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Titolo:
THE HUMAN ARP2 3 COMPLEX IS COMPOSED OF EVOLUTIONARILY CONSERVED SUBUNITS AND IS LOCALIZED TO CELLULAR REGIONS OF DYNAMIC ACTIN FILAMENT ASSEMBLY/
Autore:
WELCH MD; DEPACE AH; VERMA S; IWAMATSU A; MITCHISON TJ;
Indirizzi:
UNIV CALIF SAN FRANCISCO,DEPT CELLULAR & MOL PHARMACOL,513 PARNASSUS AVE SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS SAN FRANCISCO CA 94143 KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL YOKOHAMA KANAGAWA JAPAN
Titolo Testata:
The Journal of cell biology
fascicolo: 2, volume: 138, anno: 1997,
pagine: 375 - 384
SICI:
0021-9525(1997)138:2<375:THA3CI>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
LISTERIA-MONOCYTOGENES; PROTEINS; MOTILITY; CELLS; GENE; POLYMERIZATION; ACANTHAMOEBA; PURIFICATION; ORGANIZATION; PROFILIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
M.D. Welch et al., "THE HUMAN ARP2 3 COMPLEX IS COMPOSED OF EVOLUTIONARILY CONSERVED SUBUNITS AND IS LOCALIZED TO CELLULAR REGIONS OF DYNAMIC ACTIN FILAMENT ASSEMBLY/", The Journal of cell biology, 138(2), 1997, pp. 375-384

Abstract

The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells. The human complex consists of seven subunits which include the actin related proteins Arp2 and Arp3, and five others referred to as p41-Arc, p34-Arc, p21-Arc, p20-Arc, and p16-Arc (Arp complex), We have determined the predicted amino acid sequence of all seven subunits. Each has homologues in diverse eukaryotes, implying that the structure and function of the complex has been conserved through evolution, Human Arp2 and Arp3 are very similar to family members from other species. p41-Arc is a new member of the Sop2 family of WD (tryptophan and aspartate) repeat-containing proteins and may be posttranslationally modified, suggesting that it may be involved in regulating the activity and/or localization of the complex. p34-Arc, p21-Arc, p20-Arc, and p16-Arc define novel protein families, We sought to evaluate the function of the Arp2/3 complex in cells by determining its intracellular distribution, Arp3, p34-Arc, and p21-Arc were localized to the lamellipodia of stationary and locomoting fibroblasts, as well to Listeria monocytogenes assembled actin tails. They were not detected in cellular bundles of actin filaments. Taken together with the abilityof the Arp2/3 complex to induce actin polymerization, these observations suggest that the complex promotes actin assembly in lamellipodia and may participate in lamellipodial protrusion.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/21 alle ore 16:28:22