PARK2

(redirected from E3 Ubiquitin Ligase)

PARK2

A gene on chromosome 6q25.2-q27 that encodes a protein that functions within a multiprotein E3 ubiquitin ligase complex, catalysing the covalent attachment of ubiquitin moieties onto substrate proteins—e.g., BCL2, SYT11, CCNE1, GPR37, STUB1, SEPT5, ZNF746 and AIMP2. It also participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating polyubiquitination of misfolded proteins. PARK2 may play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis; it may have tumour suppressor activity.
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PROTACs recruit an E3 ubiquitin ligase to a specific targeted protein, labeling that protein for elimination by the ubiquitin/proteasome system.
The fruit flies' reduced distaste for camphor occurred through a mechanism that involves the degradation of the TRPL protein by an enzyme called E3 ubiquitin ligase, or Ube3a, which targets specific protein substrates for degradation.
E3 ubiquitin ligase is an enzyme that catalyzes covalent binding of multiple ubiquitin proteins to its substrates and enhances degradation of the substrate proteins in the proteasome.
The E3 ubiquitin ligase activity of transcription factor AHR permits non-genomic regulation of biological pathways
PROTACs recruit an E3 ubiquitin ligase to a specific targeted protein labeling that protein for elimination by the Ubiquitin/Proteasome System.
In a paper (Essential Role of the E3 Ubiquitin Ligase Cbl-b in T Cell Anergy Induction, Immunity, August 2004) to be published Wednesday in the scientific journal Immunity, researchers from the La Jolla Institute for Allergy and Immunology (LIAI) in San Diego, Calif.
The paper, entitled "Hijacking the E3 Ubiquitin Ligase Cereblon to Efficiently Target BRD4" by Lu et al.
today announced that findings from its study identifying the role of a E3 ubiquitin ligase known as UHRF1 in the regulation of cellular proliferation and cellular repair was published in Molecular Biology of the Cell, the journal of the American Society for Cell Biology.
The second article details a high throughput screening process that Rigel has developed to screen the anaphase-promoting complex (APC), an E3 ubiquitin ligase under scrutiny as an anti-cancer target.
These fundamental patents cover methods for identifying and/or measuring E3 ubiquitin ligase activity and screening for agents that modulate their activity, including small molecule or biological modulators.
The data demonstrate that treatment of cancer cells with inhibitors of the p27 E3 ubiquitin ligase dramatically elevate the level of the p27 tumor suppressor protein, leading to cell cycle arrest and subsequent tumor cell death.
The remarkable pleiotropy of CSN is partially explained through its enzymatic activity towards Cullin-RING E3 ubiquitin ligases (CRLs), which are activated by neddylation and inactivated by CSN-mediated deneddylation.