Francoise Degoul

Dr. Francoise Degoul

orcid

Research Focus & Metrics

Academic Career Length

38Years (1989-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 April 1998 in Nucleic Acids Research
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Journal Article
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Mark HelmMark Helm
Mark Helm
HBHervé Brulé
Hervé Brulé
FDFrancoise Degoul
Francoise Degoul
CCClaude Cepanec
Claude Cepanec
JLJean-Paul Leroux
Jean-Paul Leroux
CFCatherine Florentz
Catherine Florentz
Direct sequencing of human mitochondrial tRNALys shows the absence of editing and the occurrence of six modified nucleotides (m1A9, m2G10, Ψ27, Ψ28 and hypermodified nucleotides at positions U34 and A37). This tRNA folds into the expected cloverleaf, as confirmed by structural probing with nucleases. The solution structure of the corresponding in vitro transcript unexpectedly does not fold into a cloverleaf but into an extended bulged hairpin. This non-canonical fold, established according to the reactivity to a large set of chemical and enzymatic probes, includes a 10 bp aminoacyl acceptor stem (the canonical 7 bp and 3 new pairs between residues 8–10 and 65–63), a 13 nt large loop and an anticodon-like domain. It is concluded that modified nucleotides have a predominant role in canonical folding of human mitochondrial tRNALys. Phylogenetic comparisons as well as structural probing of selected in vitro transcribed variants argue in favor of a major contribution of m1A9 in this process.

1 May 2005 in Pharmacogenetics and Genomics
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Journal Article
Closed access
ASAngela Sutton
Angela Sutton
AIAudrey Imbert
Audrey Imbert
AIAnissa Igoudjil
Anissa Igoudjil
VDVéronique Descatoire
Véronique Descatoire
SCSophie Cazanave
Sophie Cazanave
FDFrancoise Degoul
Francoise Degoul
A genetic dimorphism incorporates either alanine (Ala) or valine (Val) in the mitochondrial targeting sequence (MTS) of manganese superoxide dismutase (MnSOD). The Ala-MTS confers a 40% higher MnSOD activity than the Val-MTS after import into isolated mitochondria in vitro. The present study aimed to characterize functional consequences in whole cells. HuH7 human hepatoma cells were transfected with vectors encoding for the human Ala- or Val-MnSOD variants fused to a Myc-His-tag. The Ala-variant resulted in four-fold higher levels of the mature exogenous protein and MnSOD activity than the Val-variant. Studies with a proteasome inhibitor indicated that precursor proteins are either imported into the mitochondria or degraded by the proteasome. Despite identical levels 8 h after transfection, mRNA levels at 36 h were two-fold higher for the Ala-encoding mRNA than the Val-mRNA. Decreasing the mitochondrial membrane potential decreased both MnSOD mitochondrial import and its mRNA levels. Much larger differences in the activity of the human Val- and Ala-MnSOD variants are observed in whole cells rather than after import experiments performed in vitro. First, the slowly imported Val-MnSOD is degraded by the proteasome in cells. Second, the slower mitochondrial import of the Val-variant may be associated with decreased mRNA stability, possibly due to impaired cotranslational import.

1 March 2003
Verified
Journal Article
Closed access
ASAngela Sutton
Angela Sutton
HKHania Khoury
Hania Khoury
CPCarina Prip-Buus
Carina Prip-Buus
CCClaude Cepanec
Claude Cepanec
DPDominique Pessayre
Dominique Pessayre
FDFrancoise Degoul
Francoise Degoul
A genetic dimorphism encodes for either alanine (Ala) or valine (Val) in the mitochondrial targeting sequence (MTS) of human manganese superoxide dismutase (MnSOD) and has been reported to modulate the risk of some cancers, neurodegenerative diseases and severe alcoholic liver disease. Although functional consequences of this dimorphism on MnSOD activity have not been assessed, computer models predict a partial alpha-helix structure for the Ala-MnSOD/MTS, but a beta-sheet structure for the Val-variant, which could hamper mitochondrial import. To investigate this hypothesis, we studied the in-vitro import of chimaeric proteins composed of either one of the MnSOD/MTS fused to the mouse dihydrofolate reductase (DHFR) protein, and the import of the two human MnSOD precursor variants into rat liver mitochondria. Compared to Ala-proteins, the Val-MnSOD/MTS-DHFR precursor and Val-MnSOD precursor were both partly arrested within the inner mitochondrial membrane. The Ala-MnSOD precursor generated 30-40% more of the active, matricial, processed MnSOD homotetramer than the Val-MnSOD precursor. These results show that the Ala-MnSOD/MTS allows efficient MnSOD import into the mitochondrial matrix, while the Val-variant causes partial arrest of the precursor within the inner membrane and decreased formation of the active MnSOD tetramer in the mitochondrial matrix.

1 June 1991 in Annals of Neurology
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Journal Article
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CMChokri Mhiri
Chokri Mhiri
MBM. Baudrimont
M. Baudrimont
GBGisèle Bonne
Gisèle Bonne
CGC. Geny
C. Geny
FDFrancoise Degoul
Francoise Degoul
RGR. Gherardi
R. Gherardi

14 January 2016 in Clinical Science
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ZBZied Boudhraa
Zied Boudhraa
BBBernadette Bouchon
Bernadette Bouchon
CVClaire Viallard
Claire Viallard
MDMichel D'Incan
Michel D'Incan
FDFrancoise Degoul
Francoise Degoul
Annexin A1 (ANXA1) is a Ca2+-regulated phospholipid-binding protein involved in various cell processes. ANXA1 was initially widely studied in inflammation resolution, but its overexpression was later reported in a large number of cancers. Further in-depth investigations have revealed that this protein could have many roles in cancer progression and act at different levels (from cancer initiation to metastasis). This is partly due to the location of ANXA1 in different cell compartments. ANXA1 can be nuclear, cytoplasmic and/or membrane associated. This last location allows ANXA1 to be proteolytically cleaved and/or to become accessible to its cognate partners, the formyl-peptide receptors. Indeed, in some cancers, ANXA1 is found at the cell surface, where it stimulates formyl-peptide receptors to trigger oncogenic pathways. In the present review, we look at the different locations of ANXA1 and their association with the deregulated pathways often observed in cancers. We have specifically detailed the non-classic pathways of ANXA1 externalization, the significance of its cleavage and the role of the ANXA1–formyl-peptide receptor complex in cancer progression.

1 March 1998 in Journal of the Neurological Sciences
Verified
Journal Article
Closed access
EBEric Boitier
Eric Boitier
FDFrancoise Degoul
Francoise Degoul
IDIsabelle Desguerre
Isabelle Desguerre
CCChristiane Charpentier
Christiane Charpentier
DFDominique François
Dominique François
CMCécile Marsac
Cécile Marsac