Family Members USPL1, CYLD, USP1, USP2, USP3, USP4, USP5, USP6, USP7, USP YSP8, USP9x, USP10, USP11, USP12, USP13, USP14
, USP15, USP16, USP17L2, USP18, USP19, USP20, USP21, USP22, USP23, USP24, USP25, USP26, USP27, USP28, USP29, USP30, USP31, USP32, USP33, USP34, USP35, USP36, USP37, USP38, USP39, USP40, USP41, USP42, USP43, USP44, USP45, USP46, USP47, USP48, USP49, USP50, USP51, USP52, USP53, USP54 OTUB1, OTUB2, OTUD1, OTUD3, OTUD4, OTUD5, OTUD6A, OTU OTUD6B, OTU1, HIN1L, A20, Cezanne, Cezanne2, TRABID, VCPIP1 UCH UCH-L1, UCH-L3, UCH37/UCH-L5, BAP1 Josephin ATXN3, ATXN3L, JOSD1, JOSD2 JAMM/MPN+ BRCC36, CSNS, POH1, AMSH, AMSH-LP, MPND, MYSM1, PRPF8 Table 2: Deubiquitinases and bone remodeling.
To better understand just what causes this malfunction, a research team led by Harvard Medical School researchers Daniel Finley, professor of cell biology, and Randall King, associate professor of cell biology, zeroed in on an enzyme called Usp14.
They found that, when activated, Usp14 disassembles the ubiquitin chain, slowing down the proteasome's ability to rid the cell of bad proteins.
The researchers wanted to see if they could find a molecule that inhibited Usp14, thus allowing the proteosome to work effectively.
Lee screened 63,000 compounds, looking for molecules that inhibited only Usp14 and could easily infiltrate the cell.
Experimenting in both human and mouse cell cultures, Min Jae Lee, also a postdoctoral researcher, and his co-workers found that IU1 inhibited Usp14 and allowed the proteasome to dispose of proteins more quickly.