Pierre Lutz
  • E-mail :[email]
  • Phone : +33 5 61 17 54 71
  • Location : Toulouse, France
Last update 2019-01-25 09:17:06.741

Pierre Lutz PhD Molecular and Cellular Biology

Course and current status

CIVIL STATUS

 Name: Pierre G. Lutz

Date of birth: October 3rd, 1967

Nationality: French

Familial status:  Married, 2 children

Laboratory:  Institut de Pharmacologie et de Biologie Structurale, CNRS UMR 5089, 205 Route de Narbonne, BP 64182, F-31077 Toulouse, France

Phone:   + 33 (0) 5 61 17 54 71               Fax: + 33 (0) 5 61 17 59 94

e-mail:    Pierre.Lutz@ipbs.fr

http://www.ipbs.fr

https://twitter.com/PierreGLutz

DEGREES AND DIPLOMA

2003:Habilitation à diriger des recherches, Paris VII University.

1992-1996: PhD, Molecular Biology, obtained with highest honors (supervisor Prof. Claude Kedinger). Louis Pasteur University, Strasbourg.

IGBMC, director Prof. Pierre Chambon, Illkirch (France).

1991: Agrégation de Biochimie-Génie Biologique

ADDITIONAL TRAINING

Jan.-July 2005: Group leader, "Targeting of proteins to proteasome in cell differentiation", Institut Cochin, INSERM U567, CNRS UMR8104, Univ. R. Descartes, Paris (France), director Prof. Axel Kahn.

2002-2004: Group leader, "Cell signaling in normal and leukemia myelopoiesis", INSERM U417, Paris (France), director Prof. Yvon E. Cayre.

1996-2000: Post-doctoral fellow, INSERM U417, Paris (France), director Prof. Yvon E. Cayre.

1992: Scientifique du Contingent (French military duties), INSERM U338, Strasbourg (France), director Dr. Dominique Aunis.

CURRENT POSITION

CNRS, Directeur de Recherche 2ème classe (since October 2009)

Group leader "Ubiquitin Enzymes in Health & Disease" (since August 2005), Institute of Pharmacology and Structural Biology, Cancer Biology Department, UMR 5089, CNRS/University of Toulouse, Toulouse (France), director Dr. Jean-Philippe Girard.

DISTINCTIONS/MEMBERSHIPS

International member of the American Society of Hematology, Member of the European Hematology Association, Member of the American Society of Biochemistry and Molecular Biology, Membre de la Société Française de Biochimie et de Biologie Moléculaire, Membre de la Société de Biologie Cellulaire de France.

PEER-REVIEWED PUBLICATIONS

Métais, A., Lamsoul, I., Melet, A., Uttenweiler-Joseph, S., Poincloux, R., Stefanovic, S., Valière, A., Gonzalez de Peredo, A., Stella, A., Burlet-Schiltz, O., Zaffran, S., Lutz, P.G.* and Moog-Lutz, C.* (2018) The Asb2α-Filamin A axis is essential for cytoskeletal remodeling during heart development. Circulation Research. 122: e34 (*: contributed equally to the work)

Spinner, C.A., Uttenweiler-Joseph, S., Métais, A., Stella, A., Burlet-Schiltz, O., Moog-Lutz, C. Lamsoul, I., and Lutz, P.G. (2015) Substrates of the ASB2α E3 ubiquitin ligase in dendritic cells. Scientific Reports, 5: 16269.

Lamsoul, I., Uttenweiler-Joseph, S., Moog-Lutz, C. and Lutz, P.G. Cullin 5-RING E3 ubiquitin Ligases, new therapeutic targets? Biochimie. pii: S0300-9084(15)00250-3. doi: 10.1016/j.biochi.

Zakaria, R., Lamsoul, I., Uttenweiler-Joseph, S., Erard, M., Monsarrat, B., Burlet-Schiltz, O., Moog-Lutz, C. and Lutz, P.G. (2013) Phosphorylation of serine 323 of ASB2α is pivotal for the targeting of filamin A to degradation, Cellular Signalling, 25: 2823-2830.

Lamsoul, I., Métais, A., Gouot, E., Heuzé, M.L., Lennon-Duménil, A.M., Moog-Lutz, C. and Lutz, P.G. (2013) ASB2α regulates migration of immature dendritic cells. Blood, 122: 533-541.

Uttenweiler-Joseph, S., Bouyssié, D., Calligaris, D., Lutz, P.G., Monsarrat, B. and Burlet-Schiltz, O. (2013) Quantitative proteomic analysis to decipher the differential apoptotic response of bortezomib-treated acute promyelocytic leukemia cells before and after retinoic acid-differentiation reveals an involvement of protein toxicity mechanisms. Proteomics, 13:37-47.

Lamsoul, I., Erard, M., van der Ven, P.F.M. and Lutz, P.G. (2012) Filamins but not Janus Kinases are substrates of the ASB2α Cullin-Ring E3 ubiquitin ligase in hematopoietic cells. PLoS ONE, 7: e43798.

Guiet, R., Verollet, C., Lamsoul, I., Cougoule, C., Poincloux, R., Labrousse, A., Calderwood, D.A., Glogauer, M., Lutz, P.G. and Maridonneau-Parini, I. (2012) Macrophage mesenchymal migration requires podosome stabilization by Filamin A. The Journal of Biological Chemistry. 287:13051-13062.

Lamsoul, I., Burande, C.F., Razinia, Z., Houles, T.C., Menoret, D., Baldassarre, M., Erard, M., Moog-Lutz, C., Calderwood, D.A., and Lutz, P.G. (2011) Functional and structural insights into ASB2α, a novel regulator of integrin-dependent adhesion of hematopoietic cells. The Journal of Biological Chemistry, 286: 30571-30581.

Razinia, Z., Baldassarre, M., Bouaouina, M., Lamsoul, I., Lutz, P.G. and Calderwood, D.A. (2011) The E3 ubiquitin ligase specificity subunit ASB2α targets filamins to proteasomal degradation by interacting with the filamin actin binding domain. Journal of Cell Science, 124: 2631-2642.

Baldassare, M., Razinia, Z., Burande, C.F., Lamsoul, I., Lutz, P.G., and Calderwood, D.A. (2009) Filamins regulate cell spreading and initiation of migration. PLoS ONE, 4(11):e7830.

Burande, C.F., Heuzé, M.L., Lamsoul, I., Monsarrat, B., Uttenweiler-Joseph, S., and Lutz, P.G. (2009) A label-free quantitative proteomic strategy to identify E3 ubiquitin ligase substrates targeted to proteasome degradation. Molecular & Cellular Proteomics, 8: 1719-1727.

Bello, N.F.*, Lamsoul, I.*, Heuzé, M.L., Métais, A., Moreaux, G., Duprez, D., Calderwood, D.A., Moog-Lutz, C., and Lutz P.G. (2009) The E3 ubiquitin ligase specificity subunit ASB2β is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradation. Cell Death & Differentiation, 16: 921-932. *Contributed equally to the work.

Luissint, A.C., Lutz, P.G., Calderwood, D.A., Couraud, P.O., and Bourdoulous, S. (2008)  JAM-L mediated leukocyte adhesion to endothelial cells is regulated in cis by α4β1 integrin activation. The Journal of Cell Biology, 183: 1159-1173.

Heuzé, M.L.*, Lamsoul, I.*, Baldassarre, M., Lad, Y., Lévêque, S., Razinia, Z., Moog-Lutz, C., Calderwood, D.A., and Lutz, P.G. (2008) ASB2 targets filamins A and B to proteasomal degradation. Blood, 112: 5130-5140. * Contributed equally to the work.

Heuzé, M. L., Lamsoul, I., Moog-Lutz, C. and Lutz, P. G. (2008). Ubiquitin-mediated proteasomal degradation in normal and malignant hematopoiesis. Blood Cells, Molecules & Diseases, 40: 200-210.

Denis, F.M., Benecke, A., Di Gioia, Y., Touw, I.P., Cayre, Y.E., and Lutz, P.G. (2005). PRAM-1 potentiates arsenic trioxide-induced JNK activation. The Journal of Biological Chemistry, 280: 9043-9048.

Heuzé, M.L., Guibal, F.C., Banks, C.A., Conaway, J.W., Conaway, R.C., Cayre, Y.E., Benecke, A., and Lutz, P.G. (2005). ASB2 is an elongin BC-interacting protein that can assemble with cullin 5 and rbx1 to reconstitute an E3 ubiquitin ligase complex. The Journal of Biological Chemistry, 280: 5468-5474.

Moog-Lutz, C., Cavé-Riant, F., Guibal, F.C., Breau, M.A., Di Gioia, Y., Couraud, P.O., Cayre, Y.E., Bourdoulous, S., and Lutz, P.G. (2003). JAML, a novel protein with characteristics of a Junctional Adhesion Molecule, is induced during differentiation of myeloid leukemia cells. Blood, 102: 3371-3378.

Rosa-Calatrava, M., Puvion-Dutilleul, F., Lutz, P., Dreyer, D., De Thé, H., Chatton, B., and Kedinger, C. (2003). Adenovirus protein IX sequesters host-cell promyelocytic leukaemia protein and contributes to efficient viral proliferation. EMBO Reports, 4: 969-975.

Lutz, P. G., Moog-Lutz, C., and Cayre, Y.E. (2002). Signaling revisited in acute promyelocytic leukemia. Leukemia, 16: 1933-1939.

Guibal, F.C., Moog-Lutz, C., Smolewski, P., Di Gioia, Y., Darzynkiewicz, Z., Lutz, P.G., and Cayre, Y.E. (2002). ASB-2 inhibits growth and promotes commitment in myeloid leukemia cells. The Journal of Biological Chemistry, 277: 218-224.

Esteve, L., Lutz, P., Thiriet, N., Revel, M-O., Aunis, D., and Zwiller, J. (2001). Cyclic GMP-dependent protein kinase potentiates serotonin-induced Egr-1 binding activity in PC12 cells. Cellular Signaling, 13: 425-432.

Moog-Lutz, C.*, Peterson, E.J.*, Lutz, P.G.*, Eliason, S., Cavé-Riant, F., Singer, A., Di Gioia, Y., Dmowski, S., Kamens, J., Cayre, Y.E., and Koretzky, G. (2001). PRAM-1 is a novel adaptor protein regulated by retinoic acid (RA) and promyelocytic leukemia (PML)-RA receptor α in acute promyelocytic leukemia cells. The Journal of Biological Chemistry 276: 22375-22381. * Contributed equally to the work.

Lutz, P.G., Houzel-Charavel, A., Moog-Lutz, C., and Cayre, Y.E. (2001). Myeloblastin is a Myb target gene; mechanisms of regulation by retinoic acid in myeloid leukemia cells. Blood 97:2449-2456.

Lutz, P.G., Moog-Lutz, C., Coumau-Gatbois, E., Kobari, L., Di Gioia, Y., and Cayre Y.E. (2000). Myeloblastin is a granulocyte colony-stimulating factor responsive gene conferring factor-independent growth to hematopoietic cells. Proceedings of the National Academy of Sciences, USA. 15: 1601-1606.

Lutz, P., Rosa-Calatrava, M., and Kedinger, C. (1997). The product of the adenovirus intermediate gene IX is a transcriptional activator. Journal of Virology 71:5102-5109.

Gustin, K., Lutz, P., and Imperiale, M.J. (1996). Interaction of the adenovirus L1 52/55-kilodalton protein with the IVa2 gene product during infection. Journal of Virology 70:6463-6467.

Lutz P., Puvion-Dutilleul, F., Lutz,Y., and Kedinger, C. (1996). Nucleoplasmic and nucleolar distribution of the adenovirus IVa2 gene product. Journal of Virology 70:3449-3460.

Lutz, P., and Kedinger, C. (1996). Properties of the adenovirus IVa2 gene product, an effector of late-phase-dependent activation of the major late promoter. Journal of Virology 70:1396-1405.

Tribouley, C., Lutz P., Staub, A. and Kedinger, C. (1994). The product of the adenovirus intermediate gene IVa2 is a transcriptional activator of the major late promoter. Journal of Virology 68:4450-4457.

Scientific summary

Ubiquitylation is a rapid, reversible and versatile post-translational modification, directing proteins to a myriad of fates. A key regulatory step of the ubiquitylation cascade is dictated by the E3 ubiquitin ligase which confers substrate selectivity. The reversibility of this post-translational modification is driven by deubiquitinating enzymes responsible for removing ubiquitin conjugates from substrates. While best known for targeting proteins to proteasomal degradation, ubiquitylation is also used for proteolytic-independent functions. Of note, alteration of the ubiquitin pathway results in human disease pathogenesis including cancer, muscle disorders or inflammatory and infectious diseases. Importantly, components of the ubiquitin system are amenable to pharmacological manipulation.

A main objective of our team is to decipher the roles of the ASB2 E3 ubiquitin ligases in physiological and pathological settings using state-of-the-art mouse mutant models as well as cellular and molecular approaches. The ASB2 gene was initially identified by our group as a retinoic acid-responsive gene deregulated by the PML-RARα oncogenic protein in leukemia cells. ASB2 encodes two protein isoforms, ASB2α and ASB2β, that are the specificity subunits of Cullin 5-RING E3 ubiquitin ligases suggesting that ASB2 proteins exert their effects through the targeting of specific substrates for degradation by the proteasome. Investigating ASB2-ASB2 substrate axes will provide important mechanistic insights into the contribution of the ubiquitin pathway to major biological functions that could be exploited in therapeutic purposes.

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