Publications de l'Equipe Friant
- Cex1 is a component of the COPI intracellular trafficking machinery
Carla Noemi Castro , Michelle Rosenzwajg, Raphael Carapito, Mohammad Shahrooei, Martina Konantz , Amjad Khan , Zhichao Miao, Miriam Groß , Thibaud Tranchant , Mirjana Radosavljevic, Nicodème Paul , Tristan Stemmelen , Fabien Pitoiset, Aurélie Hirschler , Benoit Nespola , Anne Molitor , Véronique Rolli, Angélique Pichot , Laura Eva Faletti, Bruno Rinaldi , Sylvie Friant , Mark Mednikov , Hatice Karauzum , M Javad Aman , Christine Carapito , Claudia Lengerke , Vahid Ziaee, Wafaa Eyaid , Stephan Ehl, Fayhan Alroqi , Nima Parvaneh.
The Nck-associated protein 1-like (NCKAP1L) gene, alternatively called hematopoietic protein 1 (HEM-1), encodes a hematopoietic lineage-specific regulator of the actin cytoskeleton. Nckap1l-deficient mice have anomalies in lymphocyte development, phagocytosis, and neutrophil migration. Here we report, for the first time, NCKAP1L deficiency cases in humans. In two unrelated patients of Middle Eastern origin, recessive mutations in NCKAP1L abolishing protein expression led to immunodeficiency, lymphoproliferation, and hyperinflammation with features of hemophagocytic lymphohistiocytosis. Immunophenotyping showed an inverted CD4/CD8 ratio with a major shift of both CD4+ and CD8+ cells toward memory compartments, in line with combined RNA-seq/proteomics analyses revealing a T cell exhaustion signature. Consistent with the core function of NCKAP1L in the reorganization of the actin cytoskeleton, patients' T cells displayed impaired early activation, immune synapse morphology, and leading edge formation. Moreover, knockdown of nckap1l in zebrafish led to defects in neutrophil migration. Hence, NCKAP1L mutations lead to broad immune dysregulation in humans, which could be classified within actinopathies.Biallelic PDE2A variants: a new cause of syndromic paroxysmal dyskinesia
Diane Doummar, Christel Dentel , Romane Lyautey , Julia Metreau , Boris Keren , Nathalie Drouot, Ludivine Malherbe , Viviane Bouilleret , Jérémie Courraud, Maria Paola Valenti-Hirsch , Lorella Minotti , Blandine Dozieres-Puyravel , Séverine Bär , Julia Scholly , Elise Schaefer, Caroline Nava , Thomas Wirth , Hala Nasser, Marie de Salins , Anne de Saint Martin , Marie Thérèse Abi Warde , Philippe Kahane , Edouard Hirsch , Mathieu Anheim , Sylvie Friant , Jamel Chelly , Cyril Mignot , Gabrielle Rudolf.
Cause of complex dyskinesia remains elusive in some patients. A homozygous missense variant leading to drastic decrease of PDE2A enzymatic activity was reported in one patient with childhood-onset choreodystonia preceded by paroxysmal dyskinesia and associated with cognitive impairment and interictal EEG abnormalities. Here, we report three new cases with biallelic PDE2A variants identified by trio whole-exome sequencing. Mitochondria network was analyzed after Mitotracker™ Red staining in control and mutated primary fibroblasts. Analysis of retrospective video of patients' movement disorder and refinement of phenotype was carried out. We identified a homozygous gain of stop codon variant c.1180C>T; p.(Gln394*) in PDE2A in siblings and compound heterozygous variants in young adult: a missense c.446C>T; p.(Pro149Leu) and splice-site variant c.1922+5G>A predicted and shown to produce an out of frame transcript lacking exon 22. All three patients had cognitive impairment or developmental delay. The phenotype of the two oldest patients, aged 9 and 26, was characterized by childhood-onset refractory paroxysmal dyskinesia initially misdiagnosed as epilepsy due to interictal EEG abnormalities. The youngest patient showed a proven epilepsy at the age of 4 months and no paroxysmal dyskinesia at 15 months. Interestingly, analysis of the fibroblasts with the biallelic variants in PDE2A variants revealed mitochondria network morphology changes. Together with previously reported case, our three patients confirm that biallelic PDE2A variants are a cause of childhood-onset refractory paroxysmal dyskinesia with cognitive impairment, sometimes associated with choreodystonia and interictal baseline EEG abnormalities or epilepsy.Proteasome subunit PSMC variants cause neurosensory syndrome combining deafness and cataract due to proteotoxic stress
Ariane Kröll-Hermi, Frédéric Ebstein, Corinne Stoetzel, Véronique Geoffroy, Elise Schaefer, Sophie Scheidecker, Séverine Bär , Masanari Takamiya , Koichi Kawakami, Barbara A Zieba , Fouzia Studer , Valerie Pelletier, Carine Eyermann , Claude Speeg-Schatz , Vincent Laugel, Dan Lipsker , Florian Sandron , Steven McGinn , Anne Boland , Jean-François Deleuze, Lauriane Kuhn , Johana Chicher , Philippe Hammann , Sylvie Friant , Christelle Etard , Elke Krüger , Jean Muller, Uwe Strähle , Hélène Dollfus.
The ubiquitin-proteasome system degrades ubiquitin-modified proteins to maintain protein homeostasis and to control signalling. Whole-genome sequencing of patients with severe deafness and early-onset cataracts as part of a neurological, sensorial and cutaneous novel syndrome identified a unique deep intronic homozygous variant in the PSMC3 gene, encoding the proteasome ATPase subunit Rpt5, which lead to the transcription of a cryptic exon. The proteasome content and activity in patient's fibroblasts was however unaffected. Nevertheless, patient's cells exhibited impaired protein homeostasis characterized by accumulation of ubiquitinated proteins suggesting severe proteotoxic stress. Indeed, the TCF11/Nrf1 transcriptional pathway allowing proteasome recovery after proteasome inhibition is permanently activated in the patient's fibroblasts. Upon chemical proteasome inhibition, this pathway was however impaired in patient's cells, which were unable to compensate for proteotoxic stress although a higher proteasome content and activity. Zebrafish modelling for knockout in PSMC3 remarkably reproduced the human phenotype with inner ear development anomalies as well as cataracts, suggesting that Rpt5 plays a major role in inner ear, lens and central nervous system development.Assigning mitochondrial localization of dual localized proteins using a yeast Bi-Genomic Mitochondrial-Split-GFP, Gaétan Bader , Ludovic Enkler , Yuhei Araiso , Marine Hemmerle , Krystyna Binko , Emilia Baranowska , Johan-Owen De Craene , Julie Ruer-Laventie , Jean Pieters , Déborah Tribouillard-Tanvier , Bruno Senger , Jean-Paul di Rago , Sylvie Friant , Roza Kucharczyk , Hubert Dominique Becker
A single nuclear gene can be translated into a dual localized protein that distributes between the cytosol and mitochondria. Accumulating evidences show that mitoproteomes contain lots of these dual localized proteins termed echoforms. Unraveling the existence of mitochondrial echoforms using current GFP (Green Fluorescent Protein) fusion microscopy approaches is extremely difficult because the GFP signal of the cytosolic echoform will almost inevitably mask that of the mitochondrial echoform. We therefore engineered a yeast strain expressing a new type of Split-GFP that we termed Bi-Genomic Mitochondrial-Split-GFP (BiG Mito-Split-GFP). Because one moiety of the GFP is translated from the mitochondrial machinery while the other is fused to the nuclear-encoded protein of interest translated in the cytosol, the self-reassembly of this Bi-Genomic-encoded Split-GFP is confined to mitochondria. We could authenticate the mitochondrial importability of any protein or echoform from yeast, but also from other organisms such as the human Argonaute 2 mitochondrial echoform.Yeast as a Model to Understand Actin-Mediated Cellular Functions in Mammals-Illustrated with Four Actin Cytoskeleton Proteins
Zain Akram, Ishtiaq Ahmed, Heike Mack, Ramandeep Kaur, Richard C Silva, Beatriz A Castilho, Sylvie Friant, Evelyn Sattlegger, Alan L Munn
The budding yeast Saccharomyces cerevisiae has an actin cytoskeleton that comprises a set of protein components analogous to those found in the actin cytoskeletons of higher eukaryotes. Furthermore, the actin cytoskeletons of S. cerevisiae and of higher eukaryotes have some similar physiological roles. The genetic tractability of budding yeast and the availability of a stable haploid cell type facilitates the application of molecular genetic approaches to assign functions to the various actin cytoskeleton components. This has provided information that is in general complementary to that provided by studies of the equivalent proteins of higher eukaryotes and hence has enabled a more complete view of the role of these proteins. Several human functional homologues of yeast actin effectors are implicated in diseases. A better understanding of the molecular mechanisms underpinning the functions of these proteins is critical to develop improved therapeutic strategies. In this article we chose as examples four evolutionarily conserved proteins that associate with the actin cytoskeleton: 1) yeast Hof1p/mammalian PSTPIP1, 2) yeast Rvs167p/mammalian BIN1, 3) yeast eEF1A/eEF1A1 and eEF1A2 and 4) yeast Yih1p/mammalian IMPACT. We compare the knowledge on the functions of these actin cytoskeleton-associated proteins that has arisen from studies of their homologues in yeast with information that has been obtained from in vivo studies using live animals or in vitro studies using cultured animal cell lines.
Véronique Geoffroy , Corinne Stoetzel , Sophie Scheidecker, Elise Schaefer, Isabelle Perrault , Séverine Bär , Ariane Kröll , Marion Delbarre , Manuela Antin , Anne-Sophie Leuvrey , Charline Henry , Hélène Blanché , Eva Decker , Katja Kloth9 , Günter Klaus , Christoph Mache , Dominique Martin-Coignard , Steven McGinn , Anne Boland , Jean-François Deleuze, Sylvie Friant , Sophie Saunier , Jean-Michel Rozet , Carsten Bergmann, Hélène Dollfus, Jean Muller
Ciliopathies represent a wide spectrum of rare diseases with overlapping phenotypes and a high genetic heterogeneity. Among those, IFT140 is implicated in a variety of phenotypes ranging from isolated retinis pigmentosa to more syndromic cases. Using whole-genome sequencing in patients with uncharacterized ciliopathies, we identified a novel recurrent tandem duplication of exon 27-30 (6.7 kb) in IFT140, c.3454-488_4182+2588dup p.(Tyr1152_Thr1394dup), missed by whole-exome sequencing. Pathogenicity of the mutation was assessed on the patients' skin fibroblasts. Several hundreds of patients with a ciliopathy phenotype were screened and biallelic mutations were identified in 11 families representing 12 pathogenic variants of which seven are novel. Among those unrelated families especially with a Mainzer-Saldino syndrome, eight carried the same tandem duplication (two at the homozygous state and six at the heterozygous state). In conclusion, we demonstrated the implication of structural variations in IFT140-related diseases expanding its mutation spectrum. We also provide evidences for a unique genomic event mediated by an Alu-Alu recombination occurring on a shared haplotype. We confirm that whole-genome sequencing can be instrumental in the ability to detect structural variants for genomic disorders.
Mutations in KARS cause a severe neurological and neurosensory disease with optic neuropathy.
Scheidecker S, Bär S, Stoetzel C, Geoffroy V, Lannes B, Rinaldi B, Fischer F, Becker HD, Pelletier V, Pagan C, Acquaviva-Bourdain C, Kremer S, Mirande M, Tranchant C, Muller J, Friant S, Dollfus H.
Hum Mutat. 2019 May 22. doi: 10.1002/humu.23799.
Mutations in genes encoding aaRSs (aminoacyl-tRNA synthetases) have been reported in several neurological disorders. KARS is a dual localized lysyl-tRNA synthetase (LysRS) and its cytosolic isoform belongs to the multiple aminoacyl-tRNA synthetase complex (MSC). Biallelic mutations in KARS gene were described in a wide phenotypic spectrum ranging from non-syndromic deafness to complex impairments. Here, we report on a patient with severe neurological and neurosensory disease investigated by whole exome sequencing and found to carry biallelic mutations c.683C>T (p.Pro228Leu) and c.871T>G (p.Phe291Val), the second one being novel, in the KARS gene. The patient presented with an atypical clinical presentation with an optic neuropathy not previously reported. At the cellular level, we show that cytoplasmic KARS was expressed at a lower level in patient cells and displayed decreased interaction with MSC. In vitro, these two KARS variants have a decreased aminoacylation activity compared to wild type KARS, the p.Pro228Leu being the most affected. Our data suggest that dysfunction of cytoplasmic KARS resulted in decreased level of translation of the nuclear encoded lysine rich proteins belonging to the respiratory chain complex, thus impairing mitochondria functions.
A New SLC10A7 Homozygous Missense Mutation Responsible for a Milder Phenotype of Skeletal Dysplasia With Amelogenesis Imperfecta
Virginie Laugel-Haushalter, Séverine Bär, Elise Schaefer, Corinne Stoetzel, Véronique GEOFFROY, Yves Alembik, Naji Kharouf, Mathilde Huckert, Pauline Hamm, Joseph Hemmerle, Marie-Cécile Manière, Sylvie Friant, Hélène Dollfus, Agnès Bloch-Zupan, Front. Genet., 28 May 2019
Publication dans le journal Frontiers in Genetics en collaboration avec la Faculté Dentaire et la Faculté de Médecine de Strasbourg, sur l'identification d'un nouveau gène chez des patients atteints de dysplasie squelettique, une anomalie de la croissance des os.
Amelogenesis imperfecta (AI) is a heterogeneous group of rare inherited diseases presenting with enamel defects. More than 30 genes have been reported to be involved in syndromic or non-syndromic AI and new genes are continuously discovered (Smith et al., 2017). Whole-exome sequencing was performed in a consanguineous family. The affected daughter presented with intra-uterine and postnatal growth retardation, skeletal dysplasia, macrocephaly, blue sclerae, and hypoplastic AI. We identified a homozygous missense mutation in exon 11 of SLC10A7 (NM_001300842.2: c.908C>T; p.Pro303Leu) segregating with the disease phenotype. We found that Slc10a7 transcripts were expressed in the epithelium of the developing mouse tooth, bones undergoing ossification, and in vertebrae. Our results revealed that SLC10A7 is overexpressed in patient fibroblasts. Patient cells display altered intracellular calcium localization suggesting that SLC10A7 regulates calcium trafficking. Mutations in this gene were previously reported to cause a similar syndromic phenotype, but with more severe skeletal defects (Ashikov et al., 2018;Dubail et al., 2018). Therefore, phenotypes resulting from a mutation in SLC10A7 can vary in severity. However, AI is the key feature indicative of SLC10A7 mutations in patients with skeletal dysplasia. Identifying this important phenotype will improve clinical diagnosis and patient management.Recessive PYROXD1 mutations cause adult-onset limb-girdle-type muscular dystrophy.
Sainio MT, Välipakka S, Rinaldi B, Lapatto H, Paetau A, Ojanen S, Brilhante V, Jokela M, Huovinen S, Auranen M, Palmio J, Friant S, Ylikallio E, Udd B, Tyynismaa H., J Neurol. 2018 Dec 4.
OBJECTIVE:
To describe adult-onset limb-girdle-type muscular dystrophy caused by biallelic variants in the PYROXD1 gene, which has been recently linked to early-onset congenital myofibrillar myopathy.
METHODS:
Whole exome sequencing was performed for adult-onset neuromuscular disease patients with no molecular diagnosis. Patients with PYROXD1 variants underwent clinical characterization, lower limb muscle MRI, muscle biopsy and spirometry. A yeast complementation assay was used to determine the biochemical consequences of the genetic variants.
RESULTS:
We identified four patients with biallelic PYROXD1 variants. Three patients, who had symptom onset in their 20s or 30s, were homozygous for the previously described p.Asn155Ser. The fourth patient, with symptom onset at age 49, was compound heterozygous for p.Asn155Ser variant and previously unknown p.Tyr354Cys. All patients presented with a LGMD-type phenotype of symmetric muscle weakness and wasting. Symptoms started in proximal muscles of the lower limbs, and progressed slowly to involve also upper limbs in a proximal-predominant fashion. All patients remained ambulant past the age of 60. They had restrictive lung disease but no cardiac impairment. Muscle MRI showed strong involvement of anterolateral thigh muscles. Muscle biopsy displayed chronic myopathic changes. Yeast complementation assay demonstrated the p.Tyr354Cys mutation to impair PYROXD1 oxidoreductase ability.
CONCLUSION:
PYROXD1 variants can cause an adult-onset slowly progressive LGMD-type phenotype.
Amphiphysin (BIN1) negatively regulates dynamin 2 for normal muscle maturation.
Cowling BS, Prokic I, Tasfaout H, Rabai A, Humbert F, Rinaldi B, Nicot AS, Kretz C, Friant S, Roux A, Laporte J ; J Clin Invest. 2017 Nov 13
Regulation of skeletal muscle development and organization is a complex process that is not fully understood. Here, we focused on amphiphysin 2 (BIN1, also known as bridging integrator-1) and dynamin 2 (DNM2), two ubiquitous proteins implicated in membrane remodeling and mutated in centronuclear myopathies (CNMs). We generated Bin1-/- Dnm2+/- mice to decipher the physiological interplay between BIN1 and DNM2. While Bin1-/- mice die perinatally from a skeletal muscle defect, Bin1-/- Dnm2+/- mice survived at least 18 months, and had normal muscle force and intracellular organization of muscle fibers, supporting BIN1 as a negative regulator of DNM2. We next characterized muscle-specific isoforms of BIN1 and DNM2. While BIN1 colocalized with and partially inhibited DNM2 activity during muscle maturation, BIN1 had no effect on the isoform of DNM2 found in adult muscle. Together, these results indicate that BIN1 and DNM2 regulate muscle development and organization, function through a common pathway, and define BIN1 as a negative regulator of DNM2 in vitro and in vivo during muscle maturation. Our data suggest that DNM2 modulation has potential as a therapeutic approach for patients with CNM and BIN1 defects. As BIN1 is implicated in cancers, arrhythmia, and late-onset Alzheimer disease, these findings may trigger research directions and therapeutic development for these common diseases.
WD40-repeat 47, a microtubule-associated protein, is essential for brain development and autophagy, PNAS, September 7, 2017
Meghna Kannan, Efil Bayam, Christel Wagner, Bruno Rinaldi, Perrine F. Kretz, Peggy Tilly, Marna Roos, Lara McGillewie, Séverine Bär, Shilpi Minocha, Claire Chevalier, Chrystelle Po, Sanger Mouse Genetics Project, Jamel Chelly, Jean-Louis Mandel, Renato Borgatti, Amélie Piton, Craig Kinnear, Ben Loos, David J. Adams, Yann Hérault, Stephan C. Collins, Sylvie Friant, Juliette D. Godin, and Binnaz Yalcin
The family of WD40-repeat (WDR) proteins is one of the largest in eukaryotes, but little is known about their function in brain development. Among 26 WDR genes assessed, we found 7 displaying a major impact in neuronal morphology when inactivated in mice. Remarkably, all seven genes showed corpus callosum defects, including thicker (Atg16l1, Coro1c, Dmxl2, and Herc1), thinner (Kif21b and Wdr89), or absent corpus callosum (Wdr47), revealing a common role for WDR genes in brain connectivity. We focused on the poorly studied WDR47 protein sharing structural homology with LIS1, which causes lissencephaly. In a dosage-dependent manner, mice lacking Wdr47 showed lethality, extensive fiber defects, microcephaly, thinner cortices, and sensory motor gating abnormalities. We showed that WDR47 shares functional characteristics with LIS1 and participates in key microtubule-mediated processes, including neural stem cell proliferation, radial migration, and growth cone dynamics. In absence of WDR47, the exhaustion of late cortical progenitors and the consequent decrease of neurogenesis together with the impaired survival of late-born neurons are likely yielding to the worsening of the microcephaly phenotype postnatally. Interestingly, the WDR47-specific C-terminal to LisH (CTLH) domain was associated with functions in autophagy described in mammals. Silencing WDR47 in hypothalamic GT1-7 neuronal cells and yeast models independently recapitulated these findings, showing conserved mechanisms. Finally, our data identified superior cervical ganglion-10 (SCG10) as an interacting partner of WDR47. Taken together, these results provide a starting point for studying the implications of WDR proteins in neuronal regulation of microtubules and autophagy.
Expression of the neuropathy-associated MTMR2 gene rescues MTM1-associated myopathy
Raess MA, Cowling BS, Bertazzi DL, Kretz C, Rinaldi B, Xuereb JM, Kessler P, Romero NB, Payrastre B, Friant S, Laporte J., Hum Mol Genet. 2017 Oct 1;26(19):3736-3748. doi: 10.1093/hmg/ddx258.
Myotubularins (MTMs) are active or dead phosphoinositides phosphatases defining a large protein family conserved through evolution and implicated in different neuromuscular diseases. Loss-of-function mutations in MTM1 cause the severe congenital myopathy called myotubular myopathy (or X-linked centronuclear myopathy) while mutations in the MTM1-related protein MTMR2 cause a recessive Charcot-Marie-Tooth peripheral neuropathy. Here we aimed to determine the functional specificity and redundancy of MTM1 and MTMR2, and to assess their abilities to compensate for a potential therapeutic strategy. Using molecular investigations and heterologous expression of human MTMs in yeast cells and in Mtm1 knockout mice, we characterized several naturally occurring MTMR2 isoforms with different activities. We identified the N-terminal domain as responsible for functional differences between MTM1 and MTMR2. An N-terminal extension observed in MTMR2 is absent in MTM1, and only the short MTMR2 isoform lacking this N-terminal extension behaved similarly to MTM1 in yeast and mice. Moreover, adeno-associated virus-mediated exogenous expression of several MTMR2 isoforms ameliorates the myopathic phenotype owing to MTM1 loss, with increased muscle force, reduced myofiber atrophy, and reduction of the intracellular disorganization hallmarks associated with myotubular myopathy. Noteworthy, the short MTMR2 isoform provided a better rescue when compared with the long MTMR2 isoform. In conclusion, these results point to the molecular basis for MTMs functional specificity. They also provide the proof-of-concept that expression of the neuropathy-associated MTMR2 gene improves the MTM1-associated myopathy, thus identifying MTMR2 as a novel therapeutic target for myotubular myopathy.
De Craene JO, Bertazzi DL, Bär S, Friant S., Int J Mol Sci. 2017 Mar 15
Phosphoinositides are lipids involved in the vesicular transport of proteins and lipids between the different compartments of eukaryotic cells. They act by recruiting and/or activating effector proteins and thus are involved in regulating various cellular functions, such as vesicular budding, membrane fusion and cytoskeleton dynamics. Although detected in small concentrations in membranes, their role is essential to cell function, since imbalance in their concentrations is a hallmark of many cancers. Their synthesis involves phosphorylating/dephosphorylating positions D3, D4 and/or D5 of their inositol ring by specific lipid kinases and phosphatases. This process is tightly regulated and specific to the different intracellular membranes. Most enzymes involved in phosphoinositide synthesis are conserved between yeast and human, and their loss of function leads to severe diseases (cancer, myopathy, neuropathy and ciliopathy).
Corinne Stoetze, Séverine Bär, Johan-Owen De Craene, Sophie Scheidecker, Christelle Etard, Johana Chicher, Jennifer R. Reck, Isabelle Perrault, Véronique Geoffroy, Kirsley Chennen, Uwe Strähle, Philippe Hammann, Sylvie Friant & Hélène Dollfus, Nat Commun. 2016 Nov 24.
Debard S, Bader G, De Craene JO, Enkler L, Bär S, Laporte D, Hammann P, Myslinski E, Senger B, Friant S, Becker HD, Methods. 2016 Oct 7.
O'Grady GL, Best HA, Sztal TE, Schartner V, Sanjuan-Vazquez M, Donkervoort S, Abath Neto O, Sutton RB, Ilkovski B, Romero NB, Stojkovic T, Dastgir J, Waddell LB, Boland A, Hu Y, Williams C, Ruparelia AA, Maisonobe T, Peduto AJ, Reddel SW, Lek M, Tukiainen T, Cummings BB, Joshi H, Nectoux J, Brammah S, Deleuze JF, Ing VO, Ramm G, Ardicli D, Nowak KJ, Talim B, Topaloglu H, Laing NG, North KN, MacArthur DG, Friant S, Clarke NF, Bryson-Richardson RJ, Bönnemann CG, Laporte J, Cooper ST., Am J Hum Genet. 2016 Nov 3. 10.1016/j.ajhg.2016.09.005.
- WANTED – Dead or alive: Myotubularins, a large disease-associated protein family Matthieu Raess, Sylvie Friant, Belinda S. Cowling, Jocelyn Laporte, Adv Biol Regul. 2016 Sep 15.
Bertazzi DL, De Craene JO, Bär S, Sanjuan-Vazquez M, Raess MA, Friant S., Biol Aujourdhui. 2015;209(1):97-109. doi: 10.1051/jbio/2015006.
Feyder S, De Craene JO, Bär S, Bertazzi DL, Friant S., Int J Mol Sci. 2015 Jan 9;16(1):1509-25. doi: 10.3390/ijms16011509.
Morvan J, de Craene JO, Rinaldi B, Addis V, Misslin C, Friant S., J Cell Sci. 2014 Dec 15. pii: jcs.159699.
De Craene JO, Courte F, Rinaldi B, Fitterer C, Herranz MC, Schmitt-Keichinger C, Ritzenthaler C, Friant S. PLoS One. 2014 Feb 25;9(2)
Spiess M, De Craene JO, Michelot A, Rinaldi B, Huber A, Drubin DG, Winsor B, Friant S., PLoS One. 2013
Amoasii L, Bertazzi DL, Tronchère H, Hnia K, Chicanne G, Rinaldi B, Cowling BS, Ferry A, Klaholz B, Payrastre B, Laporte J, Friant S. , PLoS Genet. 2012 Oct;8(10):e1002965. doi: 10.1371/journal.pgen.1002965. Epub 2012 Oct 11.
Morvan J, Rinaldi B, Friant S., Mol Biol Cell. 2012 Aug 23.
De Craene JO, Ripp R, Lecompte O, Thompson J, Poch O, Friant S. BMC Genomics. 2012 Jul 2;13(1):297.
Cardona F, Orozco H, Friant S, Aranda A, del Olmo M.
Arch Microbiol. 2011 Jul;193(7):515-25. Epub 2011 Mar 27.
Mirey G, Soulard A, Orange C, Friant S, Winsor B.
Biochem Soc Trans. 2005 Dec;33(Pt 6):1247-9.
Soulard A, Friant S, Fitterer C, Orange C, Kaneva G, Mirey G, Winsor B.
Protoplasma. 2005 Oct;226(1-2):89-101. Epub 2005 Oct 20.
Eugster A, Pécheur EI, Michel F, Winsor B, Letourneur F, Friant S.
Mol Biol Cell. 2004 Jul;15(7):3031-41.
Friant S, Pécheur EI, Eugster A, Michel F, Lefkir Y, Nourrisson D, Letourneur F.
Dev Cell. 2003 Sep;5(3):499-511.
Friant S, Lombardi R, Schmelzle T, Hall MN, Riezman H.
EMBO J. 2001 Dec 3;20(23):6783-92.