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Nicolas Joly

 

Since 2025: Research Director, DR2 CNRS in Dr L. Pintard laboratory (Cell Cycle and Development, Institut Jacques Monod).

2015-2025: Researcher, CR1 CNRS in Dr L. Pintard laboratory (Cell Cycle and Development, Institut Jacques Monod).

2011-2014: Researcher, CR1 CNRS in Dr T. Strick laboratory (Biomolecule nanomanipulation, Institut Jacques Monod).

2005-2010: Research Associate in Pr M. Buck laboratory (Division of Biology, Imperial College London)

2001-2004: Ph.D. thesis in Biochemistry. PhD advisor: Dr E. Richet, in AP Pugsley laboratory (Molecular Genetics Unit, Institut Pasteur Paris).

 

Unlocking the Molecular Motors of Life: The Mechanics of AAA+ Proteins

At the heart of every living cell, microscopic molecular motors work tirelessly to maintain life. Among them, the AAA+ ATPase family plays a universal role: they convert chemical energy (ATP hydrolysis) into mechanical force to remodel specific cellular substrate. From activating gene transcription to degrading proteins or reshaping the cellular cytoskeleton, nature uses this single structural engine to drive incredibly versatile activities.

Our research aims to understand the conserved features of this molecular engine. Specifically, we want to decipher how the AAA+ core transmits its energy to various cellular targets, and why specific mutations within this core are increasingly linked to human diseases including cancer and neurodegenerative disorders.

Katanin: Our Model System to Study Cellular Remodeling

To decode these mechanisms, we are focusing on a critical cellular process: the severing of microtubules. Microtubules are dynamic polymers that form the cell’s structural skeleton, playing a central role in cell division, morphogenesis, and intracellular signaling.

While most regulatory proteins only act at the tips of microtubules, a unique class of enzymes—Fidgetin, Spastin, and Katanin—interacts directly with the microtubule lattice to sever it throughout its length, precisely controlling its size, density and organization. Despite their importance, how these enzymes physically sever microtubules and how they are regulated in space and time remains poorly understood.

Current Research Focus

Combining biochemistry, genetics, and live-cell imaging, we use the microtubule-severing enzyme Katanin in the model organism C. elegans to address three key questions:

  • The Mechanism of Severing: How does Katanin utilize its AAA+ domain to disrupt the microtubule lattice?
  • Spatiotemporal Regulation: How is Katanin-mediated severing precisely controlled in space and time during development?
  • Cellular Impact: What is the exact role of microtubule-severing in female meiotic spindle assembly?

 

2026 – 2027: Grant Fondation ARC (2x35k€), France.

2024 – 2025 : Grant « IDEX AAP Emergence » Université Paris Cité 34.4k€, France.

2023 – 2024: Grant Fondation ARC (2x25k€), France.

2019 – 2022: Grant IDEX AAP Dynamique (3x15k€), France.

2017 – 2018: Grant Fondation ARC (2x25k€), France.

 

  • Jegou & G. Romet-Lemonne, H. Wioland, C. Leduc (Regulation of Actin Assembly Dynamics, IJM, Paris)
  • Minc, J. Sallé (Cellular Spatial Organisation, IJM, Paris)
  • De Beco, B. Ladoux & RM.Mège (Cell Adhesion and Mechanics, IJM, Paris)
  • Léon, M. Sanial (Membrane Trafficking, Ubiquitin and Signalling, IJM, Paris)
  • Dessauge (Physiologie, Environnement et Génétique pour l’Animal et les Systèmes d’Elevage » (PEGASE), INRAE, Rennes)
  • Gibeaux, D. Chrétien (Microtubules, de la tubuline aux fuseaux” (MiToS), IGDR, Rennes)
  • Grange (Ultrafast Optics and Nanophotonics (DON), IPCMS, Strasbourg)

 

Doctorat

  • Eva Beaumale (Master2 2018 & doctorat 2019-2022)
  • Nan Zhang (2007–2010)

Master 2

  • Navjyot Sangha (2008)
  • Selena Yan (2008)
  • Marta Carrara (2009)
  • Grégoire Mathonnet (2017)
  • Ludivine Roumbo (2022)
  • Aurélie Degenève (2023)
  • Lola Tanneur (2024)
  • Manlin Xu (2025)
  • Cecelia Westwood (2026)

Master 1 / Licence / Bachelor / Undergraduate

  • Winsome Cheung (2005)
  • Marine Parant (2007)
  • Abhay Kotecha (2008)
  • Lap Hang Chung (2008)
  • Antoine Richardot (2012)
  • Danaé David (2013)
  • Emna M’zah (2014)
  • Abir Elfarkouchi (2021)
  • Elodie Croizier (2023)
  • Lucie Pereira (2024)
  • Selma Aichour (2024)
  • Louise Descamps (2025)
  • Claudia Hayon Garcia (2026)

BTS

  • Eleonore Manso (2011)
  • Caroline Barbier (2016)
  • Laura Martin (2017)
  • Camille Aubry (2018)
  • Andréa Berne (2019)
  • Maëlann Chauvin (2020)
  • Emma Marchand (2021)
  • Yasmine El Ayachi (2022)
  • Eliott Bervelt (2022)
  • Fiona Leveau (2023)
  • Albane Thibault (2024)
  • Marwan Kebaili (2025)
  • Yasmine Ben Habhab (2026)

 

  1. Michail C, Berthelet J, Mechaly AE, Bui LC, Yang H, Cai D, Al Mahi A, Xie A, Bisio V, Sirri V, Dupret JM, Guidez F, Xu X, Joly N, Regad L, Viguier M, Deshayes F, Dulphy N, Green MR, Haouz A, Rodrigues Lima F. The SETD2 L1609P mutation found in leukemia disrupts methyltransferase activity and reduces histone H3K36 trimethylation. J Biol Chem. 2026 Feb 5;302(3):111259. doi: 10.1016/j.jbc.2026.111259. Epub ahead of print. PMID: 41654133.
  2. Joly N@, Pintard L. Intramolecular regulation of the MT-severing enzyme Katanin prevents futile ATP hydrolysis. J Cell Biol. 2026 Feb 2;225(2):e202506192. doi: 10.1083/jcb.202506192. Epub 2025 Nov 19. PMID: 41258800 (@ corresponding author)
  3. Pillan A, Ormancey P, Ben Choug C, Orlicky S, Tavernier N, Van Hove L, Ossareh-Nazari B, Joly N, Sicheri F, Lorca T, Pintard L. Molecular basis for the activation of Aurora A and Plk1 kinases during mitotic entry. EMBO J. 2026 Jan 28. doi: 10.1038/s44318-025-00679-8. PMID: 41606196
  4. Roumbo L, Ossareh-Nazari B, Vigneron S, Stefani I, Van Hove L, Legros V, Chevreux G, Lacroix B, Castro A, Joly N, Lorca T, Pintard L. (2025) The MAST kinase KIN-4 carries out mitotic entry functions of Greatwall in C. elegans EMBO J. 2025 Apr;44(7):1943-1974. doi: 10.1038/s44318-025-00364-w. Epub 2025 Feb 17. PMID: 39962268
  5. Sanial M, Miled R, Alves M, Claret S, Joly N, Proux-Gillardeaux V, Plessis A, Léon S. (2025) Direct observation of fluorescent proteins in gels: a rapid cost-efficient, and quantitative alternative to immunoblotting Biol Cell. 2025 Feb;117(2):e2400161. doi: 10.1111/boc.202400161. PMID: 39924827
  6. Strzelecki P*, Joly N*, Hébraud P, Hoffmann E, Cech GM, Kloska A, Busi F, Grange W. (2024) Enhanced Golden Gate Assembly: evaluating overhang strength for improved ligation efficiency Nucleic Acids Res. 2024 Oct 28;52(19):e95. doi: 10.1093/nar/gkae809. PMID: 39340302 (*co-first author)
  7. Beaumale E, Van Hove L, Pintard L, Joly N@ (2024) Microtubule-Binding Domains in Katanin p80 subunit are essential for severing activity in C. elegans. J Cell Biol. 2024 Apr 1;223(4):e202308023. doi: 10.1083/jcb.202308023. Epub 2024 Feb 8. PMID: 38329452 (@ corresponding author)
  8. Velez-Aguilera G, Ossareh-Nazari B, Van Hove L, Joly N, Pintard L. (2022) Cortical microtubule pulling forces contribute to the union of the parental genomes in the C. elegans zygote. Elife. 2022 Mar 8;11:e75382. doi: 10.7554/eLife.75382. PMID: 35259092
  9. Knox J, Joly N, Linossi EM, Carmona-Negrón JA, Jura N, Pintard L, Zuercher W, Roy PJ. (2021) A survey of the kinome pharmacopeia reveals multiple scaffolds and targets for the development of novel anthelmintics. Sci Rep. 2021 Apr 28;11(1):9161. doi: 10.1038/s41598-021-88150-6. PMID: 33911106
  10. Tavernier N, Thomas Y, Vigneron S, Maisonneuve P, Orlicky S, Mader P, Regmi SG, Van Hove L, Levinson NM, Gasmi-Seabrook G, Joly N, Poteau M, Velez-Aguilera G, Gavet O, Castro A, Dasso M, Lorca T, Sicheri F* and Pintard L* (2021) Bora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry. Nat Commun. 2021 Mar 26;12(1):1899. doi: 10.1038/s41467-021-21922-w. PMID: 33771996
  11. Velez-Aguilera G, Nkombo Nkoula S, Ossareh-Nazari B, Link J, Paouneskou D, Van Hove L, Joly N, Tavernier N, Verbavatz JM, Jantsch V, Pintard L. (2020) PLK-1 promotes the merger of the parental genome into a single nucleus by triggering lamina disassembly. Elife. 2020 Oct 8;9:e59510. doi: 10.7554/eLife.59510. PMID: 33030429
  12. Joly N#, Beaumale E, Martino L, Van Hove L, Pintard L#. (2020) Phosphorylation of the Microtubule-Severing AAA+ Enzyme Katanin regulates C. elegans embryo development. J Cell Biol. 2020 Jun 1;219(6):e201912037. doi: 10.1083/jcb.201912037.PMID: 32412594 (# co-corresponding authors)
  13. Martino L, Morchoisne-Bolhy S, Cheerambathur DK, Van Hove L, Dumont J, Joly N, Desai A, Doye V, Pintard L. (2017) Channel Nucleoporins Recruit PLK-1 to Nuclear Pore Complexes to Direct Nuclear Envelope Breakdown in C. elegans. Dev Cell. 2017 Oct 23;43(2):157-171.e7. doi: 10.1016/j.devcel.2017.09.019. PMID: 29065307.
  14. Richarme G, Liu C, Mihoub M, Abdallah J, Leger T, Joly N, Liebart JC, Jurkunas UV, Nadal M, Bouloc P, Dairou J, Lamouri A. (2017) Guanine glycation repair by DJ-1/Park7 and its bacterial homologs. Science. 2017 Jul 14;357(6347):208-211. PMID: 28596309.
  15. Joly N#, Martino L, Gigant E, Dumont J, Pintard L#. (2016) Microtubule-severing activity of AAA-ATPase Katanin is essential for female meiotic spindle assembly. Development. 143(19):3604-3614. (# co-corresponding authors).
  16. Thomas Y, Cirillo L, Panbianco C, Martino L, Tavernier N, Schwager F, Van Hove L, Joly N, Santamaria A, Pintard L, Gotta M.. (2016) Cdk1 Phosphorylates SPAT-1/Bora to Promote Plk1 Activation in C. elegans and Human Cells. Cell Rep. 15(3):510-8.
  17. Buck M, Engl C, Joly N, Jovanovic G, Jovanovic M, Lawton E, McDonald C, Schumacher J, Waite C, Zhang N. (2015) In vitro and in vivo methodologies for studying the sigma 54-dependent transcription. Methods Mol Biol. 1276:53-79.
  18. Darbari VC, Lawton E, Lu D, Burrows PC, Wiesler S, Joly N, Zhang N, Zhang X, Buck M. (2014) Molecular basis of nucleotide-dependent substrate engagement and remodeling by an AAA+ activator. Nucleic Acids Res 42(14):9249-61.
  19. Lawton E, Jovanovic M, Joly N, Waite C, Zhang N, Wang B, Burrows P, Buck M. (2014) Determination of the self-association residues within a Homomeric and a Heteromeric AAA+Enhancer Binding Protein. J Mol Biol 426(8): 1692-710.
  20. Zhang N, Gordiyenko Y, Joly N, Lawton E, Robinson CV, Buck M. (2014) Subunit dynamics and nucleotide-dependent asymmetry of an AAA+ transcription complex. J. Mol. Biol. 426(1):71-83.
  21. Monnet J, Grange W, Strick TR#, Joly N#. (2013) Mfd as a central partner of transcription coupled repair. Transcription. 4(3). (# co-corresponding authors)
  22. Zhang N, Simpson T, Lawton E, Uzdavinys P, Joly N, Burrows P, Buck M. (2013) A key hydrophobic patch identified in an AAA⁺ protein essential for its in trans inhibitory regulation. J. Mol. Biol. 425(15):2656-69.
  23. Howan K., Smith A.J., Westblade L.F., Joly N., Grange W., Zorman S., Darst S.A., Savery N.J. Strick T.R. (2012) Initiation of transcription-coupled repair characterized at single-molecule resolution. Nature. 490(7420):431-4.
  24. Joly N#, Zhang N, Buck M#. (2012) ATPase Site Architecture Is Required for Self-Assembly and Remodeling Activity of a Hexameric AAA+ Transcriptional Activator. Mol Cell. 47(3):484-90. (# co-corresponding authors).
  25. Zhang N, Joly N#, Buck M#. (2012) A common feature from different subunits of a homomeric AAA+ protein contacts three spatially distinct transcription elements. Nucleic Acids Res. 40(18):9139-52. (# co-corresponding authors).
  26. Richet E., Davidson AL. Joly N. (2012) The ABC transporter MalFGK(2) sequesters the MalT transcription factor at the membrane in the absence of cognate substrate. Mol. Micro. 85(4):632-47.
  27. Joly N. Zhang N, Buck M, Zhang X. (2012) Coupling AAA protein function to regulated gene expression. Biochim Biophys Acta. 1823(1):108-16. (review)
  28. Wang B, Kitney RI, Joly N, Buck M. (2011) Engineering modular and orthogonal genetic logic gates for robust digital-like synthetic biology. Nat Commun. 2:508. doi: 10.1038/ncomms1516.
  29. Joly N.# and Buck M.# (2011) Single chain forms of the enhancer binding protein PspF provide insights into geometric requirements for gene activation. J Biol Chem. 286(14):12734-42. (# co-corresponding authors).
  30. Joly N, Engl C, Jovanovic G, Huvet M, Toni T, Sheng X, Stumpf MP, Buck M. (2010) Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology. FEMS Microbiol Rev. 34(5):797-827. Review.
  31. Burrows PC, Joly N, Buck M. (2010) A prehydrolysis state of an AAA+ ATPase supports transcription activation of an enhancer-dependent RNA polymerase. Proc Natl Acad Sci U S A. 107(20):9376-81.
  32. Joly N.# and Buck M.# (2010) Engineered interfaces of an AAA+ ATPase reveal a new nucleotide-dependent coordination mechanism. J Biol Chem. 285(20):15178-86. (# co-corresponding authors)
  33. Joly N.; Burrows PC; Eng C, Jovanovic G.; Buck M. (2009) A lower order form of the phage shock protein A stably associates with the hexameric AAA+ transcription activator protein PspF for negative regulation. J. Mol. Biol. 394(4), 764-775.
  34. Zhang N.; Joly N.#; Burrows PC; Jovanovic M; Wigneshweraraj S.; Buck M.# (2009) The role of the conserved phenylalanine in the σ54-interacting GAFTGA motif of bacterial Enhancer Binding Proteins. Nucleic Acids Res.; 37(18), 5981-5992. (# co-corresponding authors)
  35. Burrows P.C., Joly N., Nixon B.T., Buck M. (2009) Comparative Analysis of activator-E54 complexes formed with Nucleotide-metal fluoride analogues Nucleic Acids Res.; 37(15), 5138-5150.
  36. Burrows P.C., Joly N., Cannon W.V., Camara B.P., Rappas M., Zhang X., Dawes K., Nixon B.T., Wigneshweraraj S.R., Buck M., (2009) Coupling sigma factor conformation to RNA polymerase reorganisation for DNA melting. J. Mol. Biol.; 387, 306-319.
  37. Burrows PC, Wigneshweraraj S, Bose D, Joly N, Schumacher J, Rappas M, Pape T, Stockley PG, Zhang X, Buck M. (2008) Visualizing the organization and reorganization of transcription complexes for gene expression. Biochem Soc Trans; 36(Pt 4):776-9. (review)
  38. Schumacher, J. Joly N., Leoz Claeys-Bouuaert I., Abdul Aziz S., Rappas M., Zhang X., Buck M. (2008) Mechanism of homotropic control to coordinate hydrolysis in a Hexameric AAA+ ring ATPase. J. Mol. Biol. 381(1):1-12.
  39. Joly N., Burrows P.C. and Buck M. (2008) An intra-molecular route for coupling ATPase activity in AAA+ proteins for transcription activation. J Biol Chem. 283(20):13725-35.
  40. Wigneshweraraj SR, Bose D, Burrows PC, Joly N, Schumacher J, Rappas M, Pape T, Zhang X, Stockley P, Severinov K and Buck M. (2008) Modus operandi of the bacterial RNA polymerase containing the σ54 promoter-specificity factor. Mol. Micro. 68(3):538-46. (review)
  41. D. Bose, N. Joly, T. Pape, M. Rappas, J. Schumacher, M. Buck and X. Zhang. (2008). Dissecting the ATP hydrolysis pathway of bacterial enhancer-binding proteins. Biochem Soc Trans. 36(1):83-8. (review)
  42. Joly N.*, Rappas M.*, Buck M., Zhang X. (2008). Trapping of stable transcription intermediates using a new ATP analogue: AMP Aluminium Fluoride. J. Mol. Biol. 375(5):1206-11. (*contributed equally to this work)
  43. Joly N., Rappas M., Wigneshweraraj SR., Zhang X., Buck M. (2007). Coupling nucleotide hydrolysis to transcription activation performance in a bacterial Enhancer Binding Protein. Mol. Micro. 66(3):583-595.
  44. Schumacher J., Joly N., Rappas M., Bradley D., Wigneshweraraj SR., Zhang X., Buck M. (2007) Sensor I threonine of the AAA+ ATPase transcriptional activator PspF involved in coupling hydrolysis to restructure the σ54-RNA polymerase. J Biol Chem. 282(13):9825-33.
  45. Joly N, Schumacher J and Buck M. (2006) Heterogeneous nucleotide occupancy stimulates functionality of PspF, an AAA+ transcriptional activator. J Biol Chem. 281:34997-5007.
  46. M Buck, D Bose, P Burrows, W Cannon, N Joly, T Pape, M Rappas, J Schumacher, S Wigneshweraraj, X Zhang. (2006) A Second Paradigm for Gene Activation in Bacteria. Biochem Soc Trans. 34(Pt 6):1067-71. (review)
  47. Schumacher J, Joly N, Rappas M, Zhang X, Buck M. (2006) Structures and organisation of AAA+ enhancer binding proteins in transcriptional activation. J Struct Biol. 156(1):190-9. (review)
  48. Richet E, Joly N and Danot O. (2005) Two Domains of MalT, the Activator of the Escherichia coli Maltose Regulon, Bear Determinants Essential for Anti-activation by MalK. J. Mol. Biol 18;347(1):1-10.
  49. Joly N, Böhm A, Boos W and Richet E. (2004). MalK, the ABC component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator MalT by antagonizing inducer binding. J Biol Chem. 279:33123-30.
  50. Joly N, Danot O, Schlegel A, Boos W, Richet E. (2002). The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon. J Biol Chem. 277:16606-13.