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Titolo:
An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles
Autore:
Engqvist-Goldstein, AEY; Kessels, MM; Chopra, VS; Hayden, MR; Drubin, DG;
Indirizzi:
Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 ll Biol, Berkeley, CA 94720 USA Univ British Columbia, Womens & Childrens Hosp, Dept Med Genet, Ctr Mol Med & Therapeut, Vancouver, BC V5Z 4H4, Canada Univ British Columbia Vancouver BC Canada V5Z 4H4 ver, BC V5Z 4H4, Canada
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 7, volume: 147, anno: 1999,
pagine: 1503 - 1518
SICI:
0021-9525(199912)147:7<1503:AAPOTS>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR-MEDIATED ENDOCYTOSIS; CYCLASE-ASSOCIATED PROTEIN; SACCHAROMYCES-CEREVISIAE; INTERNALIZATION STEP; FILAMENT TURNOVER; CYTOCHALASIN-D; LATRUNCULIN-A; IN-VIVO; YEAST; CELLS;
Keywords:
actin; endocytosis; clathrin; Huntington disease; vesicle;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Drubin, DG Univ Calif Berkeley, Dept Mol & Cell Biol, 401 Barker Hall, Berkeley, CA 94720 USA Univ Calif Berkeley 401 Barker Hall Berkeley CA USA 94720 0 USA
Citazione:
A.E.Y. Engqvist-Goldstein et al., "An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles", J CELL BIOL, 147(7), 1999, pp. 1503-1518

Abstract

The actin cytoskeleton has been implicated in endocytosis, yet few molecules that link these systems have been identified. Here, we have cloned and characterized mHip1R, a protein that is closely related to huntingtin interacting protein 1 (Hip1). These two proteins are mammalian homologues of Sla2p, an actin-binding protein important for actin organization and endocytosis in yeast. Sequence alignments and secondary structure predictions verified that mHip1R belongs to the Sla2 protein family. Thus, mHip1R contains an NH2-terminal domain homologous to that implicated in Sla2p's endocytic function, three predicted coiled-coils, a leucine zipper, and a talin-like actin-binding domain at the COOH terminus. The talin-like domain of mHip1R binds to F-actin in vitro and colocalizes with F-actin in vivo, indicating thatthis activity has been conserved from yeast to mammals. mHip1R shows a punctate immunolocalization and is enriched at the cell cortex and in the perinuclear region. We concluded that the cortical localization represents endocytic compartments, because mHip1R colocalizes with clathrin, AP-2, and endocytosed transferrin, and because mHip1R fractionates biochemically with clathrin-coated vesicles. Time-lapse video microscopy of mHip1R-green fluorescence protein (GFP) revealed a blinking behavior similar to that reported for GFP-clathrin, and an actin-dependent inward movement of punctate structures from the cell periphery. These data show that mHip1R is a component of clathrin-coated pits and vesicles and suggest that it might link the endocytic machinery to the actin cytoskeleton.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/05/20 alle ore 13:30:49