Protein quality control along the route to the plant vacuole
UNSPECIFIED. (1997) Protein quality control along the route to the plant vacuole. PLANT CELL, 9 (10). pp. 1869-1880. ISSN 1040-4651Full text not available from this repository.
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|
|Official Date:||October 1997|
|Number of Pages:||12|
|Page Range:||pp. 1869-1880|
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