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J Biol Chem, Vol. 274, Issue 21, 14724-14733, May 21, 1999
From the Department of Botany and Plant Sciences, University of
California, Riverside, California 92521-0124
Arabinogalactan proteins constitute a class of
plant cell surface proteoglycans with widespread occurrence and
suggested functions in various aspects of plant growth and development,
including cell proliferation, expansion, marking, and death. Previous
investigations of subcellular fractions from suspension-cultured cells
of "Paul's Scarlet" rose (Rosa sp.) have revealed
extensive structural similarity between some soluble arabinogalactan
proteins from the cell wall space and some plasma membrane-associated
arabinogalactan proteins, thus inspiring the present investigation of
the mechanism through which these inherently water-soluble molecules
are held on the plasma membrane. Several lines of evidence gained
through a combination of methods including reversed-phase
chromatography, treatment with phosphatidylinositol-specific
phospholipase C, and chemical structural analysis now show that some
rose arabinogalactan proteins carry a ceramide class
glycosylphosphatidylinositol lipid anchor. The predominant form of the
ceramide is composed of tetracosanoic acid and 4-hydroxysphinganine.
Plasma membrane vesicles readily shed arabinogalactan proteins by an
inherent mechanism that appears to involve a phospholipase. This
finding has significance toward understanding the biosynthesis,
localization, and function of arabinogalactan proteins and toward
stimulating other studies that may expand the currently very short list
of higher plant proteins found to carry such membrane lipid anchors.
Presence of a Glycosylphosphatidylinositol Lipid Anchor on Rose
Arabinogalactan Proteins
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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