IndraLab

Statements


| 5

reach
"The control of Imd homeostasis by USP2 is associated with the hydrolysis of Imd linked K48-ubiquitin chains and the synergistic binding of USP2 and Imd to the proteasome, as evidenced by both mass-spectrometry analysis of USP2 partners and by co-immunoprecipitation experiments."

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"Focusing on USP2 biochemical function, we show that USP2 binds to Imd and promotes the cleavage of Ub K48 chains from the protein in both cultured cells and flies."

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"USP2 interacts with Imd and promotes cleavage of Imd linked Ub K48."

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"By using GST pull-down assays with GST tagged full length or truncated forms of USP2 (USP2-N-ter [AA :1-531] and USP2-C-ter [AA :475-856]), we finally showed that USP2 preferentially interacts with Imd through its non catalytic N-ter domain."

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"Thus, the Imd and USP2 complex apparently binds more efficiently to the proteasome than do Imd or USP2 alone."