Journal
PLANT SIGNALING & BEHAVIOR
Volume 9, Issue 7, Pages -Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/psb.28194
Keywords
BiP; endoplasmic reticulum; Hsp70; J-protein; rice seed; vacuole
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [25292220]
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J-proteins are co-chaperone components of the HSP70 system. J-proteins stimulate Hsp70ATPase activity, which is responsible for stabilizing the interaction of Hsp70 with client proteins. J-proteins are localized in various intracellular compartments including the cytoplasm, mitochondria and endoplasmic reticulum (ER). Five types of ER resident J-proteins (ERdjs) have been found in plants (P58,ERdj2, ERdj2A, ERdj3B and ERdj7). Rice OsERdj3A is located in the vacuole and protein storage vacuoles (PSV, PB-II) under conditions of ER stress. J-proteins that are localized to the vacuole or lysosome are not found in mammals and yeast, suggesting that the presence of OsERdj3A in the vacuole is plant-specific and one of the features unique to plant ERdjs. In this review, we summarize the current state of knowledge and recent research advancements regarding plant ERdjs, and compare mammalian and yeast ERdjs with plant ERdjs.
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