The success of the iBV Night Hike and Run last January, with 30 people exploring the hills of Pessicart and Gairaut under the moonlight, prompted the running club to choose a hiker-friendly trail race this time. As beautiful mountain setting, sunny weather and post-race pasta were also essential prerequisites, the Trail des Merveilles of Breil-sur-Roya on March 3rd, 15 km and 900m D+, seemed like the ideal choice for making everyone happy!
Vangelis at the start, clanging cowbells on the way and a little traffic jam on the first kilometers…wait a minute, this smells like a Chamonix race! But not quite: only in Breil can you have violin, flutes and accordion concertos in the wilderness, a visit through a picturesque farmhouse (hello horsies, ponies, cows and kid goats!) and a route going through the peaceful hamlets of “Libre”.
These cheerful moments, organized by volunteers from the valley, were all the more appreciated as single-track trails were sometimes brutal, starting with a strenuous climb to the well-named tower of the Cruella above the village, later followed by a 500-m elevation gain on 2 km only, through a dark forest. It took strength and courage to all 7 hikers (Marika, Anna, Malala, Alex, Andres, Akif and Zhou) and 4 runners (Marie-Cécile, Nathalie, Clotilde and Olivier), but, rewarded by the beautiful views from the mountain top, they made it happily back to the village, proud of what they had accomplished together.
This Sunday, life was simple: wild landscapes, hospitality of the locals, colleagues made true companions for a race day and joy taken from the effort.
What more to expect? A podium and prize for Nath, 3rd in her category!
iBV is a member of Université Cote d’Azur (UCA), a cluster of Research and Higher Education on the French Riviera. Each year UCA organises a special award ceremony recognising the talent and accomplishments of researchers, students and artists who have been awarded prestigious prizes for their work.
This year, 7 iBV members will take part to the ceremony for their excellent scientific contributions:
The ceremony will take place at the "Galet" amphitheater, at the Pasteur Hospital Center in Nice on Monday December 10th at 6pm.
Congratulations to All Awardees !
Asymmetry plays a major role in biology at every scale: think of DNA spirals, the fact that the human heart is positioned on the left, our preference to use our left or right hand … A team from the Institute of biology Valrose (CNRS/Inserm/Université Côte d’Azur), in collaboration with colleagues from the University of Pennsylvania, has shown how a single protein induces a spiral motion in another molecule. Through a domino effect, this causes cells, organs, and indeed the entire body to twist, triggering lateralized behaviour. This research is published in the journal Science on November 23, 2018.
Our world is fundamentally asymmetrical: think of the double helix of DNA, the asymmetrical division of stem cells, or the fact that the human heart is positioned on the left … But how do these asymmetries emerge, and are they linked to one another?
At the Institute of biology Valrose, the team led by the CNRS researcher Stéphane Noselli, which also includes Inserm and Université Cote d’Azur researchers, has been studying right–left asymmetry for several years in order to solve these enigmas. The biologists had identified the first gene controlling asymmetry in the common fruit fly (Drosophila), one of the biologists’ favoured model organisms. More recently, the team showed that this gene plays the same role in vertebrates: the protein that it produces, Myosin 1D, controls the coiling or rotation of organs in the same direction
In this new study, the researchers induced the production of Myosin 1D in the normally symmetrical organs of Drosophila, such as the respiratory trachea. Quite spectacularly, this was enough to induce asymmetry at all levels: deformed cells, trachea coiling around themselves, the twisting of the whole body, and helicoidal locomotive behavior among fly larvae. Remarkably, these new asymmetries always develop in the same direction.
In order to identify the origin of these cascading effects, biochemists from the University of Pennsylvania contributed to the project too: on a glass coverslip, they brought Myosin 1D into contact with a component of cytoskeleton (the cell’s “backbone”), namely actin. They were able to observe that the interaction between the two proteins caused the actin to spiral.
Besides its role in right–left asymmetry among Drosophila and vertebrates, Myosin 1D appears to be a unique protein that is capable of inducing asymmetry in and of itself at all scales, first at the molecular level, then, through a domino effect, at the cell, tissue, and behavioral level. These results suggest a possible mechanism for the sudden appearance of new morphological characteristics over the course of evolution, such as, for example, the twisting of snails’ bodies. Myosin 1D thus appears to have all the necessary characteristics for the emergence of this innovation, since its expression alone suffices to induce twisting at all scales.
The molecular motor Myosin 1D creates asymmetry at all levels, from the movement of actin molecules (red and green filaments) to respiratory trachea (white tube-like structures), to the organism itself (here a Drosophila larva).
© Photo of larva: Gaëlle Lebreton; photo editing by Stéphane Noselli / iBV / CNRS
This video shows the movement of a normal larva (left) and a larva expressing Myosin 1D in its normally symmetrical epidermis. Whereas the normal larva crawls linearly, with its ventral side in contact with the liquid, the modified larva is twisted and moves via directional “barrel rolls.”
Credit: Gaëlle Lebreton / iBV / CNRS
Molecular to Organismal Chirality is induced by the Conserved Myosin1D, Gaëlle Lebreton, Charles Géminard, François Lapraz, Serapion Pyrpassopoulos, Delphine Cérézo, Pauline Spéder, E. Michael Ostap & Stéphane Noselli. Science, 23 November 2018. DOI: 10.1126/science.aat8642
CNRS Researcher l Stéphane Noselli l T +33 (0)4 92 07 64 33 l email@example.com
 Myosins are a class of proteins that interact with actin (a constituent of cell skeletons or cytoskeletons). The most well-known of them, muscular myosin, makes muscles contract.
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