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Enthoprotin : a novel clathrin-associated protein identified through subcellular proteomics

Wasiak Sylwia, Legendre-Guillemin Valérie, Puertollano Rosa, Blondeau François, Girard Martine, de Heuvel Elaine, Boismenu Daniel, Bell Alexander W., Bonifacino Juan S. et McPherson Peter S.. (2002). Enthoprotin : a novel clathrin-associated protein identified through subcellular proteomics. The Journal of Cell Biology, 158, (5), p. 855-862.

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URL officielle: http://dx.doi.org/doi:10.1083/jcb.200205078

Résumé

Despite numerous advances in the identification of the molecular machinery for clathrin-mediated budding at the plasma membrane, the mechanistic details of this process remain incomplete. Moreover, relatively little is known regarding the regulation of clathrin-mediated budding at other membrane systems. To address these issues, we have utilized the powerful new approach of subcellular proteomics to identify novel proteins present on highly enriched clathrin-coated vesicles (CCVs). Among the ten novel proteins identified is the rat homologue of a predicted gene product from human, mouse, and Drosophila genomics projects, which we named enthoprotin. Enthoprotin is highly enriched on CCVs isolated from rat brain and liver extracts. In cells, enthoprotin demonstrates a punctate staining pattern that is concentrated in a perinuclear compartment where it colocalizes with clathrin and the clathrin adaptor protein (AP)l. Enthoprotin interacts with the clathrin adaptors AP1 and with Golgi-localized, gamma-ear-containing, Arf-binding protein 2. Through its COOH-terminal domain, enthoprotin binds to the terminal domain of the clathrin heavy chain and stimulates clathrin assembly. These data suggest a role for enthoprotin in clathrin-mediated budding on internal membranes. Our study reveals the utility of proteomics in the identification of novel vesicle trafficking proteins.

Type de document:Article publié dans une revue avec comité d'évaluation
ISSN:0021-9525
Volume:158
Numéro:5
Pages:p. 855-862
Version évaluée par les pairs:Oui
Date:2002
Sujets:Sciences de la santé > Sciences médicales > Biologie cellulaire
Département, module, service et unité de recherche:Départements et modules > Département des sciences fondamentales
Mots-clés:clathrin adaptors, endosome, ENTH domain, GGAs, TGN, adaptor proteins, vesicular transport, carrier proteins, membrane, proteomics
Déposé le:06 juin 2016 13:41
Dernière modification:05 déc. 2016 20:46
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Creative Commons LicenseSauf indication contraire, les documents archivés dans Constellation sont rendus disponibles selon les termes de la licence Creative Commons "Paternité, pas d'utilisation commerciale, pas de modification" 2.5 Canada.

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