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Published on December 19, 2008; 10.1104/pp.108.127936

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Received August 10, 2008
Accepted December 18, 2008

A pollen protein, NaPCCP, that binds pistil arabinogalactan proteins also binds phosphatidylinositol 3-phosphate and associates with the pollen tube endomembrane system

Christopher B. Lee , Sunran Kim , and Bruce McClure *

Division of Biological Sciences, Interdisciplinary Plant Group, 247 Christopher S. Bond Life Sciences Center, University of Missouri, 1201 Rollins St., Columbia, Missouri, 65211; Division of Biochemistry, Interdisciplinary Plant Group, Christopher S. Bond Life Sciences Center, 240a Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, Missouri, 65211

* Corresponding author; email: mcclureb{at}missouri.edu.

As pollen tubes grow toward the ovary, they are in constant contact with the pistil extracellular matrix (ECM). ECM components are taken up during growth, and some pistil molecules exert their effect inside the pollen tube. For instance, the Nicotiana alata 120 kDa glycoprotein (120K) is an abundant arabinogalactan protein (AGP) that is taken up from the ECM; it has been detected in association with pollen tube vacuoles, but the transport pathway between these compartments is unknown. We recently identified a pollen C2-domain-containing protein (NaPCCP) that binds to the C-terminal domain of 120K. As C2-domain proteins mediate protein-lipid interactions, NaPCCP could function in intracellular transport of 120K in pollen tubes. Here, we describe binding studies showing that the NaPCCP C2-domain is functional and that binding is specific for phosphatidylinositol 3-phosphate (PI3P). Subcellular fractionation, immunolocalization, and live imaging results show that NaPCCP is associated with the plasma membrane and internal pollen tube vesicles. Colocalization between an NaPCCP::GFP fusion and internalized FM4-64 suggest an association with the endosomal system. NaPCCP localization is altered in pollen tubes rejected by the self-incompatibility (SI) mechanism, but our hypothesis is that it has a general function in transport of endocytic cargo rather than a specific function in SI. NaPCCP represents a bifunctional protein with both PI3P- and AGP-binding domains. It could, therefore, function in transport of pistil ECM proteins in the pollen tube endomembrane system.




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B. McClure
Darwin's foundation for investigating self-incompatibility and the progress toward a physiological model for S-RNase-based SI
J. Exp. Bot., March 1, 2009; 60(4): 1069 - 1081.
[Abstract] [Full Text] [PDF]


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