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Published online 21 August 2000. doi:10.1083/jcb.150.4.755
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© The Rockefeller University Press, 0021-9525/2000//755 $5.00
The Journal of Cell Biology, Volume 150, Number 4, , 2000 755-770

Original Article

Biogenesis of the Protein Storage Vacuole Crystalloid



Liwen Jianga,b, Thomas E. Phillipsc, Sally W. Rogersa, and John C. Rogersa

a Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340
b Department of Biology, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China
c Division of Biological Sciences, University of Missouri, Columbia, Missouri 65211
Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340.(509) 335-7643(509) 335-2773

bcjroger{at}wsu.edu

We identify new organelles associated with the vacuolar system in plant cells. These organelles are defined biochemically by their internal content of three integral membrane proteins: a chimeric reporter protein that moves there directly from the ER; a specific tonoplast intrinsic protein; and a novel receptor-like RING-H2 protein that traffics through the Golgi apparatus. Highly conserved homologues of the latter are expressed in animal cells. In a developmentally regulated manner, the organelles are taken up into vacuoles where, in seed protein storage vacuoles, they form a membrane-containing crystalloid. The uptake and preservation of the contents of these organelles in vacuoles represents a unique mechanism for compartmentalization of protein and lipid for storage.

Key Words: integral membrane protein • storage • protein • prevacuolar compartment • autophagy • RING-H2

© 2000 The Rockefeller University Press

Abbreviations used in this paper: CM, cell membrane fraction; CS, cell soluble fraction; CT, cytoplasmic tail; DIP, dark intrinsic protein; EST, expressed sequence tag; GUS, Escherichia coli β-glucuronidase; PSV, protein storage vacuole; RMR protein, receptor homology region-transmembrane domain-Ring H2 motif; TIP, tonoplast intrinsic protein; TMD, transmembrane domain.


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