期刊
BIOLOGICAL CHEMISTRY
卷 381, 期 9-10, 页码 779-789出版社
WALTER DE GRUYTER & CO
DOI: 10.1515/BC.2000.101
关键词
E3; N-end rule; peptide import; proteasome; proteolysis; ubiquitin
Eukaryotes contain a highly conserved multienzyme system which covalently links a smalt protein, ubiquitin, to a variety of intracellular proteins that bear degradation signals recognized by this system. The resulting ubiquitin-protein conjugates are degraded by the 26S proteasome, an ATP-dependent protease. Pathways that involve ubiquitin play major roles in a huge variety of processes, including cell differentiation, cell cycle, and responses to stress. In this article we briefly review the design of the ubiquitin system, and describe two recent advances, the finding that ubiquitin ligases interact with specific components of the 26S proteasome, and the demonstration that peptides accelerate their uptake into cells by activating the N-end rule pathway, one of several proteolytic pathways of the ubiquitin system.
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