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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Background: The E3 ubiquitin ligase neural precursor cell expressed developmentally downregulated 4-1 (NEDD4-1) negatively regulates phosphatase and tensin homolog deleted on chromosome 10 (PTEN) protein levels through polyubiquitination and proteolysis, but its significance in lung cancer is still unclear.
Ube3a, the E3 ubiquitin ligase causing Angelman syndrome and linked to autism, regulates protein homeostasis through the proteasomal shuttle Rpn10.
These results suggest that Hbo1 is a novel E3 ubiquitin ligase that activates ER[alpha]-dependent transcription.
This small molecule was found to impart its activity in a highly specific manner by reprogramming the E3 ubiquitin ligase complex to degrade a protein required for the survival of certain cancers.
The F-box and leucine rich repeat protein 2 (FBL2) is another component of the SCF (Skp1-Cullin1-F-box protein) E3 ubiquitin ligase complex that has been found to be decreased in the brains of AD patients [20].
Further studies identified ten more MARCH family members for a total of eleven mammalian proteins, all possessing RING-CH domains with E3 ubiquitin ligase activity [31-33].
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.
Specifically, activation of molecules within the canonical Akt/mTOR pathway appears to suppress gene expression of key muscle degradatory genes, namely the muscle atrophy F-box protein (MAFbx/atrogin-1), an E3 ubiquitin ligase that plays a critical role in regulating protein ubiquination and breakdown in skeletal muscle (4,11,30).
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 APC/C is a multi-subunit cullin-RING E3 ubiquitin ligase that controls progression through the cell cycle by a temporal regulation of its activity and substrate specificity.
The most well characterized neddylation substrates are the cullin family members, of which neddylation causes activation of the cullinRING E3 ubiquitin ligase complex and promotes cullin-based ubiquitination.