High impact information on USP20

• D2 interaction with VDU1 and VDU2, a closely related deubiquitinase, was confirmed in mammalian cells [1].
• VDU1, but not VDU2, is markedly increased in brown adipocytes by norepinephrine or cold exposure, further amplifying the increase in D2 activity that results from catecholamine-stimulated de novo synthesis [1].
• These findings suggest that ubiquitination of HIF-1alpha is a dynamic process and that ubiquitinated HIF-1alpha might be rescued from degradation by VDU2 through deubiquitination [2].
• Finally, we demonstrate that VDU2 can also be ubiquitinated and degraded in a pVHL-dependent manner [3].
• VDU2 contains the signature motifs of the ubiquitin-specific processing protease family and possesses deubiquitinating activity [3].

Other interactions of USP20

• Based on human and mouse cDNA sequences, VDU1 and VDU2 are identical in approximately 59% of the amino acids with strong homology in the N-terminus and C-terminus and a weaker similarity in the middle region [3].
• Since deubiquitination, by reversing ubiquitination, has been recognized as an important regulatory step in ubiquitination-related processes, VDU1 and VDU2 could be important substrates of pVHL E3 ligase complex [3].

References