Biogenesis of the Protein Storage Vacuole Crystalloid

doi:10.1083/jcb.150.4.755

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 Jiang^a^,b, Thomas E. Phillips^c, Sally W. Rogers^a, and John C. Rogers^a

^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 systemin plant cells. These organelles are defined biochemically bytheir internal content of three integral membrane proteins:a chimeric reporter protein that moves there directly from theER; a specific tonoplast intrinsic protein; and a novel receptor-likeRING-H2 protein that traffics through the Golgi apparatus. Highlyconserved homologues of the latter are expressed in animal cells.In a developmentally regulated manner, the organelles are takenup into vacuoles where, in seed protein storage vacuoles, theyform a membrane-containing crystalloid. The uptake and preservationof the contents of these organelles in vacuoles represents aunique mechanism for compartmentalization of protein and lipidfor storage.

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

Abbreviations used in this paper: CM, cell membrane fraction;CS, cell soluble fraction; CT, cytoplasmic tail; DIP, dark intrinsicprotein; EST, expressed sequence tag; GUS, Escherichia coliβ-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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