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Ubiquitin

Autophagy/lysosome and ubiquitin/proteasome (UPS) are two systems found to cross-talk recently.UPS is dynamic through conjugating enzymes (E1, E2, E3) and deubiquitinating enzymes (DUB).Autophagy is many pathways related----PI3K/mTOR, ion channles, AMPK, cAMP and etc.  [show the full text]

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The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Protein ubiquitination controls many intracellular processes, including cell cycle progression, transcriptional activation, and signal transduction. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s.

Conversely, deubiquitinating enzymes (DUB) play an opposing role to the E3 ubiquitin ligases. DUBs are cysteine proteases that specifically cleave ubiquitin from ubiquitin-conjugated protein substrates. Cleaved ubiquitin molecules are recycled.

In short, ubiquitination is dynamic through above conjugating enzymes (E1, E2, E3) and deubiquitinating enzymes (DUB).

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.

Autophagy is defined as: The segregation and degradation of damaged or unwanted cytoplasmic constituents by autophagic vacuoles (cytolysosomes) composed of LYSOSOMES containing cellular components in the process of digestion; it plays an important role in BIOLOGICAL METAMORPHOSIS of amphibians, in the removal of bone by osteoclasts, and in the degradation of normal cell components in nutritional deficiency states.