A membrane-proximal tyrosine-based signal mediates internalization of the HIV-1 envelope glycoprotein via interaction with the AP-2 clathrin adaptor.

Détails

ID Serval
serval:BIB_7373
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
A membrane-proximal tyrosine-based signal mediates internalization of the HIV-1 envelope glycoprotein via interaction with the AP-2 clathrin adaptor.
Périodique
Journal of Biological Chemistry
Auteur(s)
Boge M., Wyss S., Bonifacino J.S., Thali M.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
1998
Volume
273
Numéro
25
Pages
15773-15778
Langue
anglais
Résumé
The envelope glycoprotein (Env) of human immunodeficiency virus, type 1 (HIV-1) undergoes rapid internalization after its transport to the cell surface. Env internalization is dependent upon information contained within the cytosolic domain of the protein. Here, we report that the cytosolic domain of Env binds specifically to the medium chain, mu 2, of the clathrin-associated protein complex AP-2, as well as to the complete AP-2 complex. The Env cytosolic domain contains two highly conserved tyrosine-based motifs (Y712SPL and Y768HRL), both of which are capable of binding to mu 2 when presented as short peptides. However, only the membrane-proximal motif Y712SPL binds to mu 2 and is required for internalization in the context of the whole cytosolic domain of Env. A glycine residue (Gly711) adjacent to the Y712SPL motif is also important for binding to mu 2/AP-2 and internalization. These observations suggest that the accessibility of the membrane-proximal GY712SPL to mu 2/AP-2 determines its function as a signal for recruitment of HIV-1 Env into clathrin-coated pits and its ensuing internalization.
Mots-clé
Adaptor Proteins, Vesicular Transport, Clathrin/metabolism, Cytosol/metabolism, Enzyme Inhibitors/metabolism, Gene Products, env/metabolism, Glutathione Transferase/genetics, Glutathione Transferase/metabolism, HIV-1, Humans, Kinetics, Nerve Tissue Proteins/metabolism, Phospholipase D/antagonists & inhibitors, Phosphoproteins/metabolism, Protein Sorting Signals/metabolism, Recombinant Fusion Proteins/metabolism, Tyrosine/metabolism
Pubmed
Web of science
Création de la notice
19/11/2007 13:45
Dernière modification de la notice
03/03/2018 18:19
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