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PLANT PHYSIOLOGY , Vol 115, Issue 1 29-39, Copyright © 1997 by American Society of Plant Biologists

CELL BIOLOGY AND SIGNAL TRANSDUCTION

Molecular Cloning and Further Characterization of a Probable Plant Vacuolar Sorting Receptor

N. Paris, S. W. Rogers, L. Jiang, T. Kirsch, L. Beevers, T. E. Phillips and J. C. Rogers
Biochemistry Department (N.P., S.W.R., L.J., J.C.R.), and Division of Biological Sciences (T.E.P.), University of Missouri, Columbia, Missouri 65211

BP-80 is a type I integral membrane protein abundant in pea (Pisum sativum) clathrin-coated vesicles (CCVs) that binds with high affinity to vacuole-targeting determinants containing asparagine-proline-isoleucine-arginine. Here we present results from cDNA cloning and studies of its intracellular localization. Its sequence and sequences of homologs from Arabidopsis, rice (Oryza sativa), and maize (Zea mays) define a novel family of proteins unique to plants that is highly conserved in both monocotyledons and dicotyledons. The BP-80 protein is present in dilated ends of Golgi cisternae and in "prevacuoles," which are small vacuoles separate from but capable of fusing with lytic vacuoles. Its cytoplasmic tail contains a Tyr-X-X-hydrophobic residue motif associated with transmembrane proteins incorporated into CCVs. When transiently expressed in tobacco (Nicotiana tabacum) suspension-culture protoplasts, a truncated form lacking transmembrane and cytoplasmic domains was secreted. These results, coupled with previous studies of ligand-binding specificity and pH dependence, strongly support our hypothesis that BP-80 is a vacuolar sorting receptor that trafficks in CCVs between Golgi and a newly described prevacuolar compartment.


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