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First published online August 26, 2005; 10.1105/tpc.105.034330

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The Plant Cell 17:2817-2831 (2005)
© 2005 American Society of Plant Biologists

Plasmodesmal-Associated Protein Kinase in Tobacco and Arabidopsis Recognizes a Subset of Non-Cell-Autonomous Proteins{boxw}

Jung-Youn Leea,b,1, Ken-ichiro Taokaa, Byung-Chun Yooa,b,2, Gili Ben-Nissanb, Dong-Jin Kimb and William J. Lucasa,1

a Section of Plant Biology, Division of Biological Sciences, University of California, Davis, California 95616
b Plant and Soil Sciences, Delaware Biotechnology Institute, University of Delaware, Newark, Delaware 19711

1 To whom correspondence should be addressed. E-mail lee{at}dbi.udel.edu or wjlucas{at}ucdavis.edu; fax 302-831-4841 or 530-753-5410.

Cell-to-cell communication in plants involves the trafficking of macromolecules through specialized intercellular organelles, termed plasmodesmata. This exchange of proteins and RNA is likely regulated, and a role for protein phosphorylation has been implicated, but specific components remain to be identified. Here, we describe the molecular characterization of a plasmodesmal-associated protein kinase (PAPK). A 34-kD protein, isolated from a plasmodesmal preparation, exhibits calcium-independent kinase activity and displays substrate specificity in that it recognizes a subset of viral and endogenous non-cell-autonomous proteins. This PAPK specifically phosphorylates the C-terminal residues of tobacco mosaic virus movement protein (TMV MP); this posttranslational modification has been shown to affect MP function. Molecular analysis of purified protein established that tobacco (Nicotiana tabacum) PAPK is a member of the casein kinase I family. Subcellular localization studies identified a possible Arabidopsis thaliana PAPK homolog, PAPK1. TMV MP and PAPK1 are colocalized within cross-walls in a pattern consistent with targeting to plasmodesmata. Moreover, Arabidopsis PAPK1 also phosphorylates TMV MP in vitro at its C terminus. These results strongly suggest that Arabidopsis PAPK1 is a close homolog of tobacco PAPK. Thus, PAPK1 represents a novel plant protein kinase that is targeted to plasmodesmata and may play a regulatory role in macromolecular trafficking between plant cells.




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