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Titolo:
EGF receptor residues Leu(679), Leu(680) mediate selective sorting of ligand-receptor complexes in early endosomal compartments
Autore:
Kil, SJ; 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, Ctr Canc, Cleveland, OH 44106 USA Case Western Reserve Univ Cleveland OH USA 44106 Cleveland, OH 44106 USA Rainbow Babies & Childrens Hosp, Rainbow Ctr Childhood PKD, Cleveland, OH 44106 USA Rainbow Babies & Childrens Hosp Cleveland OH USA 44106 land, OH 44106 USA
Titolo Testata:
JOURNAL OF CELLULAR PHYSIOLOGY
fascicolo: 1, volume: 185, anno: 2000,
pagine: 47 - 60
SICI:
0021-9541(200010)185:1<47:ERRLLM>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPIDERMAL GROWTH-FACTOR; FACTOR-ALPHA; TRANSFERRIN RECEPTORS; A431 CELLS; POSTENDOCYTIC TRAFFICKING; MULTIVESICULAR ENDOSOMES; PRELYSOSOMAL COMPARTMENT; ENHANCED DEGRADATION; ENDOCYTIC PATHWAY; MEMBRANE-PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
74
Recensione:
Indirizzi per estratti:
Indirizzo: Carlin, C Case Western Reserve Univ, Sch Med, Dept Physiol & Biophys, 10900 Euclid Ave, Cleveland, OH 44106 USA Case Western Reserve Univ 10900 Euclid Ave Cleveland OH USA 44106
Citazione:
S.J. Kil e C. Carlin, "EGF receptor residues Leu(679), Leu(680) mediate selective sorting of ligand-receptor complexes in early endosomal compartments", J CELL PHYS, 185(1), 2000, pp. 47-60

Abstract

Dileucine-based motifs have been shown to regulate endosomal sorting of a number of membrane proteins. Previously, we have shown that the dileucine motif Leu(679), Leu(680) in the juxtamembrane domain of the human epidermal growth factor receptor is involved in the endosome-to-lysosome transport ofligand-receptor reduction in ligand-induced receptor degradation without affecting internalization. In the current study, we have further characterized ligand-dependent intracellular sorting of EGF receptors containing a L679A, L680A. Immunocytochemical studies reveal that although mutant receptorsredistribute from the cell surface to transferrin receptor-positive endocytic vesicles similar to wild-type following ligand stimulation, their accumulation in Lamp-1-positive late endosomes/lysosomes is retarded compared towild-type. Kinetic analysis of I-125-EGF trafficking shows that reduced accumulation of internalized mutant receptors in Lamp-1-positive vesicles is due to rapid recycling of ligand-receptor complexes from early endocytic compartments. In addition, the fraction of intracellular I-125-EGF that is transported to late endocytic compartments in cells with mutant receptors is not as efficiently degraded as it is in cells with wild-type receptors. Furthermore, wild-type receptors in endocytic vesicles isolated by Percoll gradient fractionation are more resistant to in vitro digestion with proteinase K than mutant receptors. We propose that mutant receptors interact inefficiently with lysosomal sorting machinery, leading to their increased recycling. Our results are consistent with a model in which the Leu(679), Leu(680) signal facilitates sequestration of ligand-receptor complexes into internal Vesicles of multivesicular endosome-to-lysosome transport intermediates. (C) 2000 Wiley-Liss, Inc.

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Documento generato il 07/07/20 alle ore 15:43:02