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Titolo:
Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/Rsp5p family of ubiquitin-protein ligases
Autore:
Rotin, D; Staub, O; Haguenauer-Tsapis, R;
Indirizzi:
Univ Toronto, Hosp Sick Children, Toronto, ON M5G 1X8, Canada Univ Toronto Toronto ON Canada M5G 1X8 ldren, Toronto, ON M5G 1X8, Canada Univ Toronto, Dept Biochem, Toronto, ON M5G 1X8, Canada Univ Toronto Toronto ON Canada M5G 1X8 ochem, Toronto, ON M5G 1X8, Canada Univ Lausanne, Inst Pharmacol & Toxicol, CH-1015 Lausanne, Switzerland Univ Lausanne Lausanne Switzerland CH-1015 CH-1015 Lausanne, Switzerland Univ Paris 06, CNRS, Inst Jacques Monod, F-75251 Paris 05, France Univ Paris 06 Paris France 05 st Jacques Monod, F-75251 Paris 05, France Univ Paris 07, CNRS, Inst Jacques Monod, F-75251 Paris 05, France Univ Paris 07 Paris France 05 st Jacques Monod, F-75251 Paris 05, France
Titolo Testata:
JOURNAL OF MEMBRANE BIOLOGY
fascicolo: 1, volume: 176, anno: 2000,
pagine: 1 - 17
SICI:
0022-2631(20000701)176:1<1:UAEOPM>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPITHELIAL SODIUM-CHANNEL; YEAST URACIL PERMEASE; GROWTH-HORMONE RECEPTOR; LIGAND-INDUCED INTERNALIZATION; YES-ASSOCIATED PROTEIN; CELL ANTIGEN RECEPTOR; AMINO-ACID PERMEASE; ALPHA-FACTOR RECEPTOR; A-FACTOR TRANSPORTER; FACTOR BETA-RECEPTOR;
Keywords:
ubiquitin; endocytosis; ubiquitin protein ligase; Nedd4/Rsp5p; plasma membrane proteins;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
192
Recensione:
Indirizzi per estratti:
Indirizzo: Haguenauer-Tsapis, R Univ Toronto, Hosp Sick Children, 555 Univ Ave, Toronto, ON M5G 1X8, Canada Univ Toronto 555 Univ Ave Toronto ON Canada M5G 1X8 a
Citazione:
D. Rotin et al., "Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/Rsp5p family of ubiquitin-protein ligases", J MEMBR BIO, 176(1), 2000, pp. 1-17

Abstract

In addition to its well-known role in recognition by the proteasome, ubiquitin-conjugation is also involved in downregulation of membrane receptors, transporters and channels. In most cases, ubiquitination of these plasma membrane proteins leads to their internalization followed by targeting to thelysosome/vacuole for degradation. A crucial role in ubiquitination of manyplasma membrane proteins appears to be played by ubiquitin-protein ligasesof the Nedd4/Rsp5p family. All family members carry an N-terminaI Ca2+-dependent lipid/protein binding (C2) domain, two to four WW domains and a C-terminal catalytic Hect-domain. Nedd4 is involved in downregulation of the epithelial Na+ channel, by binding of its WW domains to specific PY motifs ofthe channel. Rsp5p, the unique family member in S. cerevisiae, is involvedin ubiquitin-dependent endocytosis of a great number of yeast plasma membrane proteins. These proteins lack apparent PY motifs, but carry acidic sequences, and/or phosphorylated-based sequences that might be important, directly or indirectly, for their recognition by Rsp5p. In contrast to polyubiquitination leading to proteasomal recognition, a number of Rsp5p targets carry few ubiquitins per protein, and moreover with a different ubiquitin linkage. Accumulating evidence suggests that, at least in yeast, ubiquitin itself may constitute an internalization signal, recognized by a hypothetical receptor, Recent data also suggest that Nedd4/Rsp5p might play a role in theendocytic process possibly involving its C2 domain, in addition to its role in ubiquitinating endocytosed proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 15:30:41