RT Journal Article
SR Electronic
T1 Molecular Cloning and Further Characterization of a Probable Plant Vacuolar Sorting Receptor
JF Plant Physiology
JO Plant Physiol.
FD American Society of Plant Biologists
SP 29
OP 39
DO 10.1104/pp.115.1.29
VO 115
IS 1
A1 Paris, N.
A1 Rogers, S. W.
A1 Jiang, L.
A1 Kirsch, T.
A1 Beevers, L.
A1 Phillips, T. E.
A1 Rogers, J. C.
YR 1997
UL http://www.plantphysiol.org/content/115/1/29.abstract
AB 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.