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Titolo:
Down-regulation of cell surface receptors is modulated by polar residues within the transmembrane domain
Autore:
Zaliauskiene, L; Kang, SH; Brouillette, CG; Lebowitz, J; Arani, RB; Collawn, JF;
Indirizzi:
Univ Alabama, Dept Cell Biol, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Cell Biol, Birmingham, AL 35294 USA Univ Alabama, Dept Biochem & Mol Genet, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Mol Genet, Birmingham, AL 35294 USA Univ Alabama, Dept Microbiol, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Microbiol, Birmingham, AL 35294 USA Univ Alabama, Biostat Unit, Ctr Comprehens Canc, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 ehens Canc, Birmingham, AL 35294 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 8, volume: 11, anno: 2000,
pagine: 2643 - 2655
SICI:
1059-1524(200008)11:8<2643:DOCSRI>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN TRANSFERRIN RECEPTOR; EPIDERMAL GROWTH-FACTOR; INTERMOLECULAR DISULFIDE BONDS; MANNOSE 6-PHOSPHATE RECEPTOR; LIVER GLYCOPROTEIN RECEPTOR; INVARIANT CHAIN CONTAINS; FACTOR-II RECEPTOR; DI-LEUCINE MOTIF; CYTOPLASMIC TAIL; MEDIATED ENDOCYTOSIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Collawn, JF Univ Alabama, Dept Cell Biol, Birmingham, AL 35294 USA Univ Alabama Birmingham AL USA 35294 Birmingham, AL 35294 USA
Citazione:
L. Zaliauskiene et al., "Down-regulation of cell surface receptors is modulated by polar residues within the transmembrane domain", MOL BIOL CE, 11(8), 2000, pp. 2643-2655

Abstract

How recycling receptors are segregated from down-regulated receptors in the endosome is unknown. In previous studies, we demonstrated that substitutions in the transferrin receptor (TR) transmembrane domain (TM) convert the protein from an efficiently recycling receptor to one that is rapidly down regulated. In this study, we demonstrate that the "signal" within the TM necessary and sufficient for down-regulation is Thr(11)Gln(17)Thr(19) (numbering in TM). Transplantation of these polar residues into the wild-type TR promotes receptor down-regulation that can be demonstrated by changes in protein half-life and in receptor recycling. Surprisingly, this modification dramatically increases the TR internalization rate as well. (similar to 79% increase). Sucrose gradient centrifugation and cross-linking studies revealthat propensity of the receptors to self-associate correlates with downregulation. Interestingly, a number of cell surface proteins that contain TM polar residues are known to be efficiently down-regulated, whereas recyclingreceptors for low-density lipoprotein and transferrin conspicuously lack these residues. Our data, therefore, suggest a simple model in which specific residues within the TM sequences dramatically influence the fate of membrane proteins after endocytosis, providing an alternative signal for down-regulation of receptor complexes to the well-characterized cytoplasmic tail targeting signals.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 05:04:08