http://www.cnr.it/ontology/cnr/individuo/prodotto/ID12299
E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation. (Articolo in rivista)
- Type
- Label
- E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation. (Articolo in rivista) (literal)
- Anno
- 2005-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1111/j.1600-0854.2005.00294.x (literal)
- Alternative label
d'Azzo A1; Bongiovanni A2; Nastasi T1 (2005)
E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation.
in Traffic (Copenhagen. Print); Wiley-Blackwell Publishing, Inc., Malden (Stati Uniti d'America)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- d'Azzo A1; Bongiovanni A2; Nastasi T1 (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://onlinelibrary.wiley.com/doi/10.1111/j.1600-0854.2005.00294.x/abstract;jsessionid=A511C1E7DCECDF0C6067D6B11ED23765.d03t03 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1Department of Genetics and Tumor Cell Biology, St. Jude
Children's Research Hospital, Memphis, TN, USA
2Istituto di Biomedicina e Immunologia Molecolare, IBIM
Consiglio Nazionale delle Ricerche, Palermo, Italy (literal)
- Titolo
- E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation. (literal)
- Abstract
- Ubiquitination is a regulated post-translational modification that conjugates ubiquitin (Ub) to lysine residues of target proteins and determines their intracellular fate. The canonical role of ubiquitination is to mediate degradation by the proteasome of short-lived cytoplasmic proteins that carry a single, polymeric chain of Ub on a
specific lysine residue. However, protein modification by Ub has much broader and diverse functions involved
in a myriad of cellular processes. Monoubiquitination, at one or multiple lysine residues of transmembrane proteins,
influences their stability, protein-protein recognition, activity and intracellular localization. In these processes, Ub functions as an internalization signal that sends the modified substrate to the endocytic/sorting compartments, followed by recycling to the plasma membrane or degradation in the lysosome. E3 ligases
play a pivotal role in ubiquitination, because they recognize the acceptor protein and hence dictate the high
specificity of the reaction. The multitude of E3s present in nature suggests their nonredundant mode of action
and the need for their controlled regulation. Here we give a short account of E3 ligases that specifically modify and regulate membrane proteins. We emphasize the intricate network of interacting proteins that contribute to the substrate-E3 recognition and determine the substrate's cellular fate. (literal)
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