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USP32 activates RAB7A. 4 / 4
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"Taken together, our data indicated that Rab7 function can be modulated by USP32-sensitive ubiquitination and that USP32 deficiency resulted in altered retromer-mediated trafficking and autophagy induc[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Indeed, USP32 depletion sequesters Rab7 in abnormally enlarged endosomal structures, and the accumulation of ubiquitinylated Rab7 promotes interactions with the retromer and inhibits interactions with RILP [29]."

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"Using proteome-wide ubiquitin remnant profiling, we reveal Rab7 to be a key substrate of USP32 and go on to show that USP32 supports Rab7 functions in transport and recycling from the MVB by two different mechanisms."

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"Secondly, USP32 supports the role of Rab7 in the transport and circulation of MVB through two different mechanisms [35]."