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USP32 deubiquitinates RAB7A. 6 / 6
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"25 To confirm that Rab7 is deubiquitinated by USP32, Rab7 ubiquitination was monitored in the presence and absence of exogenous USP32."
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"11 Their data also showed that USP32 deubiquitinates Rab7, which impacts binding efficiency of the small GTPase to different effector proteins and thereby regulates Rab7 function."
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"13 Loss of USP32 increased ubiquitination of Rab7 at K191/194, which enhanced binding of Rab7 to its effector protein RILP and accelerated retrograde transport of CI-MPR."
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"Having established that USP32 can deubiquitylate Rab7 in vitro and in situ, we sought to understand the interplay between USP32 and Rab7 in endosome biology."
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"This suggested that deubiquitylation of Rab7 by USP32 promotes release of Rab7 from the membrane to the cytosol, where a new functional cycle of this Rab can commence (Fig. 5i)."
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"Taken together with the observations on endosomal transport (Fig. 6), these findings support a model wherein deubiquitylation of Rab7 by USP32 exerts multifaceted control over membrane dynamics at the LE/MVB by promoting their intracellular motility as well as enabling efficient recycling from these organelles (Fig. 9)."
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