Disease relevance of USP2

• USP2, a cysteine protease and a member of the ubiquitin specific protease family, is overexpressed in prostate cancer and stabilizes fatty acid synthase, which has been associated with the malignancy of some aggressive prostate cancers [1].

High impact information on USP2

• When cell extracts were used, the EcR-B1-USP-2 heterodimer showed no binding to EcRE1, and the presence of excess USP-2 prevented the binding of EcR-B1-USP-1 to this element [2].
• We found that overexpression of Ubp41 is sufficient to elicit all features of apoptosis in human cells [3].
• Overexpression of Ubp41 resulted in a strong deubiquitination of a broad range of proteins, but surprisingly did not lead to a stabilization of protein substrates known to be regulated by the ubiquitin-proteasome system such as the cell cycle factors p21 and p27 [3].
• VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha [4].
• To develop an enzymatic assay for the search of UCH-L3 and USP2 inhibitors, C-terminally labeled ubiquitin substrates were enzymatically synthesized [5].

Biological context of USP2

• Here, we report the structure of the human USP2 catalytic domain in complex with ubiquitin [1].
• The deduced amino acid sequence of C. suppressalis USP (CsUSP) was very similar to those of other lepidopteran USPs, especially to the Manduca sexta USP-2 isoform [6].
• The in vitro release kinetics of diltiazem hydrochloride sustained-release tablets were evaluated using the USP 2 (paddle) and USP 4 (flow-through) apparatus [7].

Anatomical context of USP2

• METHODS: Transected bovine tendons (male Japanese black cattle, 24 months old) of the medial gastrocnemius (9-11x14-16mm in diameter) were sutured with the side-locking loop technique using a USP2-sized polyethylene and polyester multifilament suture or polyester multifilament suture [8].

Associations of USP2 with chemical compounds

• In contrast, in vitro-transcribed-translated USP-1 and USP-2 both formed heterodimeric complexes with EcR-B1 that bound ponasterone A with the same Kd (7 x 10(-10) M) and bound to both EcRE1 and heat shock protein 27 EcRE [2].

Other interactions of USP2

• Moreover, expression of USP-2 prevented activation by EcR-B1-USP-1 [2].

References