LiveZilla Live Chat Software

Constellation, le dépôt institutionnel de l'Université du Québec à Chicoutimi

HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin : identification of a novel interaction with clathrin light chain

Legendre-Guillemin Valérie, Metzler Martina, Charbonneau Martine, Gan Lu, Chopra Vikramjit, Philie Jacynthe, Hayden Michael R. et McPherson Peter S.. (2002). HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin : identification of a novel interaction with clathrin light chain. The Journal of Biological Chemistry, 277, (22), p. 19897-19904.

[img]
Prévisualisation
PDF - Version publiée
407kB

URL officielle: http://dx.doi.org/doi:10.1074/jbc.M112310200

Résumé

Huntingtin-interacting protein 1 (HIP1) and HIP12 are orthologues of Sla2p, a yeast protein with essential functions in endocytosis and regulation of the actin cytoskeleton. We now report that HIP1 and HIP12 are major components of the clathrin coat that interact but differ in their ability to bind clathrin and the clathrin adaptor AP2. HIP1 contains a clathrin-box and AP2 consensus-binding sites that display high affinity binding to the terminal domain of the clathrin heavy chain and the ear domain of the AP2 alpha subunit, respectively. These consensus sites are poorly conserved in HIP12 and correspondingly, HIP12 does not bind to AP2 nor does it demonstrate high affinity clathrin binding. Moreover, HIP12 co-sediments with F-actin in contrast to HIP1, which exhibits no interaction with actin in vitro. Despite these differences, both proteins efficiently stimulate clathrin assembly through their central helical domain. Interestingly, in both HIP1 and HIP12, this domain binds directly to the clathrin light chain. Our data suggest that HIP1 and HIP12 play related yet distinct functional roles in clathrin-mediated endocytosis.

Type de document:Article publié dans une revue avec comité d'évaluation
ISSN:0021-9258
Volume:277
Numéro:22
Pages:p. 19897-19904
Version évaluée par les pairs:Oui
Date:2002
Sujets:Sciences de la santé > Sciences médicales > Biochimie
Sciences de la santé > Sciences médicales > Biologie cellulaire
Sciences de la santé > Sciences médicales > Biologie moléculaire
Département, module, service et unité de recherche:Départements et modules > Département des sciences fondamentales
Mots-clés:HIP1, HIP12, clathrin, endocytosis, Huntington disease, proteins
Informations complémentaires:This research was originally published in The Journal of Biological Chemistry. Legendre-Guillemin V, Metzler M, Charbonneau M, Gan L, Chopra V, Philie J, Hayden MR et McPherson PS. HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin - Identification of a novel interaction with clathrin light chain. Journal of Biological Chemistry. 2002; 277 : 19897-19904. © the American Society for Biochemistry and Molecular Biology.
Déposé le:01 juin 2016 17:43
Dernière modification:05 déc. 2016 20:47
Afficher les statistiques de telechargements

Éditer le document (administrateurs uniquement)

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.

Bibliothèque Paul-Émile-Boulet, UQAC
555, boulevard de l'Université
Chicoutimi (Québec)  CANADA G7H 2B1
418 545-5011, poste 5630