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Titolo:
The carboxyl terminus of the cystic fibrosis transmembrane conductance regulator binds to AP-2 clathrin adaptors
Autore:
Weixel, KM; Bradbury, NA;
Indirizzi:
Univ Pittsburgh, Sch Med, Dept Cell Biol & Physiol, Cyst Fibrosis Res Ctr,Pittsburgh, PA 15261 USA Univ Pittsburgh Pittsburgh PA USA 15261 Res Ctr,Pittsburgh, PA 15261 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 5, volume: 275, anno: 2000,
pagine: 3655 - 3660
SICI:
0021-9258(20000204)275:5<3655:TCTOTC>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSFERRIN RECEPTOR INTERNALIZATION; DI-LEUCINE MOTIF; CHLORIDE CHANNELS; AMINO-ACID; ENDOCYTOSIS; CFTR; TYROSINE; PROTEIN; SIGNAL; SEQUENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Bradbury, NA Univ Pittsburgh, Sch Med, Dept Cell Biol & Physiol, Cyst Fibrosis Res Ctr,3500 Terrace St, Pittsburgh, PA 15261 USA Univ Pittsburgh 3500Terrace St Pittsburgh PA USA 15261 1 USA
Citazione:
K.M. Weixel e N.A. Bradbury, "The carboxyl terminus of the cystic fibrosis transmembrane conductance regulator binds to AP-2 clathrin adaptors", J BIOL CHEM, 275(5), 2000, pp. 3655-3660

Abstract

The cystic fibrosis transmembrane conductance regulator (CFTR) undergoes rapid and efficient endocytosis. Since functionally active CFTR is found in purified clathrin-coated vesicles isolated from both cultured epithelial cells and intact epithelial tissues, we investigated the molecular mechanismswhereby CFTR could enter such endocytic clathrin-coated vesicles. In vivo cross-linking and in vitro pull-down assays show that full-length CFTR binds to the endocytic adaptor complex AP-2. Fusion proteins containing the carboxyl terminus of CFTR (amino acids 1404-1480) were also able to bind AP-2 but did not bind the Golgi-specific adaptor complex AP-1, Substitution of an alanine residue for tyrosine at position 1424 significantly reduced the ability of AP-2 to bind the carboxyl terminus of CFTR; however, mutation to a phenylalanine residue (an amino acid found at position 1424 in dogfish CFTR) did not perturb AP-2 binding. Secondary structure predictions suggest that Tyr(1424) is present in a beta-turn conformation, a conformation disrupted by alanine but not phenylalanine. Together, these data suggest that thecarboxyl terminus of CFTR contains a tyrosine-based internalization signalthat interacts with the endocytic adaptor complex AP-2 to facilitate efficient entry of CFTR into clathrin-coated vesicles.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 13:34:33