Search tips
Search criteria 


Logo of biolettersThe Royal Society PublishingBiology LettersAboutBrowse By SubjectAlertsFree Trial
Biol Lett. 2010 June 23; 6(3): 379–381.
Published online 2010 January 13. doi:  10.1098/rsbl.2009.0878
PMCID: PMC2880051

Rab14 from Bombyx mori (Lepidoptera: Bombycidae) shows ATPase activity


Rab GTPases are essential for vesicular transport, whereas adenosine triphosphate (ATP) is the most important and versatile of the activated carriers in the cell. But there are little reports to clarify the connection between ATP and Rab GTPases. A cDNA clone (Rab14) from Bombyx mori was expressed in Escherichia coli as a glutathione S-transferase fusion protein and purified. The protein bound to [3H]-GDP and [35S]-GTPγS. Binding of [35S]-GTPγS was inhibited by guanosine diphosphate (GDP), guanosine triphosphate (GTP) and ATP. Rab14 showed GTP- and ATP-hydrolysis activity. The Km value of Rab14 for ATP was lower than that for GTP. Human Rab14 also showed an ATPase activity. Furthermore, bound [3H]-GDP was exchanged efficiently with GTP and ATP. These results suggest that Rab14 is an ATPase as well as GTPase and gives Rab14 an exciting integrative function between cell metabolic status and membrane trafficking.

Keywords: Bombyx mori, ATP, Rab

Articles from Biology Letters are provided here courtesy of The Royal Society