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Delivery of a Secreted Soluble Protein to the Vacuole via a
Membrane Anchor1
François Barrieu and
Maarten J. Chrispeels*
Department of Biology, University of California at San Diego, La
Jolla, California 92093-0116
To further understand how membrane
proteins are sorted in the secretory system, we devised a strategy that
involves the expression of a membrane-anchored yeast invertase in
transgenic plants. The construct consisted of a signal peptide followed
by the coding region of yeast invertase and the transmembrane domain
and cytoplasmic tail of calnexin. The substitution of a lysine near the
C terminus of calnexin with a glutamic acid residue ensured progression
through the secretory system rather than retention in or return to the endoplasmic reticulum. In the transformed plants, invertase activity and a 70-kD cross-reacting protein were found in the vacuoles. This
yeast invertase had plant-specific complex glycans, indicating that
transport to the vacuole was mediated by the Golgi apparatus. The
microsomal fraction contained a membrane-anchored 90-kD cross-reacting polypeptide, but was devoid of invertase activity. Our results indicate
that this membrane-anchored protein proceeds in the secretory system
beyond the point where soluble proteins are sorted for secretion, and
is detached from its membrane anchor either just before or just after
delivery to the vacuole.
1
This work was supported by a grant from the U.S.
Department of Energy, Energy Biosciences Program.
*
Corresponding author; e-mail mchrispeels{at}ucsd.edu; fax
619-534-4052.
Plant Physiol. (1999) 120: 961-968
Copyright Clearance Center: 0032-0889/99/120//08
© 1999 American Society of Plant Physiologists
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