Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Structural requirements for function of yeast GGAs in vacuolar protein sorting, alpha-factor maturation, and interactions with clathrin
Autore:
Mullins, C; Bonifacino, JS;
Indirizzi:
NICHHD, Cell Biol & Metab Branch, NIH, Bethesda, MD 20892 USA NICHHD Bethesda MD USA 20892 & Metab Branch, NIH, Bethesda, MD 20892 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 23, volume: 21, anno: 2001,
pagine: 7981 - 7994
SICI:
0270-7306(200112)21:23<7981:SRFFOY>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
GOLGI MEMBRANE-PROTEIN; AP-3 ADAPTER COMPLEX; SACCHAROMYCES-CEREVISIAE; GAMMA-ADAPTIN; TRANS-GOLGI; SELECTIVE TRANSPORT; GENE-PRODUCTS; DOMAIN; RECEPTOR; FAMILY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Bonifacino, JS NICHHD, Cell Biol & Metab Branch, NIH, Bldg 18T,Room 101,18Lib Dr,MSC 5430, Bethesda, MD 20892 USA NICHHD Bldg 18T,Room 101,18 Lib Dr,MSC 5430 Bethesda MD USA 20892
Citazione:
C. Mullins e J.S. Bonifacino, "Structural requirements for function of yeast GGAs in vacuolar protein sorting, alpha-factor maturation, and interactions with clathrin", MOL CELL B, 21(23), 2001, pp. 7981-7994

Abstract

The GGAs (Golgi-localized, gamma-ear-containing, ARF-binding proteins) area family of multidomain adaptor proteins involved in protein sorting at the trans-Golgi network of eukaryotic cells. Here we present results from a functional characterization of the two Saccharomyces cerevisiae GGAs, Gga1p and Gga2p. We show that deletion of both GGA genes causes defects in sorting of carboxypeptidase Y (CPY) and proteinase A to the vacuole, vacuolar morphology, and maturation of alpha -factor. A structure-function analysis reveals a requirement of the VHS, GAT, and hinge for function, while the GAE domain is less important. We identify putative clathrin-binding motifs in the hinge domain of both yeast GGAs. These motifs are shown to mediate clathrin binding in vitro. While mutation of these motifs alone does not block function of the GGAs in vivo, combining these mutations with truncations of the hinge and GAE domains diminishes function, suggesting functional cooperation between different clathrin-binding elements. Thus, these observations demonstrate that the yeast GGAs play important roles in the CPY pathway, vacuole biogenesis, and alpha -factor maturation and identify structural determinants that are critical for these functions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/10/20 alle ore 10:08:43