Journal
ISCIENCE
Volume 23, Issue 3, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.isci.2020.100889
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Funding
- Ministere de la Recherche Francaise
- UCLouvain-FSR
- UCLouvain-ADRI
- Wallonia-Brussels Federation Joint Research Action (ARC grant) [11/16-036]
- Belgian Funds for Scientific Research (FNRS) [19516174, 6794930, T.0050.18]
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Conserved translocator proteins (TSPOs) mediate cell stress responses possibly in a cell-type-specific manner. This work reports on the molecular function of plant TSPO and their possible evolutionary divergence. Arabidopsis thaliana TSPO (AtTSPO) is stress induced and has a conserved polybasic, plant-specific N-terminal extension. AtTSPO reduces water loss by depleting aquaporin PIP2;7 in the plasma membrane. Herein, AtTSPO was found to bind phosphoinositides in vitro, but only fulllength AtTSPO or chimericmouse TSPO with an AtTSPON-terminus bound PI(4,5)P-2 in vitro andmodified PIP2;7 levels in vivo. Expression of AtTSPO but not its N-terminally truncated variant enhanced phospholipase C activity and depleted PI(4,5)P-2 from the plasma membrane and its enrichment in Golgi membranes. Deletion or point mutations within the AtTSPO N-terminus affected PI(4,5)P-2 binding and almost prevented AtTSPO-PIP2;7 interaction in vivo. The findings imply functional divergence of plant TSPOs from bacterial and animal counterparts via evolutionary acquisition of the phospholipid-interacting N-terminus.
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