Modulating cAMP and cGMP Levels to Treat Fragile X Syndrome

FRAXA Research Foundation funded a 2016 grant of $90,000 over two years for a postdoctoral fellowship for Thomas Maurin, PhD, who is working under the mentorship of Dr. Barbara Bardoni at INSERM in France. This project has been renewed in 2017 for a second year. The team works on the biochemistry of the fragile X protein.

$90,000 Grant
Thomas Maurin, PhD
FRAXA Fellow
Barbara Bardoni, PhD
Principal Investigator
INSERM – Valbonne, France
2016 FRAXA Research Grant
$90,000 over 2 Years

The fragile X protein (FMRP) does not work alone. FMRP is present in particles which contain many other proteins, and the composition of these particles can vary significantly. Understand the protein partners of FMRP and their roles in shaping the different normal functions of FMRP is the primary interest of the Bardoni lab.

Read More: Brain Revolution: French Scientists Study FMRP

Previous Grant to this Team
$30,000 in 2005
Composition and Dynamics of FMRP-Containing RNP Complexes

FMRP is a RNA-binding protein containing at least three domains mediating its binding to RNA (two KH domains and one RGG box) and it appears to be implicated in several steps of mRNA metabolism. These properties suggest that it is likely a component of different complexes, whose identification will result in a more precise dissection of FMRP function.

We plan to use sucrose gradient fractionation and FPLC chromatography with the purpose to perform a detailed analysis of FMRP-containing complexes in cultured cell lines and mouse brain, taking into consideration the composition and the dynamics of FMRP-containing complexes, the expression of FMRP-interacting proteins and, as a more long term project, the expression level of mRNAs that are targets of FMRP.

Another important point is to clearly elucidate the anatomy of the FMRP/mRNA complex at the molecular level. During the last four years, many putative RNA targets for FMRP have been identified. However, up to date, it has been reported that FMRP binds only two structures (G-quartet and kissing complex RNA) and a sequence (poly(U) stretch). We propose here a novel approach to identify sequence and/or structures, other than purine-quartet, that are recognized and bound by FMRP.