Publications
2021
Nettersheim Jo-Ann, Janel-Bintz Régine, Kuhn Lauriane, Cordonnier Agnès M.
DNA polymerase η is a substrate for calpain: a possible mechanism for pol η retention in UV-induced replication foci Journal Article
In: Journal of Cell Science, vol. 134, no. 13, pp. jcs258637, 2021, ISSN: 1477-9137.
Abstract | Links | BibTeX | Tags: calpain, Calpain protease, CAPNS1, DNA Damage, DNA damage response, DNA polymerase η, DNA Repair, DNA Replication, DNA-Directed DNA Polymerase, PPSE, Replication foci, Translesion DNA synthesis
@article{nettersheim_dna_2021,
title = {DNA polymerase η is a substrate for calpain: a possible mechanism for pol η retention in UV-induced replication foci},
author = {Jo-Ann Nettersheim and Régine Janel-Bintz and Lauriane Kuhn and Agnès M. Cordonnier},
doi = {10.1242/jcs.258637},
issn = {1477-9137},
year = {2021},
date = {2021-07-01},
journal = {Journal of Cell Science},
volume = {134},
number = {13},
pages = {jcs258637},
abstract = {DNA polymerase η (pol η) is specifically required for translesion DNA synthesis across UV-induced DNA lesions. Recruitment of this error-prone DNA polymerase is tightly regulated during replication to avoid mutagenesis and perturbation of fork progression. Here, we report that pol η interacts with the calpain small subunit-1 (CAPNS1) in a yeast two-hybrid screening. This interaction is functional, as demonstrated by the ability of endogenous calpain to mediate calcium-dependent cleavage of pol η in cell-free extracts and in living cells treated with a calcium ionophore. The proteolysis of pol η was found to occur at position 465, leading to a catalytically active truncated protein containing the PCNA-interacting motif PIP1. Unexpectedly, cell treatment with the specific calpain inhibitor calpeptin resulted in a decreased extent of pol η foci after UV irradiation, indicating that calpain positively regulates pol η accumulation in replication foci.},
keywords = {calpain, Calpain protease, CAPNS1, DNA Damage, DNA damage response, DNA polymerase η, DNA Repair, DNA Replication, DNA-Directed DNA Polymerase, PPSE, Replication foci, Translesion DNA synthesis},
pubstate = {published},
tppubtype = {article}
}
2001
Georgel Philippe, Naitza S, Kappler Christine, Ferrandon Dominique, Zachary Daniel, Swimmer C, Kopczynski C, Duyk G, Reichhart Jean-Marc, Hoffmann Jules A
Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis Journal Article
In: Dev. Cell, vol. 1, no. 4, pp. 503–514, 2001, ISSN: 1534-5807.
Abstract | BibTeX | Tags: Animals, Anti-Infective Agents, Apoptosis, Bacterial Infections, Caspases, Chromosome Mapping, Cysteine Proteinase Inhibitors, DNA Damage, Female, ferrandon, Gene Expression, hoffmann, I-kappa B Kinase, Immunocompromised Host, In Situ Nick-End Labeling, Insect Proteins, M3i, Male, Mutation, Phenotype, Protein Structure, Protein-Serine-Threonine Kinases, reichhart, Tertiary
@article{georgel_drosophila_2001,
title = {Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis},
author = {Philippe Georgel and S Naitza and Christine Kappler and Dominique Ferrandon and Daniel Zachary and C Swimmer and C Kopczynski and G Duyk and Jean-Marc Reichhart and Jules A Hoffmann},
issn = {1534-5807},
year = {2001},
date = {2001-10-01},
journal = {Dev. Cell},
volume = {1},
number = {4},
pages = {503--514},
abstract = {We report the molecular characterization of the immune deficiency (imd) gene, which controls antibacterial defense in Drosophila. imd encodes a protein with a death domain similar to that of mammalian RIP (receptor interacting protein), a protein that plays a role in both NF-kappaB activation and apoptosis. We show that imd functions upstream of the DmIKK signalosome and the caspase DREDD in the control of antibacterial peptide genes. Strikingly, overexpression of imd leads to constitutive transcription of these genes and to apoptosis, and both effects are blocked by coexpression of the caspase inhibitor P35. We also show that imd is involved in the apoptotic response to UV irradiation. These data raise the possibility that antibacterial response and apoptosis share common control elements in Drosophila.},
keywords = {Animals, Anti-Infective Agents, Apoptosis, Bacterial Infections, Caspases, Chromosome Mapping, Cysteine Proteinase Inhibitors, DNA Damage, Female, ferrandon, Gene Expression, hoffmann, I-kappa B Kinase, Immunocompromised Host, In Situ Nick-End Labeling, Insect Proteins, M3i, Male, Mutation, Phenotype, Protein Structure, Protein-Serine-Threonine Kinases, reichhart, Tertiary},
pubstate = {published},
tppubtype = {article}
}