcium-induced thick vimentin filaments
    • Hofmann I., Herrmann H., and Franke W.W. Assembly and structure of calcium-induced thick vimentin filaments. Eur. J. Cell Biol. 56 (1991) 328-341
    • (1991) Eur. J. Cell Biol. , vol.56 , pp. 328-341
    • Hofmann, I.1    Herrmann, H.2    Franke, W.W.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0020024240 scopus 로고
    • Intermediate filaments: a chemically heterogeneous, developmentally regulated class of proteins
    • Lazarides E. Intermediate filaments: a chemically heterogeneous, developmentally regulated class of proteins. Annu. Rev. Biochem. 51 (1982) 219-250
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 219-250
    • Lazarides, E.1
  • 25
    • 33644883329 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts
    • Liu J., Chen Q., Huang W., Horak K.M., Zheng H., Mestril R., and Wang X. Impairment of the ubiquitin-proteasome system in desminopathy mouse hearts. FASEB J. 20 (2006) 362-364
    • (2006) FASEB J. , vol.20 , pp. 362-364
    • Liu, J.1    Chen, Q.2    Huang, W.3    Horak, K.M.4    Zheng, H.5    Mestril, R.6    Wang, X.7
  • 31
    • 0026729140 scopus 로고
    • In vivo expression and stoichiometric sulfation of the artificial protein sulfophilin, a polymer of tyrosine sulfation sites
    • Niehrs C., Huttner W.B., and Ruther U. In vivo expression and stoichiometric sulfation of the artificial protein sulfophilin, a polymer of tyrosine sulfation sites. J. Biol. Chem. 267 (1992) 15938-15942
    • (1992) J. Biol. Chem. , vol.267 , pp. 15938-15942
    • Niehrs, C.1    Huttner, W.B.2    Ruther, U.3
  • 32
    • 6344273968 scopus 로고    scopus 로고
    • Intermediate filament proteins and their associated diseases
    • Omary M.B., Coulombe P.A., and McLean W.H. Intermediate filament proteins and their associated diseases. N. Engl. J. Med. 351 (2004) 2087-2100
    • (2004) N. Engl. J. Med. , vol.351 , pp. 2087-2100
    • Omary, M.B.1    Coulombe, P.A.2    McLean, W.H.3
  • 34
    • 17444414616 scopus 로고    scopus 로고
    • Microdissection of the sequence and structure of intermediate filament chains
    • Parry D.A. Microdissection of the sequence and structure of intermediate filament chains. Adv. Protein Chem. 70 (2005) 113-142
    • (2005) Adv. Protein Chem. , vol.70 , pp. 113-142
    • Parry, D.A.1
  • 35
    • 33645090204 scopus 로고    scopus 로고
    • Search and destroy: the role of protein quality control in maintaining cardiac function
    • Patterson C. Search and destroy: the role of protein quality control in maintaining cardiac function. J. Mol. Cell Cardiol. 40 (2006) 438-441
    • (2006) J. Mol. Cell Cardiol. , vol.40 , pp. 438-441
    • Patterson, C.1
  • 37
    • 0023769829 scopus 로고
    • Control of myogenesis in the mouse myogenic C2 cell line by medium composition and by insulin: characterization of permissive and inducible C2 myoblasts
    • Pinset C., Montarras D., Chenevert J., Minty A., Barton P., Laurent C., and Gros F. Control of myogenesis in the mouse myogenic C2 cell line by medium composition and by insulin: characterization of permissive and inducible C2 myoblasts. Differentiation 38 (1988) 28-34
    • (1988) Differentiation , vol.38 , pp. 28-34
    • Pinset, C.1    Montarras, D.2    Chenevert, J.3    Minty, A.4    Barton, P.5    Laurent, C.6    Gros, F.7
  • 38
    • 33947331651 scopus 로고    scopus 로고
    • Pruszczyk, P., Kostera-Pruszczyk, A., Shatunov, A., Goudeau, B., Draminska, A., Takeda, K., Vicart, P., Strelkov, S.V., Goldfarb, L., Kaminska, A., 2006. Autosomal dominant restrictive cardiomyopathy with atrioventricular conduction block caused by a mutation located in a highly conserved segment of desmin coiled-coil domain. Int. J. Cardiol. (Epub ahead of print).
  • 39
    • 0030198631 scopus 로고    scopus 로고
    • Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels
    • Rogers K.R., Herrmann H., and Franke W.W. Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels. J. Struct. Biol. 117 (1996) 55-69
    • (1996) J. Struct. Biol. , vol.117 , pp. 55-69
    • Rogers, K.R.1    Herrmann, H.2    Franke, W.W.3
  • 41
    • 0035936792 scopus 로고    scopus 로고
    • The genetic basis for cardiomyopathy: from mutation identification to mechanistic paradigms
    • Seidman J.G., and Seidman C. The genetic basis for cardiomyopathy: from mutation identification to mechanistic paradigms. Cell 104 (2001) 557-567
    • (2001) Cell , vol.104 , pp. 557-567
    • Seidman, J.G.1    Seidman, C.2
  • 42
    • 0037086445 scopus 로고    scopus 로고
    • Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly
    • Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R., Aebi U., and Burkhard P. Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 21 (2002) 1255-1266
    • (2002) EMBO J. , vol.21 , pp. 1255-1266
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Wedig, T.4    Zimbelmann, R.5    Aebi, U.6    Burkhard, P.7
  • 43
    • 25144515509 scopus 로고    scopus 로고
    • Nuclear envelope, nuclear lamina, and inherited disease
    • Worman H.J., and Courvalin J.C. Nuclear envelope, nuclear lamina, and inherited disease. Int. Rev. Cytol. 246 (2005) 231-279
    • (2005) Int. Rev. Cytol. , vol.246 , pp. 231-279
    • Worman, H.J.1    Courvalin, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.