Rho family GTPases are implicated in a variety of biological activities, including endocytic vesicle trafficking. Rnd2 is a new member of Rho family GTPases, but its biological functions are not known. In the present study, we have performed a yeast two-hybrid screening using Rnd2 as bait and revealed that Rnd2 binds specifically to Vps4-A (where Vsp4-A is vacuolar protein sorting 4-A), a member of the AAA ATPase family and a central regulator for early endosome trafficking. This interaction was determined by the yeast two-hybrid system, in vitro binding and co-immunoprecipitation studies. Vps4-A associated with both guanosine 5′-[β-thio]triphosphate-bound active and guanosine 5′-[β-thio]diphosphate-bound inactive forms of Rnd2. An ATPase-defective Vps4-A mutant, Vps4-AE228Q, expressed in HeLa cells was accumulated in the early endosomes. When Rnd2 was co-expressed with Vps4-AE228Q, Rnd2 was recruited to the Vps4-A-bound early endosomes. These results suggest that Rnd2 is involved in the regulation of endosomal trafficking via direct binding to Vps4-A.
Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTPase, Rnd2
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Hiroko TANAKA, Hirotada FUJITA, Hironori KATOH, Kazutoshi MORI, Manabu NEGISHI; Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTPase, Rnd2. Biochem J 15 July 2002; 365 (2): 349–353. doi: https://doi.org/10.1042/bj20020062
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