Rho-dependent membrane folding causes Shigella entry into epithelial cells, The EMBO Journal, vol.15, pp.3315-3321, 1996. ,
Bacterial Toxins That Modify The Actin Cytoskeleton, Annual Review of Cell and Developmental Biology, vol.18, issue.1, pp.315-344, 2002. ,
DOI : 10.1146/annurev.cellbio.18.012502.134748
Calpain Activation by the Shigella flexneri Effector VirA Regulates Key Steps in the Formation and Life of the Bacterium's Epithelial Niche, Cell Host & Microbe, vol.11, issue.3, pp.240-252, 2012. ,
DOI : 10.1016/j.chom.2012.01.013
Calcium regulation of neural rhythms, memory and Alzheimer's disease, The Journal of Physiology, vol.9, issue.Suppl 1, pp.281-293, 2014. ,
DOI : 10.2174/156720512800492495
effector AmpA hijacks host cell SUMOylation, Cellular Microbiology, vol.79, issue.4, pp.504-519, 2015. ,
DOI : 10.1128/IAI.05422-11
URL : http://onlinelibrary.wiley.com/doi/10.1111/cmi.12380/pdf
Pathogenic Pore-Forming Proteins: Function and Host Response, Cell Host & Microbe, vol.12, issue.3, pp.266-275, 2012. ,
DOI : 10.1016/j.chom.2012.08.005
URL : https://doi.org/10.1016/j.chom.2012.08.005
Targeting SUMO E1 to Ubiquitin Ligases, Journal of Biological Chemistry, vol.1695, issue.21, pp.15376-15382, 2007. ,
DOI : 10.1093/embo-reports/kvf213
Characterization of the Promoter, MxiE Box and 5??? UTR of Genes Controlled by the Activity of the Type III Secretion Apparatus in Shigella flexneri, PLoS ONE, vol.14, issue.3, p.22427898, 2012. ,
DOI : 10.1371/journal.pone.0032862.t001
How shigella utilizes Ca(2+) jagged edge signals during invasion of epithelial cells, Frontiers in Cellular and Infection Microbiology, vol.6, p.26904514, 2016. ,
Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1, Nature Cell Biology, vol.194, issue.5, pp.477-483, 2010. ,
DOI : 10.1093/emboj/18.3.578
Calcium signaling: a historical account DOI: https://doi.org/ 10, Biological Research, vol.374067, pp.497-505, 2004. ,
Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix- associated PML bodies, The Journal of Cell Biology, vol.131, issue.1, pp.45-56, 1995. ,
DOI : 10.1083/jcb.131.1.45
Revealing the three dimensional architecture of focal adhesion components to explain Ca 2+ -mediated turnover of focal adhesions, Biochimica et Biophysica Acta (BBA) - General Subjects, vol.1861, issue.3, pp.624-635, 2017. ,
DOI : 10.1016/j.bbagen.2017.01.002
Calcium Signaling, Cell, vol.131, issue.6, pp.1047-1058, 2007. ,
DOI : 10.1016/j.cell.2007.11.028
SUMO: A Multifaceted Modifier of Chromatin Structure and Function, Developmental Cell, vol.24, issue.1, pp.1-12, 2013. ,
DOI : 10.1016/j.devcel.2012.11.020
Calpain 3 Is a Rapid-Action, Unidirectional Proteolytic Switch Central to Muscle Remodeling, PLoS ONE, vol.52, issue.1, p.20694146, 2010. ,
DOI : 10.1371/journal.pone.0011940.s009
Sumoylation by Ubc9 Regulates the Stem Cell Compartment and Structure and Function of the Intestinal Epithelium in Mice, Gastroenterology, vol.140, issue.1, pp.286-296, 2011. ,
DOI : 10.1053/j.gastro.2010.10.002
URL : https://hal.archives-ouvertes.fr/pasteur-00572277
ABSTRACT, Infection and Immunity, vol.82, issue.10, pp.4154-4168, 2014. ,
DOI : 10.1128/IAI.01984-14
Arkadia, a Novel SUMO-Targeted Ubiquitin Ligase Involved in PML Degradation, Molecular and Cellular Biology, vol.33, issue.11, pp.2163-217701019, 1128. ,
DOI : 10.1128/MCB.01019-12
Interplay between viruses and host sumoylation pathways, Nature Reviews Microbiology, vol.87, issue.6, pp.400-411, 2013. ,
DOI : 10.1128/JVI.02950-12
Bacterial virulence strategies that utilize Rho GTPases DOI: https://doi, Current Topics in Microbiology and Immunology, vol.291, pp.1-10, 2005. ,
DOI : 10.1007/3-540-27511-8_1
Sumoylation: A Regulatory Protein Modification in Health and Disease, Annual Review of Biochemistry, vol.82, issue.1, pp.357-385, 2013. ,
DOI : 10.1146/annurev-biochem-061909-093311
Sumoylation controls host anti-bacterial response to the gut invasive pathogen Shigella flexneri, EMBO reports, vol.15, issue.9, pp.965-972, 2014. ,
DOI : 10.15252/embr.201338386
The 'invisible hand': regulation of RHO GTPases by RHOGDIs, Nature Reviews Molecular Cell Biology, vol.275, issue.8, pp.493-504, 2011. ,
DOI : 10.1074/jbc.275.1.423
Calpain activity promotes the sealing of severed giant axons, Proceedings of the National Academy of Sciences, vol.26, issue.2, pp.4751-4756, 1997. ,
DOI : 10.1002/neu.480260209
A comprehensive compilation of SUMO proteomics, Nature Reviews Molecular Cell Biology, vol.15, issue.9, pp.581-595, 2016. ,
DOI : 10.1021/acs.jproteome.5b00062
Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli, Proceedings of the National Academy of Sciences, vol.6, issue.11, pp.12432-12437, 2014. ,
DOI : 10.1038/nmeth1109-786
URL : https://hal.archives-ouvertes.fr/pasteur-01104237
Host Cell Nuclear Localization of Shigella flexneri Effector OspF Is Facilitated by SUMOylation, Journal of Microbiology and Biotechnology, vol.27, issue.3, pp.610-615, 2017. ,
DOI : 10.4014/jmb.1611.11066
MxiE Regulates Intracellular Expression of Factors Secreted by the Shigella flexneri 2a Type III Secretion System, Journal of Bacteriology, vol.184, issue.16, pp.4409-4419, 2002. ,
DOI : 10.1128/JB.184.16.4409-4419.2002
How calpain is activated by calcium, Nature Structural Biology, vol.9, issue.4, pp.239-241, 1038. ,
DOI : 10.1038/nsb0402-239
IpgB2 in Complex with Human RhoA, Journal of Biological Chemistry, vol.12, issue.22, pp.17197-17208, 2010. ,
DOI : 10.1126/science.1174468
Statistical analysis of molecule colocalization in bioimaging, Cytometry Part A, vol.205, issue.2 Pt 1, pp.568-579, 2015. ,
DOI : 10.1083/jcb.201403041
URL : https://hal.archives-ouvertes.fr/hal-01218596
are selectively favoured by impaired autophagy to replicate intracellularly, Cellular Microbiology, vol.448, issue.1, pp.99-113, 2010. ,
DOI : 10.4161/auto.5075
URL : http://onlinelibrary.wiley.com/doi/10.1111/j.1462-5822.2009.01381.x/pdf
Proteasome inhibitors: valuable new tools for cell biologists, Trends in Cell Biology, vol.8, issue.10, pp.397-403, 1016. ,
DOI : 10.1016/S0962-8924(98)01346-4
Viral manipulation of cellular protein conjugation pathways: The SUMO lesson, World Journal of Virology, vol.2, issue.2, pp.79-90, 2013. ,
DOI : 10.5501/wjv.v2.i2.79
Identification of the cis-Acting Site Involved in Activation of Promoters Regulated by Activity of the Type III Secretion Apparatus in Shigella flexneri, Journal of Bacteriology, vol.184, issue.24, pp.6751-6759, 2002. ,
DOI : 10.1128/JB.184.24.6751-6759.2002
Regulation of the CUL3??Ubiquitin Ligase by a Calcium-Dependent Co-adaptor, Cell, vol.167, issue.2, pp.514-538, 2016. ,
DOI : 10.1016/j.cell.2016.09.026
Inhibition of the proteolysis of rat erythrocyte membrane proteins by a synthetic inhibitor of calpain DOI: https://doi.org/10, Biochemical and Biophysical Research Communications, vol.15788, pp.1117-1123, 1016. ,
Calcium-dependent plasma membrane repair requires m- or ??-calpain, but not calpain-3, the proteasome, or caspases, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1793, issue.12, pp.1886-1893, 2009. ,
DOI : 10.1016/j.bbamcr.2009.09.013
URL : https://hal.archives-ouvertes.fr/hal-01610039
Calpain Is Required for the Rapid, Calcium-dependent Repair of Wounded Plasma Membrane, Journal of Biological Chemistry, vol.1, issue.4, pp.2567-2575, 2007. ,
DOI : 10.1083/jcb.200411109
Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility, Journal of Cell Science, vol.112, pp.2069-2080, 1999. ,
The IpaC Carboxyterminal Effector Domain Mediates Src-Dependent Actin Polymerization during Shigella Invasion of Epithelial Cells, PLoS Pathogens, vol.581, issue.1, p.19165331, 2009. ,
DOI : 10.1371/journal.ppat.1000271.s009
SUMO-specific proteases/isopeptidases: SENPs and beyond, Genome Biology, vol.13, issue.7, pp.422-25315341, 2014. ,
DOI : 10.7314/APJCP.2012.13.5.2045
URL : http://doi.org/10.1186/s13059-014-0422-2
Effector Protein Involved in Bacterial Invasion of Host Cells, Journal of Biological Chemistry, vol.4, issue.25, pp.24022-24034, 2005. ,
DOI : 10.1016/0022-2836(80)90283-1
Calpains ??? An elaborate proteolytic system, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1824, issue.1, pp.224-236, 2012. ,
DOI : 10.1016/j.bbapap.2011.08.005
URL : https://doi.org/10.1016/j.bbapap.2011.08.005
Yersinia Virulence Depends on Mimicry of Host Rho-Family Nucleotide Dissociation Inhibitors, Cell, vol.126, issue.5, pp.869-880, 2006. ,
DOI : 10.1016/j.cell.2006.06.056
Listeria monocytogenes impairs SUMOylation for efficient infection, Nature, vol.22, issue.7292, pp.1192-1195, 2010. ,
DOI : 10.1038/nature08963
URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3627292/pdf
SUMO-2/3, Journal of Biological Chemistry, vol.72, issue.9, pp.6252-6258, 2000. ,
DOI : 10.1083/jcb.147.2.221
SUMO and the robustness of cancer, Nature Reviews Cancer, vol.11, issue.3, pp.184-197, 2017. ,
DOI : 10.1016/j.urolonc.2012.03.007
Shigella Infection Interferes with SUMOylation and Increases PML-NB Number, PLOS ONE, vol.552, issue.2???3, pp.258487-98, 2015. ,
DOI : 10.1371/journal.pone.0122585.s002
URL : https://doi.org/10.1371/journal.pone.0122585
Understanding the substrate specificity of conventional calpains DOI: https://doi, Biological Chemistry, vol.393, pp.853-871, 2012. ,
Sumoylation as an Integral Mechanism in Bacterial Infection and Disease Progression, Experimental Medicine and Biology, vol.29, issue.Suppl 3, pp.389-408978, 1007. ,
DOI : 10.1038/onc.2009.459
The VE-cadherin cytoplasmic domain undergoes proteolytic processing during endocytosis, Molecular Biology of the Cell, vol.9, issue.1, pp.76-84, 2017. ,
DOI : 10.1371/journal.pone.0106328
URL : http://www.molbiolcell.org/content/28/1/76.full.pdf
Salmonella Engages Host MicroRNAs To Modulate SUMOylation: a New Arsenal for Intracellular Survival, Molecular and Cellular Biology, vol.35, issue.17, pp.2932-294600397, 1128. ,
DOI : 10.1128/MCB.00397-15
RhoGDI SUMOylation at Lys-138 Increases Its Binding Activity to Rho GTPase and Its Inhibiting Cancer Cell Motility, Journal of Biological Chemistry, vol.31, issue.17, pp.13752-13760, 2012. ,
DOI : 10.1101/gad.1214604
Sequential cleavage of insulin receptor by calpain 2 and ??-secretase impairs insulin signalling, Diabetologia, vol.2, issue.Suppl 1, pp.2711-2721, 1007. ,
DOI : 10.1016/S0140-6736(61)90312-9