In our lab we challenge the central dogma postulating that regulation of gene expression and protein quantity is a unidirectional process. We have recently shown how tubulin protein quantity feeds back into its encoding mRNA stability via a specificity factor. Our goal is to reveal how cells control protein quantity to ensure homeostasis. To address the functional aspects of protein quantity control, we love fluorescent imaging of live and fixed mammalian cultured cells.
Our favourite proteins are tubulins—the main constituents of the microtubule cytoskeleton. Tubulins are amongst the most abundant proteins in cells (making ~1% of cellular proteome!). They exist as soluble heterodimers and polymers known as microtubules. Microtubules are exceptionally dynamic, undergoing phases of growth and shrinkage. And so they re-invent themselves over and over, to respond to cellular needs. These properties, combined with exceptional chemical tools to manipulate them make tubulins and microtubules an ideal system to study how protein quantity is achieved and how it impacts cellular functions. Under the microscope, microtubules resemble a cob web, and when filmed live in partnership with their end-binding proteins they throw a real fireworks show.
But we understand that the world doesn't spin around tubulins and are eager to welcome new fellows whose precise quantity is key to cellular happiness. To learn more about us, read on or visit us in the beautiful international city of Geneva in Switzerland, at the Faculty of Sciences.