First published online October 14, 2005; 10.1105/tpc.105.035212
The Plant Cell 17:3066-3080 (2005)
© 2005 American Society of Plant Biologists
Selective Membrane Protein Internalization Accompanies Movement from the Endoplasmic Reticulum to the Protein Storage Vacuole Pathway in Arabidopsis
Mohammed Oufattolea,
Joon Ho Parka,
Marianne Poxleitnera,
Liwen Jiangb and
John C. Rogersa,1,2
a Institute of Biological Chemistry, Washington State University, Pullman, Washington 99163
b Department of Biology, Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China
2 To whom correspondence should be addressed. E-mail jrogers{at}nsf.gov; fax 703-292-9061.
In plant cells, certain membrane proteins move by unknown mechanisms directly from the endoplasmic reticulum (ER) to prevacuolar or vacuole-like organelles where membrane is internalized to form a dense, lattice-like structure. Here, we identify a sequence motif, PIEPPPHH, in the cytoplasmic tail of a membrane protein that directs the protein from the ER to vacuoles where it is internalized. A type II membrane protein in Arabidopsis thaliana, (At)SRC2 (for Soybean Gene Regulated by Cold-2), binds specifically to PIEPPPHH and moves from the ER to the same vacuoles where it is internalized. Not all proteins that move in this pathway are internalized because another Arabidopsis type II membrane protein, (At)VAP (for Vesicle-Associated Protein), localizes to the same organelles but remains exposed on the limiting membrane. The identification of (At)SRC2 and its preference for interaction with a targeting motif specific for the ER-to-vacuole pathway may provide tools for future dissection of mechanisms involved in this unique trafficking system.
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