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First published online May 28, 2005
doi: 10.1242/10.1242/jcs.02369

Journal of Cell Science 118, 2471-2484 (2005)
Published by The Company of Biologists 2005
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Research Article

Centaurin-{alpha}1 interacts directly with kinesin motor protein KIF13B

Kanamarlapudi Venkateswarlu1,*, Toshihiko Hanada2 and Athar H. Chishti2

1 Department of Pharmacology, School of Medical Sciences, The University of Bristol, University Walk, Bristol, BS8 1TD, UK
2 Department of Pharmacology, UIC Cancer Center, University of Illinois College of Medicine, 900 S. Ashland Avenue, Chicago, IL 60607, USA

* Author for correspondence (e-mail: k.venkateswarlu{at}bristol.ac.uk)

Accepted 9 March 2005

Centaurin-{alpha}1 is a phosphatidylinositol 3,4,5-trisphosphate binding protein as well as a GTPase activating protein (GAP) for the ADP-ribosylation factor (ARF) family of small GTPases. To further understand its cellular function, we screened a rat brain cDNA library using centaurin-{alpha}1 as bait to identify centaurin-{alpha}1 interacting proteins. The yeast two-hybrid screen identified a novel kinesin motor protein as a centaurin-{alpha}1 binding partner. The motor protein, termed KIF13B, encoded by a single ~9.5-kb transcript, is widely expressed with high levels observed in brain and kidney. Yeast two-hybrid and GST pull-down assays showed that the interaction between centaurin-{alpha}1 and KIF13B is direct and mediated by the GAP domain of centaurin-{alpha}1 and the stalk domain of KIF13B. Centaurin-{alpha}1 and KIF13B form a complex in vivo and the KIF13B interaction appears to be specific to centaurin-{alpha}1 as other members of the ARF GAP family did not show any binding activity. We also show that KIF13B and centaurin-{alpha}1 colocalize at the leading edges of the cell periphery whereas a deletion mutant of centaurin-{alpha}1 that lacks the KIF13B binding site, failed to colocalize with KIF13B in vivo. Finally, we demonstrate that KIF13B binding suppresses the ARF6 GAP activity of centaurin-{alpha}1 in intact cells. Together, our data suggest a mechanism where direct binding between centaurin-{alpha}1 and KIF13B could concentrate centaurin-{alpha}1 at the leading edges of cells, thus modulating ARF6 function.

Key words: Centaurin-{alpha}1, KIF13B, PI 3-kinase, PtdIns(3,4,5)P3, ARF6, Trafficking


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