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Titolo:
E3-13.7 integral membrane proteins encoded by human adenoviruses alter epidermal growth factor receptor trafficking by interacting directly with receptors in early endosomes
Autore:
Crooks, D; Kil, SJ; McCaffery, JM; Carlin, C;
Indirizzi:
Case Western Reserve Univ, Sch Med, Dept Physiol & Biophys, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA Case Western Reserve Univ, Sch Med, Mol Virol Training Program, Cleveland,OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 , Cleveland,OH 44106 USA Case Western Reserve Univ, Sch Med, Ctr Canc, Cleveland, OH 44106 USA CaseWestern Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA Rainbow Babies & Childrens Hosp, Rainbow Ctr Childhood Polycyst Kidney Dis, Cleveland, OH 44106 USA Rainbow Babies & Childrens Hosp Cleveland OH USA44106 land, OH 44106 USA Johns Hopkins Univ, Dept Biol, Integrated Imaging Ctr, Baltimore, MD 21218USA Johns Hopkins Univ Baltimore MD USA 21218 ing Ctr, Baltimore, MD 21218USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 10, volume: 11, anno: 2000,
pagine: 3559 - 3572
SICI:
1059-1524(200010)11:10<3559:EIMPEB>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
FACTOR EGF RECEPTOR; PLASMA-MEMBRANE; TRANSFERRIN RECEPTORS; LYSOSOMAL MEMBRANE; ENDOCYTIC PATHWAY; MULTIVESICULAR ENDOSOMES; PRELYSOSOMAL COMPARTMENT; INTRACELLULAR-TRANSPORT; ENHANCED DEGRADATION; TYROSINE KINASES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Carlin, C Case Western Reserve Univ, Sch Med, Dept Physiol & Biophys, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 , OH 44106 USA
Citazione:
D. Crooks et al., "E3-13.7 integral membrane proteins encoded by human adenoviruses alter epidermal growth factor receptor trafficking by interacting directly with receptors in early endosomes", MOL BIOL CE, 11(10), 2000, pp. 3559-3572

Abstract

Animal cell viruses provide valuable model systems for studying many normal cellular processes, including membrane protein sorting. The focus of thisstudy is an integral membrane protein encoded by the E3 transcription region of human adenoviruses called E3-13.7, which diverts recycling EGF receptors to lysosomes without increasing the rate of receptor internalization orintrinsic receptor tyrosine kinase activity. Although E3-13.7 can be foundon the plasma membrane when it is overexpressed, its effect on EGF receptor trafficking suggests that the plasma membrane is not its primary site of action. Using cell fractionation and immunocytochemical experimental approaches, we now report that the viral protein is located predominantly in early endosomes and limiting membranes of endosome-to-lysosome transport intermediates called multivesicular endosomes. We also demonstrate that E3-13.7 physically associates with EGF receptors undergoing E3-13.7-mediated down-regulation in early endosomes. Receptor-viral protein complexes then dissociate, and EGF receptors proceed to lysosomes, where they are degraded, while E3-13.7 is retained in endosomes. We conclude that E3-13.7 is a resident early endocytic protein independent of EGF receptor expression, because it has identical intracellular localization in mouse cells lacking endogenous receptors and cells expressing a human cytomegalovirus-driven receptor cDNA. Finally, we demonstrate that EGF receptor residues 675-697 are required forE3-13.7-mediated down-regulation. Interestingly, this sequence includes a known EGF receptor leucine-based lysosomal sorting signal used during ligand-induced trafficking, which is also conserved in the viral protein. E3-13.7, therefore, provides a novel model system for determining the molecular basis of selective membrane protein transport in the endocytic pathway. Our studies also suggest new paradigms for understanding EGF receptor sorting in endosomes and adenovirus pathogenesis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 22:23:07