TY - JOUR
AU - Rogers, J. C.
AB - Abstract 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. This content is only available as a PDF. Copyright © 1997 by American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)
TI - Molecular Cloning and Further Characterization of a Probable Plant Vacuolar Sorting Receptor
JF - Plant Physiology
DO - 10.1104/pp.115.1.29
DA - 1997-09-01
UR - https://www.deepdyve.com/lp/oxford-university-press/molecular-cloning-and-further-characterization-of-a-probable-plant-5SaC54dD2A
SP - 29
EP - 39
VL - 115
IS - 1
DP - DeepDyve
ER -