RING finger proteins: mediators of ubiquitin ligase activity

Article Abstract:

This review discusses the new function carried out by the RING finger proteins besides being involved in the dimerization of proteins. Research reveals that RING proteins function as ubiquitin protein ligases mediating ubiquitin transfer within and among heterologous substrates. Ubiquitination of the RING proteins was first reported in 1998.

Research, Analysis, Metabolic regulation, Structure-activity relationships (Pharmacology), Structure-activity relationship (Pharmacology)

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Pirh2, a p-53-induced ubiquitin-protein ligase, promotes p53 degradation

Article Abstract:

Results reveal that tumor suppressor p53 regulated Pirh2 gene, encoding a protein with ubiquitin-protein ligase activity, interacts with p53 and ubiquitinantes it. The expression of Pirh2 is connected with the p53 synthesis and degradation and it represses p53 function such as p53-dependent transactivation and growth.

Canada, Genetic aspects, Tumor suppressor genes, Proteolysis, Enzyme regulation, Tumour suppressor genes

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Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-1

Article Abstract:

Results demonstrate that ESCRT-1 is a 350 kilodalton complex, which recognizes ubiquitinated multivesicular body cargo and sorts them into multivesicular body vesicles. Data suggest that ESCRT-1 represents a component of the endosomal sorting machinery coupling ubiquitin modification to protein sorting.

Biological transport, Cell receptors

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