High impact information on WWP2

• Our results indicate that AIP2 negatively regulates ABA signaling by targeting ABI3 for post-translational destruction [1].
• The AIP2 E3 ligase acts as a novel negative regulator of ABA signaling by promoting ABI3 degradation [1].
• Here, we show that PPXY-dependent viral budding is unusually sensitive to inhibitory fragments derived from specific HECT ubiquitin ligases, namely WWP1 and WWP2 [2].
• 5. Interestingly, coexpression of WWP2 competed with the effect of Nedd4-2 [3].
• We established a histobiochemical approach targeting micron-order inclusion bodies possessing extensive aggregation properties in situ by using a nonchemical denaturant (oligomeric actin interacting protein 2/d-lactate dehydrogenase protein 2 [Aip2p/Dld2p]) with the combinatorial method of laser-microdissection and immunoblot analysis [4].

Biological context of WWP2

• The deduced amino acid sequence of the cDNA clone showed homology to a recently reported human cDNA, called WWP2, that encodes an N-terminal C2-like domain [5].

Associations of WWP2 with chemical compounds

• Following negative results with chemical denaturants or detergent, including 6 M guanidine hydrochloride, 8 M urea, and 2% SDS, the laser-microdissected pick bodies were pretreated with oligomeric Aip2p/Dld2p, which possesses robust protein unfolding activity under biological conditions [4].

Other interactions of WWP2

• This screen yielded three ubiquitin-protein ligases, WWP1, WWP2, and AIP4, all of which belong to the HECT family and contain multiple WW domains [6].

References