• E-mail :[email]
  • Phone : 673357038
  • Location : 21000, France
Last update 2022-02-21 17:15:10.063

Laurence Dubrez PhD biochemistry, cell biology

Course and current status


  • 1996 PhD in Molecular and cellular Biology, Université of Burgundy, Dijon, France
  • 2010: HDR (habilitation à diriger des recherches), University of Bungundy, Dijon, France

Research experience:

  • 1993-1996 PhD studies: Cancer biology and therapy Department, Inserm CJF 94-04 – Dijon,France
  • 1997-1998: Postdoctoral fellow, Molecular and Cellular pharmacology department - School ofBiological Sciences - Manchester, GB
  • 1998-2000: Postdoctorl fellow, Bases moléculaires de l'initiation et de la progression descancers du poumon - INSERM E9924 - Institut Albert Bonniot – Grenoble, France
  • 2001-2004: Postdoctorl fellow, Cell Death and Cancer, INSERM U517 – Dijon, France
  • 2004-2006: Inserm Researcher, PI “IAP project“ - Cell Death and Cancer, INSERM U517 –Dijon, France
  • Since 2007: Inserm researcher, PI “IAP project“ - Research Center LNC (Lipides, Nutrition,Cancer) – Inserm/University of Burgundy, Dijon, France

Scientific summary

IAPs (inhibitors of apoptosis) constitute an evolutionary conserved family of proteins, discovered in baculovirus as potent inhibitors of apoptosis in infected insect cells.

Beside apoptosis regulation, most of them also display non-apoptotic functions in innate immunity, inflammatory response, cell proliferation, cell division and cell motility. Human genome encodes 8 IAPs including cIAP1 (cellular IAP1), cIAP2 and XIAP (X-linked IAP) that display structural and functional homology.

Among IAPs, cIAP1 is an E3-ubiquitin ligase with oncogenic properties. It is highly expressed in number of cancer samples and its expression has been correlated with poor prognosis or low response to anti-cancer therapy. cIAP1 is an important regulator of signaling pathways activated by membrane receptor such as the Tumor Necrosis Factor (TNF) receptor superfamily members. It controles NF-κB and MAPK activation while it represses cell death signaling platform assembly. 

We previously demonstrated that cIAP1 is detected in the nucleus of undifferentiated and tumor cells (Plenchette et al. Blood 2004; Didelot et al. Cell Death Differ. 2008; Dupoux et al. Blood 2009; Cartier et al. J. Biol. Chem. 2011). The nuclear expression of cIAP1 has been associated with advanced disease stages suggesting that the nuclear function of cIAP1 could account for its oncogenic properties. 

Our goals were to identify the nuclear functions of cIAP1 and to determine the importance of these functions in oncogenic activity of cIAP1. We demonstrated the capacity of cIAP1 to control the activity of E2F1 transcription factor (Cartier et al. J. Biol. Chem. 2011; Glorian et al. Cell Death Dis. 2017)

Our project is

  • To identify new nuclear partners of cIAP1
  • To analyze the role of cIAP1 in the regulation of E2F1 transcription factor
  • To analyze the oncogenic activity of cIAP1
Image d’exemple