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Titolo:
Intracellular pH modulation of ADF/cofilin proteins
Autore:
Bernstein, BW; Painter, WB; Chen, H; Minamide, LS; Abe, H; Bamburg, JR;
Indirizzi:
Colorado State Univ, Dept Biochem & Mol Biol, Ft Collins, CO 80523 USA Colorado State Univ Ft Collins CO USA 80523 iol, Ft Collins, CO 80523 USA Colorado State Univ, Program Mol Cellular & Integrat Neurosci, Ft Collins,CO 80523 USA Colorado State Univ Ft Collins CO USA 80523 osci, Ft Collins,CO 80523 USA Chiba Univ, Dept Biol, Chiba, Japan Chiba Univ Chiba JapanChiba Univ, Dept Biol, Chiba, Japan
Titolo Testata:
CELL MOTILITY AND THE CYTOSKELETON
fascicolo: 4, volume: 47, anno: 2000,
pagine: 319 - 336
SICI:
0886-1544(200012)47:4<319:IPMOAP>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIN-DEPOLYMERIZING FACTOR; CULTURED MUSCLE-CELLS; F-ACTIN; BINDING PROTEIN; ACANTHAMOEBA ACTOPHORIN; FILAMENT TURNOVER; NA+/H+ EXCHANGE; CYTOPLASMIC PH; FACTOR COFILIN; PHORBOL ESTER;
Keywords:
actin localization; actin cytoskeleton; green fluorescent protein; ADF overexpression; cell wounding;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
81
Recensione:
Indirizzi per estratti:
Indirizzo: Bernstein, BW Colorado State Univ, Dept Biochem & Mol Biol, Ft Collins, CO80523 USA Colorado State Univ Ft Collins CO USA 80523 s, CO 80523 USA
Citazione:
B.W. Bernstein et al., "Intracellular pH modulation of ADF/cofilin proteins", CELL MOTIL, 47(4), 2000, pp. 319-336

Abstract

The ADF/cofilin (AC) proteins are necessary for the high rates of actin filament turnover seen in vivo. Their regulation is complex enough to underlie the precision in filament dynamics needed by stimulated cells. Disassembly of actin by AC proteins is inhibited in vitro by phosphorylation of ser3 and pH<7.1. This study of Swiss 3T3 cells demonstrates that pH also affectsAC behavior in vivo: (1) Wounded cells show pH-dependent AC translocation to alkaline-induced ruffling membrane; (2) The Triton extractable (soluble)ADF from Swiss 3T3 cells decreases from 42+/-4% to 23+/-4% when the intracellular pH (pH(i)) is reduced from 7.4 to 6.6; (3) Covariance and colocalization analyses of immunostained endogenous proteins show that ADF partitions more with monomeric actin and less with polymeric actin when pH(i) increases. However, the distribution of cofilin, a less pH-sensitive AC in vitro,does not change with pH; (4) Only the unphosphorylatable AC mutant (A3), when overexpressed as a GFP chimera, uniquely produces aberrant cellular phenotypes and only if the pH is shifted from 7.1 to 6.6 or 7.4. A mechanism is proposed that explains why AC(A3)-GFP and AC(wt)-GFP chimeras generate different phenotypes in response to pH changes. Phospho-AC levels increase with cell density, and in motile cells, phospho-AC increases with alkalization, suggesting a homeostatic mechanism that compensates for increased AC activity and filament turnover. These results show that the behavior of AC proteins with pH-sensitivity in vitro is affected by pH in vivo. Cell Motil. Cytoskeleton 47:319-336, 2000. (C) 2006 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 13:19:02