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First published online October 1, 2004; 10.1104/pp.104.045369

Plant Physiology 136:3080-3094 (2004)
© 2004 American Society of Plant Biologists

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CELL BIOLOGY AND SIGNAL TRANSDUCTION

Patellin1, a Novel Sec14-Like Protein, Localizes to the Cell Plate and Binds Phosphoinositides1

T. Kaye Peterman*, Yamini M. Ohol2, Lisa J. McReynolds3 and Elizabeth J. Luna

Department of Biological Sciences, Wellesley College, Wellesley, Massachusetts 02481 (T.K.P., Y.M.O., L.J.M.); and Department of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01605 (E.J.L.)

Membrane trafficking is central to construction of the cell plate during plant cytokinesis. Consequently, a detailed understanding of the process depends on the characterization of molecules that function in the formation, transport, targeting, and fusion of membrane vesicles to the developing plate, as well as those that participate in its consolidation and maturation into a fully functional partition. Here we report the initial biochemical and functional characterization of patellin1 (PATL1), a novel cell-plate-associated protein that is related in sequence to proteins involved in membrane trafficking in other eukaryotes. Analysis of the Arabidopsis genome indicated that PATL1 is one of a small family of Arabidopsis proteins, characterized by a variable N-terminal domain followed by two domains found in other membrane-trafficking proteins (Sec14 and Golgi dynamics domains). Results from immunolocalization and biochemical fractionation studies suggested that PATL1 is recruited from the cytoplasm to the expanding and maturing cell plate. In vesicle-binding assays, PATL1 bound to specific phosphoinositides, important regulators of membrane trafficking, with a preference for phosphatidylinositol(5)P, phosphatidylinositol(4,5)P2, and phosphatidylinositol(3)P. Taken together, these findings suggest a role for PATL1 in membrane-trafficking events associated with cell-plate expansion or maturation and point to the involvement of phosphoinositides in cell-plate biogenesis.

1 This work was supported by the United States Department of Agriculture (grant no. 2001–35304–10903 to T.K.P.) and benefited from support from the National Institutes of Health (grant no. GM33048 to E.J.L.).

2 Present address: Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143–2200.

3 Present address: Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY 10461.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.045369.

* Corresponding author; e-mail kpeterman{at}wellesley.edu; fax 781–283–3642.

Received April 29, 2004; returned for revision July 23, 2004; accepted July 23, 2004.


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