Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
INTERACTION OF CTLA-4 WITH THE CLATHRIN-ASSOCIATED PROTEIN AP50 RESULTS IN LIGAND-INDEPENDENT ENDOCYTOSIS THAT LIMITS CELL-SURFACE EXPRESSION
Autore:
CHUANG E; ALEGRE ML; DUCKETT CS; NOEL PJ; VANDERHEIDEN MG; THOMPSON CB;
Indirizzi:
UNIV CHICAGO,GWEN KNAPP CTR LUPUS & IMMUNOL RES,COMM IMMUNOL,924 E 57TH ST,R413A CHICAGO IL 60637 UNIV CHICAGO,GWEN KNAPP CTR LUPUS & IMMUNOL RES,COMM IMMUNOL CHICAGO IL 60637 UNIV CHICAGO,HOWARD HUGHES MED INST,DEPT MED CHICAGO IL 60637 UNIV CHICAGO,HOWARD HUGHES MED INST,DEPT MOL GENET & CELL BIOL CHICAGO IL 60637
Titolo Testata:
The Journal of immunology
fascicolo: 1, volume: 159, anno: 1997,
pagine: 144 - 151
SICI:
0022-1767(1997)159:1<144:IOCWTC>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
LYSOSOMAL ACID-PHOSPHATASE; GROWTH-FACTOR RECEPTORS; CYTOPLASMIC TAIL; INVITRO BINDING; COATED PITS; T-CELLS; TYROSINE; PHOSPHORYLATION; ADAPTORS; SIGNALS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
E. Chuang et al., "INTERACTION OF CTLA-4 WITH THE CLATHRIN-ASSOCIATED PROTEIN AP50 RESULTS IN LIGAND-INDEPENDENT ENDOCYTOSIS THAT LIMITS CELL-SURFACE EXPRESSION", The Journal of immunology, 159(1), 1997, pp. 144-151

Abstract

CTLA-4 is a lymphocyte cell surface receptor expressed by activated Tcells that functions to down-regulate T cell responses induced by TCRand CD28 stimulation. Since CTLA-4 competes with CD28 for binding to the common ligands B7-1 and B7-2, the level of CTLA-4 surface expression is likely to play an important role in its ability to inhibit CD28-dependent T cell activation. The factors that regulate these levels are poorly understood. Recent studies have revealed that following T cell activation, the majority of CTLA-4 is localized intracellularly rather than on the cell surface, and surface CTLA-4 is rapidly reinternalized. In this study, we investigate the molecular mechanism underlying the rapid clearance of CTLA-4 from the cell surface. The data demonstrate that cell surface CTLA-4 is endocytosed into clathrin-coated vesicles even in the absence of ligand. The targeting of CTLA-4 to clathrin-coated vesicles is mediated by the clathrin-associated adaptor complex AP-2, The cytoplasmic domain of CTLA-4 was found to specifically bind to AP50, the medium chain subunit of AP-2 in both yeast two-hybrid and coimmunoprecipitation assays. The interaction requires the peptide sequence 199-CVYVKM-204 in the cytoplasmic tail of CTLA-4. Mutation ofthe CTLA-4 amino acid residue Y201 abrogates the interaction with AP50, resulting in the accumulation of CTLA-4 at the cell surface. Together these data suggest that the interaction of CTLA-4 with AP50 plays an important role in regulating the cell surface expression of CTLA-4.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 03:35:35