Molecular cloning and further characterization of a probable plant vacuolar sorting receptor.

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.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Paris N,Rogers SW,Jiang L,Kirsch T,Beevers L,Phillips TE,Rogers JC

doi

10.1104/pp.115.1.29

subject

Has Abstract

pub_date

1997-09-01 00:00:00

pages

29-39

issue

1

eissn

0032-0889

issn

1532-2548

pii

115/1/29

journal_volume

115

pub_type

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