Roles of maize PIP2 aquaporins in the structural organization of the cell

Plasma membrane (PM) Intrinsic Proteins (PIPs) are aquaporins that facilitate the diffusion of water through cell membranes. By regulating PIP activity, plant cells adjust water permeability rapidly and reversibly. PIP PM lateral diffusion is affected by the cell wall and actin. Also, PM-located PIPs interact with VAP27s at the endoplasmic reticulum (ER)–PM contact sites (EPCS).

Evidence suggests that PIPs get organized in interaction with other cellular structures. However, the functional relevance of these interactions has not been extensively studied.

The PIPContactSites project's main goal is to understand whether ZmPIP2s mediate PM interaction with other cellular structures (ER, cytoskeleton) and elucidate the physiological relevance of the contact sites under salt stress conditions.

Our hypothesis is that PIP2 interactions on EPCS and with the cytoskeleton facilitate an efficient response to stimuli by participating in the structural organization of the cell.

Our strategy integrates cutting-edge technologies for genome edition (CRISPR/Cas9) and real-time monitoring of interactions (split Fluorescence-Activating and absorption Shifting Tag) with advanced microscopy technologies (i.e., confocal super-resolution and Correlative Light and Electron Microscopy).

The originality of this project is to consider PIPs as multifunctional proteins: channels and scaffold proteins.

The MSCA fellowship, the great intellectual environment, the infrastructure and the administrative support at the LIBST-UCLouvain, the research and project managing experience of Prof. Chaumont, and my background in molecular biology will synergistically promote the success of the project. The host group will benefit from hosting an independent, creative, and highly skilled scientist.

And I will gain experience and networking opportunities to shape my long-term objective of becoming a group leader.