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, 0021-9525/2000/8/755/ $5.00
The Journal of Cell Biology, Volume 150, Number 4, August 21, 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

Correspondence to: John C. Rogers, Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340. Tel:(509) 335-2773 Fax:(509) 335-7643 E-mail: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

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