RhoB has been shown to be an endosomal GTPase both by immunocytochemis
try and electron microscopy, however, its role in endocytosis is unkno
wn. Elucidation of the cellular roles of other members of this superfa
mily of signaling proteins has come with the identification of their d
ownstream partners. We show here that the recently isolated serine/thr
eonine kinase PRK1 is targeted to the endosomal compartment by RhoB. T
his is established both through immunofluorescence and cell fractionat
ion. PRK1 is shown to interact with activated RhoB in cells and is loc
alized to endosomes through its Rho-binding HR1 domain. Translocation
of PRK1 to the endosomal compartment by RhoB is accompanied by a shift
in the electrophoretic mobility of the kinase indicative of an accomp
anying activation.