Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
NP/NMP4 transcription factors have distinct osteoblast nuclear matrix subdomains
Autore:
Feister, HA; Torrungruang, K; Thunyakitpisal, P; Parker, GE; Rhodes, SJ; Bidwell, JP;
Indirizzi:
Indiana Univ, Sch Dent, Dept Periodont, Indianapolis, IN 46202 USA IndianaUniv Indianapolis IN USA 46202 iodont, Indianapolis, IN 46202 USA Indiana Univ, Sch Med, Dept Anat & Cell Biol, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 l Biol, Indianapolis, IN 46202 USA Indiana Univ Purdue Univ, Dept Biol, Indianapolis, IN 46202 USA Indiana Univ Purdue Univ Indianapolis IN USA 46202 anapolis, IN 46202 USA
Titolo Testata:
JOURNAL OF CELLULAR BIOCHEMISTRY
fascicolo: 3, volume: 79, anno: 2000,
pagine: 506 - 517
SICI:
0730-2312(2000)79:3<506:NTFHDO>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
MITOTIC APPARATUS PROTEIN; I COLLAGEN PROMOTER; ZINC-FINGER MOTIFS; LOCALIZATION SIGNALS; BINDING PROTEINS; DNA-BINDING; CELL-CYCLE; DOMAINS; IDENTIFICATION; EXPRESSION;
Keywords:
bone; architectural transcription factors; CIZ; zinc fingers collagen; matrix metalloproteinases;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Bidwell, JP Indiana Univ, Sch Dent, Dept Periodont, DS235,1121 W Michigan St, Indianapolis, IN 46202 USA Indiana Univ DS235,1121 W Michigan St Indianapolis IN USA 46202
Citazione:
H.A. Feister et al., "NP/NMP4 transcription factors have distinct osteoblast nuclear matrix subdomains", J CELL BIOC, 79(3), 2000, pp. 506-517

Abstract

The mechanisms underlying the coupling of type I collagen and matrix metalloproteinase (MMP) expression to cell structure and adhesion are poorly understood. We propose that nuclear matrix architectural transcription factorslink cell structure and transcription via their association with nuclear matrix subdomains and by their capacity for altering promoter geometry. NP/NMP4 are nuclear matrix proteins that contain from five to eight Cys(2)His(2) zinc fingers. Some NP/NMP4 isoforms bind to the rat type I collagen alpha1(I) polypeptide chain promoter in the manner of architectural transcription factors and alter basal transcription in osteoblast-like cells (Thunyakitpisal ct al. in review). Certain isoforms of NP/NMP4 are identical to CIZ, Gas-interacting zinc finger protein, a nucleocytoplasmic shuttling protein that associates with focal adhesions and regulates MMP expression [Nakamotoct al. (2000): Mol Cell Biol 20:1649-1658]. To better understand the role of subnuclear architecture in collagen and MMP expression, we mapped the osteoblast nuclear distribution of NP/NMP4 proteins and identified the functional motifs necessary for nuclear localization and nuclear matrix targeting. Immunofluorescence microscopy was used to determine the cellular and subnuclear distribution of native NP/NMP4 proteins and green fluorescent protein (GFP)-NP/NMP4 fusion proteins in osteoblast-like cells. All GFP-NP/NMP4 fusion proteins localized to the nucleus, but accumulated in distinct nuclear matrix subdomains. The zinc finger domain was necessary and sufficient For nuclear import and matrix targeting. We conclude that the arrangement of the NP/NMP4 zinc fingers largely determines the subnuclear location of these isoforms. (C) 2000 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/10/20 alle ore 01:08:26