Main research interest:
My main research interest is to understand how AAA+ ATPases are using ATP hydrolysis to remodel their specific substrates. Indeed, in all kingdom of life, a same structural unit (AAA+ core) is used for very versatile cellular activities (for example for transcription activation, protein degradation, or microtubule severing).

Understanding the conserved feature of such domain is critical to understand how these different molecular machines are working. In addition, more and more human diseases have been linked to defective proteins member of the AAA+ protein family. Strikingly, deep sequencing approaches have reported that the mutations responsible for the activity default were, in most of the time, located into the AAA+ core, pointing out the importance of understanding the molecular bases allowing the AAA+ core to use ATP hydrolysis and to transmit this "energy" to the remodeling motifs.

Currently, I am using the AAA+ microtubule-severing enzyme Katanin as system model.

Contact : email

Recent papers:

Richarme G, Liu C, Mihoub M, Abdallah J, Leger T, Joly N, Liebart JC, Jurkunas UV, Nadal M, Bouloc P, Dairou J, Lamouri A.
Science. 2017 Jun 8. pii: eaag1095. doi: 10.1126/science.aag1095. [Epub ahead of print] PMID: 28596309

Joly N, Martino L, Gigant E, Dumont J, Pintard L.
Development. 2016 Oct 1;143(19):3604-3614.

Thomas Y, Cirillo L, Panbianco C, Martino L, Tavernier N, Schwager F, Van Hove L, Joly N, Santamaria A, Pintard L, Gotta M.
Cell Rep. 2016 Apr 5. pii: S2211-1247(16)30320-5. doi: 10.1016/j.celrep.2016.03.049. 

In vitro and in vivo methodologies for studying the sigma 54-dependent transcription.

Buck M, Engl C, Joly N, Jovanovic G, Jovanovic M, Lawton E, McDonald C, Schumacher J, Waite C, Zhang N.
Methods Mol Biol. 2015;1276:53-79. doi: 10.1007/978-1-4939-2392-2_4.