Ubiquitin Specific Peptidase 10 (USP10)

Ubiquitin, a highly conserved protein involved in the regulation of intracellular protein breakdown, cell cycle regulation, and stress response, is released from degraded proteins by disassembly of the polyubiquitin chains. Chemical cross-linking of cell lysates followed by immunoblotting revealed a high molecular mass band that was immunoprecipitated with either anti-G3P or anti-USP10 antibodies, suggesting that USP10 and G3BP are part of a large macromolecular complex. Incubation of osteosarcoma and HeLa cells with a proteasome inhibitor had no effect on G3BP protein levels, suggesting that G3BP is unlikely to be degraded by the ubiquitin-proteasome pathway. Addition of G3BP to a deubiquitinating assay resulted in inhibition of USP10 activity.