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Titolo:
Dose-dependent linkage, assembly inhibition and disassembly of vimentin and cytokeratin 5/14 filaments through plectin's intermediate filament-binding domain
Autore:
Steinbock, FA; Nikolic, B; Coulombe, PA; Fuchs, E; Traub, P; Wiche, G;
Indirizzi:
Univ Vienna, Inst Biochem & Mol Cell Biol, Vienna Bioctr, A-1030 Vienna, Austria Univ Vienna Vienna Austria A-1030 Vienna Bioctr, A-1030 Vienna, Austria Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA JohnsHopkins Univ Baltimore MD USA 21205 l Chem, Baltimore, MD 21205 USA Johns Hopkins Univ, Sch Med, Dept Dermatol, Baltimore, MD 21205 USA Johns Hopkins Univ Baltimore MD USA 21205 rmatol, Baltimore, MD 21205 USA Univ Chicago, Howard Hughes Med Inst, Dept Mol Genet, Chicago, IL 60637 USA Univ Chicago Chicago IL USA 60637 , Dept Mol Genet, Chicago, IL 60637 USA Univ Chicago, Howard Hughes Med Inst, Dept Cell Biol, Chicago, IL 60637 USA Univ Chicago Chicago IL USA 60637 , Dept Cell Biol, Chicago, IL 60637 USA Univ Chicago, Howard Hughes Med Inst, Dept Biochem & Mol Biol, Chicago, IL60637 USA Univ Chicago Chicago IL USA 60637 iochem & Mol Biol, Chicago, IL60637 USA Max Planck Inst Zellbiol, D-68526 Ladenburg, Germany Max Planck Inst Zellbiol Ladenburg Germany D-68526 26 Ladenburg, Germany
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 3, volume: 113, anno: 2000,
pagine: 483 - 491
SICI:
0021-9533(200002)113:3<483:DLAIAD>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
BULLOUS PEMPHIGOID ANTIGEN; EPIDERMOLYSIS-BULLOSA; MUSCULAR-DYSTROPHY; CULTURED-CELLS; ROD DOMAIN; ORGANIZATION; PROTEIN; EXPRESSION; DYNAMICS; CLONING;
Keywords:
plectin; cytolinker protein; intermediate filament; vimentin; cytokeratin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Wiche, G Univ Vienna, Inst Biochem & Mol Cell Biol, Vienna Bioctr, Waehringer Guertel 18, A-1030 Vienna, Austria Univ Vienna Waehringer Guertel 18 Vienna Austria A-1030 Austria
Citazione:
F.A. Steinbock et al., "Dose-dependent linkage, assembly inhibition and disassembly of vimentin and cytokeratin 5/14 filaments through plectin's intermediate filament-binding domain", J CELL SCI, 113(3), 2000, pp. 483-491

Abstract

Plectin, the largest and most versatile member of the cytolinker/plakin family of proteins characterized to date, has a tripartite structure comprising a central 200 nm-long alpha-helical rod domain flanked by large globulardomains. The C-terminal domain comprises a short tail region preceded by six highly conserved repeats (each 28-39 kDa), one of which (repeat 5) contains plectin's intermediate filament (IF)-binding site. We used recombinant and native proteins to assess the effects of plectin repeat 5-binding to IFproteins of different types. Quantitative Eu3+-based overlay assays showedthat plectin's repeat 5 domain bound to type III IF proteins (vimentin) with preference over type I and II cytokeratins 5 and 14. The ability of bothtypes of IF proteins to self-assemble into filaments in vitro was impairedby plectin's repeat 5 domain in a concentration-dependent manner, as revealed by negative staining and rotary shadowing electron microscopy. This effect was much more pronounced in the case of vimentin compared to cytokeratins 5/14. Preassembled filaments of both types became more and more crosslinked upon incubation with increasing concentrations of plectin repeat 5, However, at high proportions of plectin to IF proteins, disassembly of filaments occurred. Again, vimentin filaments proved considerably more sensitive towards disassembly than those composed of cytokeratins 5 and 14. In general, IFs formed from recombinant proteins were found to be slightly more responsive towards plectin influences than their native counterparts. A dose-dependent plectin-inflicted collapse and putative disruption of Ifs was also observed in vivo after ectopic expression of vimentin and repeat 5 domain incotransfected deficient SW13 (vim(-)) cells. Our results suggest an involvement of plectin not only in crosslinking and plectin's deficient involvement stabilization of cytoskeletal regulation of their dynamics.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 13:27:54