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Vol. 17, Issue 5, 2476-2487, May 2006

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Arl2 and Arl3 Regulate Different Microtubule-dependent Processes

Chengjing Zhou ^*, Leslie Cunningham ^*, Adam I. Marcus , Yawei Li ^*, and Richard A. Kahn ^*

^* Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322-3050; Department of Winship Cancer Institute, Emory University School of Medicine, Atlanta, GA 30322-3050

Submitted October 14, 2005; Revised February 21, 2006; Accepted February 27, 2006
Monitoring Editor: Sean Munro

Arl2 and Arl3 are closely related members of the Arf family of regulatory GTPases that arose from a common ancestor early in eukaryotic evolution yet retain extensive structural, biochemical, and functional features. The presence of Arl3 in centrosomes, mitotic spindles, midzones, midbodies, and cilia are all supportive of roles in microtubule-dependent processes. Knockdown of Arl3 by siRNA resulted in changes in cell morphology, increased acetylation of -tubulin, failure of cytokinesis, and increased number of binucleated cells. We conclude that Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis. In contrast, an excess of Arl2 activity, achieved by expression of the [Q70L]Arl2 mutant, caused the loss of microtubules and cell cycle arrest in M phase. Initial characterization of the underlying defects suggests a defect in the ability to polymerize tubulin in the presence of excess Arl2 activity. We also show that Arl2 is present in centrosomes and propose that its action in regulating tubulin polymerization is mediated at centrosomes. Somewhat paradoxically, no phenotypes were observed Arl2 expression was knocked down or Arl3 activity was increased in HeLa cells. We conclude that Arl2 and Arl3 have related but distinct roles at centrosomes and in regulating microtubule-dependent processes.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Address correspondence to: Richard A. Kahn (rkahn{at}emory.edu).

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