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Titolo:
MOESIN, EZRIN, AND P205 ARE ACTIN-BINDING PROTEINS ASSOCIATED WITH NEUTROPHIL PLASMA-MEMBRANES
Autore:
PESTONJAMASP K; AMIEVA MR; STRASSEL CP; NAUSEEF WM; FURTHMAYR H; LUNA EJ;
Indirizzi:
WORCESTER FDN EXPTL BIOL INC,222 MAPLE AVE SHREWSBURY MA 01545 WORCESTER FDN EXPTL BIOL INC SHREWSBURY MA 01545 STANFORD UNIV,DEPT PATHOL STANFORD CA 94305 UNIV IOWA,DEPT MED IOWA CITY IA 52242
Titolo Testata:
Molecular biology of the cell
fascicolo: 3, volume: 6, anno: 1995,
pagine: 247 - 259
SICI:
1059-1524(1995)6:3<247:MEAPAA>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE KINASE SUBSTRATE; LIGAND-RECEPTOR COMPLEXES; MICROVILLAR CORE PROTEIN; EPIDERMAL GROWTH-FACTOR; DICTYOSTELIUM-DISCOIDEUM; F-ACTIN; POLYMORPHONUCLEAR LEUKOCYTES; CHEMOATTRACTANT RECEPTORS; CYTOSKELETAL LINKER; BOVINE NEUTROPHILS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
80
Recensione:
Indirizzi per estratti:
Citazione:
K. Pestonjamasp et al., "MOESIN, EZRIN, AND P205 ARE ACTIN-BINDING PROTEINS ASSOCIATED WITH NEUTROPHIL PLASMA-MEMBRANES", Molecular biology of the cell, 6(3), 1995, pp. 247-259

Abstract

Actin-binding proteins in bovine neutrophil plasma membranes were identified using blot overlays with I-125-labeled F-actin. Along with surface-biotinylated proteins, membranes were enriched in major actin-binding polypeptides of 78, 81, and 205 kDa. Binding was specific for F-actin because G-actin did not bind. Further, unlabeled F-actin blocked the binding of I-125-labeled F-actin whereas other acidic biopolymers were relatively ineffective. Binding also was specifically inhibited by myosin subfragment 1, but not by CapZ or plasma gelsolin, suggestingthat the membrane proteins, like myosin, bind along the sides of the actin filaments. The 78- and 81-kDa polypeptides were identified as moesin and ezrin, respectively, by co-migration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoprecipitation with antibodies specific for moesin and ezrin. Although not present in detectable amounts in bovine neutrophils, radixin (a third and closely relatedmember of this gene family) also bound I-125-labeled F-actin on blot overlays. Experiments with full-length and truncated bacterial fusion proteins localized the actin-binding site in moesin to the extreme carboxy terminus, a highly conserved sequence. Immunofluorescence micrographs of permeabilized cells and cell ''footprints'' showed moesin co-localization with actin at the cytoplasmic surface of the plasma membrane, consistent with a role as a membrane-actin-linking protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 03:25:59