UNSPECIFIED. (1997) Protein quality control along the route to the plant vacuole. PLANT CELL, 9 (10). pp. 1869-1880. ISSN 1040-4651

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Abstract

To acquire information on the relationships between structural maturation of proteins in the endoplasmic reticulum (ER) and their transport along the secretory pathway, we have analyzed the destiny of an assembly-defective form of the trimeric vacuolar storage glycoprotein phaseolin. In leaves of transgenic tobacco, where assembly-competent phaseolin is correctly targeted to the vacuole, defective phaseolin remains located in the ER or a closely related compartment where it represents a major ligand of the chaperone Dip. Defective phaseolin maintained susceptibility to endoglycosidase H and was slowly degraded by a process that is not inhibited by heat shock or brefeldin A, indicating that degradation does not involve transport along the secretory pathway. These results provide evidence for the presence of a quality control mechanism in the ER of plant cells that avoids intracellular trafficking of severely defective proteins and eventually leads to their degradation.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry S Agriculture > SB Plant culture Q Science > QH Natural history > QH301 Biology
Journal or Publication Title:	PLANT CELL
Publisher:	AMER SOC PLANT PHYSIOLOGISTS
ISSN:	1040-4651
Official Date:	October 1997
Dates:	Date Event October 1997 UNSPECIFIED
Volume:	9
Number:	10
Number of Pages:	12
Page Range:	pp. 1869-1880
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/16294

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