N-Terminal polyubiquitination of the ARF tumor suppressor, a natural lysine-less protein.
Cell Cycle
; 3(11): 1367-9, 2004 Nov.
Article
de En
| MEDLINE
| ID: mdl-15467472
ABSTRACT
Ubiquitin-dependent proteolysis by proteasomes generally depends upon the conjugation of polyubiquitin chains to lysine epsilon-NH(2) groups within the targeted proteins. However, engineered lysine-less mutants of certain viral and cellular proteins can undergo polyubiquitination at their N-termini. Is N-terminal polyubiquitination a physiologic process, and how many cellular proteins can be targeted for proteasomal degradation through this mechanism? Recent work indicates that the turnover of the endogenous lysine-less human ARF tumor suppressor protein and its mouse Arf counterpart (containing a single, non-conserved lysine residue) is regulated in this manner.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Maturation post-traductionnelle des protéines
/
Inhibiteur p16 de kinase cycline-dépendante
/
Polyubiquitine
Langue:
En
Journal:
Cell Cycle
Année:
2004
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique