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J. Biol. Chem., Vol. 282, Issue 19, 14121-14131, May 11, 2007

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Arabidopsis Phosphatidylinositol Phosphate Kinase 1 Binds F-actin and Recruits Phosphatidylinositol 4-Kinase 1 to the Actin Cytoskeleton^*

Amanda J. Davis, Yang Ju Im, Joshua S. Dubin, Kenneth B. Tomer, and Wendy F. Boss¹

From the Plant Biology, North Carolina State University, Raleigh, North Carolina 27695 and Laboratory of Structural Biology, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709

The actin cytoskeleton can be influenced by phospholipids and lipid-modifying enzymes. In animals the phosphatidylinositol phosphate kinases (PIPKs) are associated with the cytoskeleton through a scaffold of proteins; however, in plants such an interaction was not clear. Our approach was to determine which of the plant PIPKs interact with actin and determine whether the PIPK-actin interaction is direct. Our results indicate that AtPIPK1 interacts directly with actin and that the binding is mediated through a predicted linker region in the lipid kinase. AtPIPK1 also recruits AtPI4K1 to the cytoskeleton. Recruitment of AtPI4K1 to F-actin was dependent on the C-terminal catalytic domain of phosphatidylinositol-4-phosphate 5-kinase but did not require the presence of the N-terminal 251 amino acids, which includes 7 putative membrane occupation and recognition nexus motifs. In vivo studies confirm the interaction of plant lipid kinases with the cytoskeleton and suggest a role for actin in targeting PIPKs to the membrane.

Received for publication, December 21, 2006 , and in revised form, March 14, 2007.

^* This work was supported in part by funding from the North Carolina Agricultural Research Service and by the National Science Foundation (to W. F. B.) and by the NIEHS, National Institutes of Health (to K. B. T.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1–3.

¹ To whom correspondence should be addressed: Plant Biology, Box 7649, NC State University, Raleigh NC 27695-7649. Tel.: 919-515-3496; Fax: 919-515-3436; E-mail: wendy_boss{at}ncsu.edu.

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