Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A high molecular weight intermediate filament-associated protein in BHK-21cells is nestin, a type VI intermediate filament protein - Limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV alpha-internexin
Autore:
Steinert, PM; Chou, YH; Prahlad, V; Parry, DAD; Marekov, LN; Wu, KC; Jang, SI; Goldman, RD;
Indirizzi:
NIAMSD, Skin Biol Lab, NIH, Bethesda, MD 20892 USA NIAMSD Bethesda MD USA20892 , Skin Biol Lab, NIH, Bethesda, MD 20892 USA Northwestern Univ, Sch Med, Dept Cell & Mol Biol, Chicago, IL 60611 USA Northwestern Univ Chicago IL USA 60611 & Mol Biol, Chicago, IL 60611 USA Massey Univ, Inst Fundamental Sci, Palmerston North, New Zealand Massey Univ Palmerston North New Zealand Palmerston North, New Zealand
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 14, volume: 274, anno: 1999,
pagine: 9881 - 9890
SICI:
0021-9258(19990402)274:14<9881:AHMWIF>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
COILED-COIL; NF-L; END DOMAINS; ROD DOMAIN; IN-VIVO; INVITRO; EXPRESSION; MOUSE; RAT; GENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Steinert, PM NIAMSD, Skin Biol Lab, NIH, Bldg 6,Rm 425,9000 Rockville Pike, Bethesda, MD NIAMSD Bldg 6,Rm 425,9000 Rockville Pike Bethesda MD USA 20892
Citazione:
P.M. Steinert et al., "A high molecular weight intermediate filament-associated protein in BHK-21cells is nestin, a type VI intermediate filament protein - Limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV alpha-internexin", J BIOL CHEM, 274(14), 1999, pp. 9881-9890

Abstract

BHK-21 fibroblasts contain type III vimentin/desmin intermediate filament (IF) proteins that typically coisolate and co-cycle in in vitro experimentswith certain high molecular weight proteins. Here, we report purification of one of these and demonstrate that it is in fact the type VI IF protein nestin, Nestin is expressed in several fibroblastic but not epithelioid celllines. We show that nestin forms homodimers and homotetramers but does notform IF by itself in vitro, In mixtures, nestin preferentially co-assembles with purified vimentin or the type IV IF protein alpha-internexin to formheterodimer coiled-coil molecules. These molecules may co-assemble into 10nm IF provided that the total amount of nestin does not exceed about 25%. However, nestin does not dimerize with types I/II keratin IF chains. The bulk of the nestin protein consists of a long carboxyl-terminal tail composedof various highly charged peptide repeats. By analogy with the larger neurofilament chains, we postulate that these sequences serve as cross-bridgersor spacers between IF and/or other cytoskeletal constituents. In this way,we propose that direct incorporation of modest amounts of nestin into the backbone of cytoplasmic types III and IV Ifs affords a simple yet flexible method for the regulation of their dynamic supramolecular organization and function in cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/02/20 alle ore 15:04:34