Community Research and Development Information Service - CORDIS

ERC

APPL Report Summary

Project ID: 336360
Funded under: FP7-IDEAS-ERC
Country: France

Mid-Term Report Summary - APPL (Anionic PhosPhoLipids in plant receptor kinase signaling)

Many signalling proteins permanently or transiently localize to specific organelles for function. It is well established that certain lipids act as biochemical landmarks to specify compartment identity. However, they also influence membrane biophysical properties, which emerge as important features in specifying cellular territories. Such parameters include the membrane inner surface potential, which varies according to the lipid composition of each organelle. In particular, anionic phospholipids, which are minor lipids in biological membranes, are critical to establish membrane electrostatic properties as well as defining docking platforms on the surface of cellular compartments. Using plants as a research model, we are tackling the following questions:

i) Where are anionic phospholipids localized in the cell and by which mechanisms?
ii) What are the functions of these anionic phospholipids in controlling membrane identity and organization?
iii) How anionic phospholipids contribute to receptor signalling to regulate plant development?

We found that the plant plasma membrane (PM) and the cell plate of dividing cells have a unique electrostatic signature controlled by phosphatidylinositol-4-phosphate (PI4P) (Simon, Platre et al., 2016 Nature Plants). Our results further revealed that, contrarily to other eukaryotes, PI4P massively accumulates at the PM, establishing it as a critical hallmark of this membrane in plants. Membrane surface charges control the PM localization and function of the polar auxin transport regulator PINOID, as well as proteins from the BRI1 KINASE INHIBITOR1 (BKI1)/MEMBRANE ASSOCIATED KINASE REGULATORs (MAKRs) family, which are involved in brassinosteroid and receptor-like kinase signalling. We anticipate that this PI4P-driven physical membrane property will control the localization and function of many proteins involved in development, reproduction, immunity and nutrition.

Contact

Pascaline TOUTOIS, (Responsable Service Partenariat et Valorisation)
Tel.: +33 472445641
E-mail
Follow us on: RSS Facebook Twitter YouTube Managed by the EU Publications Office Top