Protein degradation or regulation: Ub the judge

Article Abstract:

Posttranslational modifications are covalent alterations that lead to a variety of changes in the target protein. These alterations change the size, conformation and charge of the protein and can also affect its interaction with other proteins, enzymatic action and subcellular localization. Ubiquitination is unusual among such alterations because the ubiquitin molecule, which is in itself a protein, acts as the steric modifier. Ubiquitination aids the degradation of target proteins and is also believed to have a role in regulating vacuolar targeting and endocytosis.

Research, Protein binding, Proteolysis, Genetic translation, Translation (Genetics), Endocytosis

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Substrate targeting in the ubiquitin system

Article Abstract:

The ubiquitin system is responsible for degrading damaged, misfolded or misasembled proteins. It also targets short-lived proteins such as transcription factors, cell growth modulators, signal transducers and cell cycle proteins. After the ubiquitin system established the target substrates, their destruction is performed by the large, complex protease, 26S proteasome. Ubiquitin's targeting has been found to be influenced by specific degradation signals that are part of the structural features of the substrate.

Analysis, Proteases, Cell research, Cytological research

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SP-RING for SUMO: new functions bloom for a ubiquitin-like protein

Article Abstract:

Activity of the ubiquitin-like protein SUMO is influenced by E3-like factors, which enhance SUMO protein transfer to specific proteins. The E3-like factor proteins are comprised of proteins involved in chromosome condensation, signal transduction, and biogenesis of ion channel proteins.

United States, Cellular signal transduction, Ion channels, Chromosome banding, Post-translational modification

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