Concerted Transport and Phosphorylation of Diacylglycerol at ER-PM Contacts Sites Regulates Phospholipid Dynamics During Stress

A - Papers appearing in refereed journals

Garcia-Hernandez, S., Haslam, R. P., Moya-Cuevas, J., Catala, R., Michaelson, L. V., Amorim-Silva, V., Markovic, V., Salinas, J., Napier, J. A., Jaillais, Y., Ruiz-Lopez, N. and Botella, M. A. 2024. Concerted Transport and Phosphorylation of Diacylglycerol at ER-PM Contacts Sites Regulates Phospholipid Dynamics During Stress. bioRxiv. https://doi.org/10.1101/2024.01.16.575708

AuthorsGarcia-Hernandez, S., Haslam, R. P., Moya-Cuevas, J., Catala, R., Michaelson, L. V., Amorim-Silva, V., Markovic, V., Salinas, J., Napier, J. A., Jaillais, Y., Ruiz-Lopez, N. and Botella, M. A.
Abstract

A universal response of plants to environmental stresses is the activation of plasma membrane (PM) phospholipase C (PLC) that hydrolyzes phosphatidylinositol phosphate (PIP) to produce soluble inositol phosphate (IP) and diacylglycerol (DAG). DAG produced in this way can be either phosphorylated by PM diacylglycerol kinases (DGKs) to produce the second messenger phosphatidic acid (PA) or transferred to the endoplasmic reticulum (ER) by the Synaptotagmin 1 (SYT1) protein at ER-PM Contact Sites (CS). In Arabidopsis, the clearance of DAG at the PM (avoiding deleterious accumulation) by the transfer activity of SYT is essential to maintain PM stability after stress. In this study we identify that DGK1 and DGK2 form a module with SYT1 at ER-PM CS through interaction of their C1 and C2 domains respectively. Global transcriptomic and metabolomic analyses confirms that SYT1 and DGK1/DGK2 are functionally related and lipidomic analysis supports the hypothesis that DGK1 and DGK2 function at the ER by phosphorylating DAG transferred by SYT1 from the PM. DGK1 and DGK2 show structural similarity to human DGKε, the DGK isoform that function at ER-PM CS in the phosphoinositide (PI) cycle. Our data indicate that components of the PI cycle are conserved between animals and plants and provide a novel mechanism leading to an increase in the efficiency of the PI cycle by channeling the transport and hydrolysis of DAG at the ER-PM CS.

Year of Publication2024
JournalbioRxiv
Digital Object Identifier (DOI)https://doi.org/10.1101/2024.01.16.575708
Open accessPublished as non-open access
FunderBiotechnology and Biological Sciences Research Council
Funder project or codeGreen Engineering - knowledge-based delivery of sustainable products in plants (WP1): Harnessing endogenous pathways to enhance yield
Publisher's version
Output statusPublished
Publication dates
Online17 Jan 2024
PublisherPublic Library of Science (PLOS)

Permalink - https://repository.rothamsted.ac.uk/item/98z5x/concerted-transport-and-phosphorylation-of-diacylglycerol-at-er-pm-contacts-sites-regulates-phospholipid-dynamics-during-stress

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