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Link to original content: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222680
Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTPase, Rnd2 - PMC Skip to main content
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Biochemical Journal logoLink to Biochemical Journal
. 2002 Jul 15;365(Pt 2):349–353. doi: 10.1042/BJ20020062

Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTPase, Rnd2.

Hiroko Tanaka 1, Hirotada Fujita 1, Hironori Katoh 1, Kazutoshi Mori 1, Manabu Negishi 1
PMCID: PMC1222680  PMID: 11931639

Abstract

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'-[beta-thio]triphosphate-bound active and guanosine 5'-[beta-thio]diphosphate-bound inactive forms of Rnd2. An ATPase-defective Vps4-A mutant, Vps4-A(E228Q), expressed in HeLa cells was accumulated in the early endosomes. When Rnd2 was co-expressed with Vps4-A(E228Q), 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.

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Selected References

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