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Titolo:
INTERACTION OF ENDOCYTIC SIGNALS FROM THE HIV-1 ENVELOPE GLYCOPROTEINCOMPLEX WITH MEMBERS OF THE ADAPTER MEDIUM-CHAIN FAMILY
Autore:
OHNO H; AGUILAR RC; FOURNIER MC; HENNECKE S; COSSON P; BONIFACINO JS;
Indirizzi:
NICHHD,CELL BIOL & METAB BRANCH,NIH BETHESDA MD 20892 NICHHD,CELL BIOL & METAB BRANCH,NIH BETHESDA MD 20892 BASEL INST IMMUNOL CH-4005 BASEL SWITZERLAND
Titolo Testata:
Virology
fascicolo: 2, volume: 238, anno: 1997,
pagine: 305 - 315
SICI:
0042-6822(1997)238:2<305:IOESFT>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; TRANS-GOLGI NETWORK; TRANSFERRIN RECEPTOR INTERNALIZATION; CLATHRIN-ASSOCIATED PROTEINS; VARICELLA-ZOSTER VIRUS; CYTOPLASMIC DOMAIN; AMINO-ACID; TRANSMEMBRANE PROTEIN; SORTING SIGNALS; CELL-SURFACE;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
H. Ohno et al., "INTERACTION OF ENDOCYTIC SIGNALS FROM THE HIV-1 ENVELOPE GLYCOPROTEINCOMPLEX WITH MEMBERS OF THE ADAPTER MEDIUM-CHAIN FAMILY", Virology, 238(2), 1997, pp. 305-315

Abstract

The envelope glycoprotein (Env) complex of HIV-I undergoes rapid internalization from the plasma membrane of human cells by virtue of a tyrosine-based endocytic signal (RQGYSPL, residues 704-710) in the cytosolic tail of the protein (J. F. Rowell et al., J. Immunol. 155, 473-488, 1995). Here we demonstrate that this tyrosine-based signal interactswith the mu 2 (medium) chain of the AP-2 clathrin-associated adaptor,a protein complex involved in endocytosis of cell surface receptors. he same signal is also capable of interacting with two other members of the adaptor medium chain family, mu 1 and mu 3A, which are components of the AP-I and AP-3 adaptor complexes, respectively. Interactions with mu 1 and mu 3A might be responsible for the targeting of the internalized envelope glycoprotein to lysosomes or to the basolateral plasma membrane of polarized epithelial cells. A second potential tyrosine-based signal (LFSYHRL, residues 760-766) also interacts with mu 1, mu 2, and mu 3A, although it is less important for internalization in vivo probably due to its position within the cytosolic tail. Overexpression of chimeric proteins having the HIV-1 Env cytosolic tail increases expression of the transferrin receptor on the cell surface, probably due to saturation of the cellular pool of mu 2 by the overexpressed proteins. These observations suggest that HIV-I Env utilizes the protein sorting machinery of the host cells for internalization and sorting atvarious steps of the endocytic and biosynthetic pathways. (C) 1997 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/04/20 alle ore 11:13:02