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  1. Article: Editorial: Dissecting the Intraflagellar Transport System in Physiology and Disease: Cilia-Related and -Unrelated Roles.

    Finetti, Francesca / Pan, Junmin / Qin, Hongmin / Delaval, Benedicte

    Frontiers in cell and developmental biology

    2020  Volume 8, Page(s) 615588

    Language English
    Publishing date 2020-11-27
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2020.615588
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Non-ciliary Roles of IFT Proteins in Cell Division and Polycystic Kidney Diseases.

    Vitre, Benjamin / Guesdon, Audrey / Delaval, Benedicte

    Frontiers in cell and developmental biology

    2020  Volume 8, Page(s) 578239

    Abstract: Cilia are small organelles present at the surface of most differentiated cells where they act as sensors for mechanical or biochemical stimuli. Cilia assembly and function require the Intraflagellar Transport (IFT) machinery, an intracellular transport ... ...

    Abstract Cilia are small organelles present at the surface of most differentiated cells where they act as sensors for mechanical or biochemical stimuli. Cilia assembly and function require the Intraflagellar Transport (IFT) machinery, an intracellular transport system that functions in association with microtubules and motors. If IFT proteins have long been studied for their ciliary roles, recent evidences indicate that their functions are not restricted to the cilium. Indeed, IFT proteins are found outside the ciliary compartment where they are involved in a variety of cellular processes in association with non-ciliary motors. Recent works also provide evidence that non-ciliary roles of IFT proteins could be responsible for the development of ciliopathies related phenotypes including polycystic kidney diseases. In this review, we will discuss the interactions of IFT proteins with microtubules and motors as well as newly identified non-ciliary functions of IFT proteins, focusing on their roles in cell division. We will also discuss the potential contribution of non-ciliary IFT proteins functions to the etiology of kidney diseases.
    Language English
    Publishing date 2020-09-22
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2020.578239
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Editorial

    Francesca Finetti / Junmin Pan / Hongmin Qin / Benedicte Delaval

    Frontiers in Cell and Developmental Biology, Vol

    Dissecting the Intraflagellar Transport System in Physiology and Disease: Cilia-Related and -Unrelated Roles

    2020  Volume 8

    Keywords intraflagellar transport (IFT) ; IFT-A and IFT-B complexes ; IFT interactors ; IFT- related diseases ; protein trafficking ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2020-11-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Non-ciliary Roles of IFT Proteins in Cell Division and Polycystic Kidney Diseases

    Benjamin Vitre / Audrey Guesdon / Benedicte Delaval

    Frontiers in Cell and Developmental Biology, Vol

    2020  Volume 8

    Abstract: Cilia are small organelles present at the surface of most differentiated cells where they act as sensors for mechanical or biochemical stimuli. Cilia assembly and function require the Intraflagellar Transport (IFT) machinery, an intracellular transport ... ...

    Abstract Cilia are small organelles present at the surface of most differentiated cells where they act as sensors for mechanical or biochemical stimuli. Cilia assembly and function require the Intraflagellar Transport (IFT) machinery, an intracellular transport system that functions in association with microtubules and motors. If IFT proteins have long been studied for their ciliary roles, recent evidences indicate that their functions are not restricted to the cilium. Indeed, IFT proteins are found outside the ciliary compartment where they are involved in a variety of cellular processes in association with non-ciliary motors. Recent works also provide evidence that non-ciliary roles of IFT proteins could be responsible for the development of ciliopathies related phenotypes including polycystic kidney diseases. In this review, we will discuss the interactions of IFT proteins with microtubules and motors as well as newly identified non-ciliary functions of IFT proteins, focusing on their roles in cell division. We will also discuss the potential contribution of non-ciliary IFT proteins functions to the etiology of kidney diseases.
    Keywords microtubule – associated proteins ; cell division ; ciliopathies ; molecular motor ; intraflagellar transport ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2020-09-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: The emergence of spontaneous coordinated epithelial rotation on cylindrical curved surfaces.

    Glentis, Alexandros / Blanch-Mercader, Carles / Balasubramaniam, Lakshmi / Saw, Thuan Beng / d'Alessandro, Joseph / Janel, Sebastien / Douanier, Audrey / Delaval, Benedicte / Lafont, Frank / Lim, Chwee Teck / Delacour, Delphine / Prost, Jacques / Xi, Wang / Ladoux, Benoit

    Science advances

    2022  Volume 8, Issue 37, Page(s) eabn5406

    Abstract: Three-dimensional collective epithelial rotation around a given axis represents a coordinated cellular movement driving tissue morphogenesis and transformation. Questions regarding these behaviors and their relationship with substrate curvatures are ... ...

    Abstract Three-dimensional collective epithelial rotation around a given axis represents a coordinated cellular movement driving tissue morphogenesis and transformation. Questions regarding these behaviors and their relationship with substrate curvatures are intimately linked to spontaneous active matter processes and to vital morphogenetic and embryonic processes. Here, using interdisciplinary approaches, we study the dynamics of epithelial layers lining different cylindrical surfaces. We observe large-scale, persistent, and circumferential rotation in both concavely and convexly curved cylindrical tissues. While epithelia of inverse curvature show an orthogonal switch in actomyosin network orientation and opposite apicobasal polarities, their rotational movements emerge and vary similarly within a common curvature window. We further reveal that this persisting rotation requires stable cell-cell adhesion and Rac-1-dependent cell polarity. Using an active polar gel model, we unveil the different relationships of collective cell polarity and actin alignment with curvatures, which lead to coordinated rotational behavior despite the inverted curvature and cytoskeleton order.
    Language English
    Publishing date 2022-09-14
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abn5406
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The use of the NEDD8 inhibitor MLN4924 (Pevonedistat) in a cyclotherapy approach to protect wild-type p53 cells from MLN4924 induced toxicity.

    Malhab, Lara J Bou / Descamps, Simon / Delaval, Benedicte / Xirodimas, Dimitris P

    Scientific reports

    2016  Volume 6, Page(s) 37775

    Abstract: Targetting the ubiquitin pathway is an attractive strategy for cancer therapy. The inhibitor of the ubiquitin-like molecule NEDD8 pathway, MLN4924 (Pevonedistat) is in Phase II clinical trials. Protection of healthy cells from the induced toxicity of the ...

    Abstract Targetting the ubiquitin pathway is an attractive strategy for cancer therapy. The inhibitor of the ubiquitin-like molecule NEDD8 pathway, MLN4924 (Pevonedistat) is in Phase II clinical trials. Protection of healthy cells from the induced toxicity of the treatment while preserving anticancer efficacy is a highly anticipated outcome in chemotherapy. Cyclotherapy was proposed as a promising approach to achieve this goal. We found that cytostatic activation of p53 protects cells against MLN4924-induced toxicity and importantly the effects are reversible. In contrast, cells with mutant or no p53 remain sensitive to NEDD8 inhibition. Using zebrafish embryos, we show that MLN4924-induced apoptosis is reduced upon pre-treatment with actinomycin D in vivo. Our studies show that the cellular effects of NEDD8 inhibition can be manipulated based on the p53 status and that NEDD8 inhibitors can be used in a p53-based cyclotherapy protocol to specifically target cancer cells devoid of wild type p53 function, while healthy cells will be protected from the induced toxicity.
    Language English
    Publishing date 2016-11-30
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep37775
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: De nouvelles fonctions extraciliaires pour les protéines ciliaires - quelles conséquences sur l'apparition de ciliopathies ?

    Taulet, Nicolas / Delaval, Bénédicte

    Medecine sciences : M/S

    2014  Volume 30, Issue 11, Page(s) 1040–1046

    Abstract: Cilia proteins have long been characterized for their role in cilia formation and function, and their implications in ciliopathies. However, several cellular defects induced by cilia proteins deregulation suggest that they could have non-ciliary roles. ... ...

    Title translation Non-ciliary functions of cilia proteins.
    Abstract Cilia proteins have long been characterized for their role in cilia formation and function, and their implications in ciliopathies. However, several cellular defects induced by cilia proteins deregulation suggest that they could have non-ciliary roles. Indeed, several non-ciliary functions have been recently characterized for cilia proteins including roles in intra-cellular and in vesicular transport, in spindle orientation or in the maintenance of genomic stability. These observations thus raise the crucial question of the contribution of non-ciliary functions of cilia proteins to the pathological manifestations associated with ciliopathies such as polycystic kidney disease.
    MeSH term(s) Animals ; Cell Cycle/genetics ; Cell Cycle/physiology ; Cell Cycle Proteins/deficiency ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/physiology ; Chlamydomonas reinhardtii/genetics ; Chlamydomonas reinhardtii/physiology ; Chlamydomonas reinhardtii/ultrastructure ; Chromosome Segregation/physiology ; Ciliary Motility Disorders/genetics ; Ciliary Motility Disorders/pathology ; Cytokinesis/physiology ; DNA Repair/physiology ; Genomic Instability/genetics ; Genomic Instability/physiology ; Humans ; Kidney Diseases, Cystic/genetics ; Kidney Diseases, Cystic/pathology ; Mammals ; Microtubule Proteins/deficiency ; Microtubule Proteins/genetics ; Microtubule Proteins/physiology ; Mitosis/physiology ; Molecular Motor Proteins/deficiency ; Molecular Motor Proteins/genetics ; Molecular Motor Proteins/physiology ; Phenotype ; Plant Proteins/genetics ; Plant Proteins/physiology ; Protein Transport/genetics ; Protein Transport/physiology ; Spindle Apparatus/ultrastructure ; Zebrafish ; Zebrafish Proteins/genetics ; Zebrafish Proteins/physiology
    Chemical Substances Cell Cycle Proteins ; Microtubule Proteins ; Molecular Motor Proteins ; Plant Proteins ; Zebrafish Proteins
    Language French
    Publishing date 2014-11
    Publishing country France
    Document type English Abstract ; Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 632733-3
    ISSN 1958-5381 ; 0767-0974
    ISSN (online) 1958-5381
    ISSN 0767-0974
    DOI 10.1051/medsci/20143011019
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: IFT88 controls NuMA enrichment at k-fibers minus-ends to facilitate their re-anchoring into mitotic spindles.

    Taulet, Nicolas / Douanier, Audrey / Vitre, Benjamin / Anguille, Christelle / Maurin, Justine / Dromard, Yann / Georget, Virginie / Delaval, Benedicte

    Scientific reports

    2019  Volume 9, Issue 1, Page(s) 10311

    Abstract: To build and maintain mitotic spindle architecture, molecular motors exert spatially regulated forces on microtubules (MT) minus-ends. This spatial regulation is required to allow proper chromosomes alignment through the organization of kinetochore ... ...

    Abstract To build and maintain mitotic spindle architecture, molecular motors exert spatially regulated forces on microtubules (MT) minus-ends. This spatial regulation is required to allow proper chromosomes alignment through the organization of kinetochore fibers (k-fibers). NuMA was recently shown to target dynactin to MT minus-ends and thus to spatially regulate dynein activity. However, given that k-fibers are embedded in the spindle, our understanding of the machinery involved in the targeting of proteins to their minus-ends remains limited. Intraflagellar transport (IFT) proteins were primarily studied for their ciliary roles but they also emerged as key regulators of cell division. Taking advantage of MT laser ablation, we show here that IFT88 concentrates at k-fibers minus-ends and is required for their re-anchoring into spindles by controlling NuMA accumulation. Indeed, IFT88 interacts with NuMA and is required for its enrichment at newly generated k-fibers minus-ends. Combining nocodazole washout experiments and IFT88 depletion, we further show that IFT88 is required for the reorganization of k-fibers into spindles and thus for efficient chromosomes alignment in mitosis. Overall, we propose that IFT88 could serve as a mitotic MT minus-end adaptor to concentrate NuMA at minus-ends thus facilitating k-fibers incorporation into the main spindle.
    MeSH term(s) Animals ; Cell Cycle Proteins/metabolism ; Cell Line ; HCT116 Cells ; Humans ; Laser Therapy ; Nocodazole/pharmacology ; Spindle Apparatus/drug effects ; Spindle Apparatus/metabolism ; Sus scrofa ; Tumor Suppressor Proteins/metabolism
    Chemical Substances Cell Cycle Proteins ; IFT88 protein, human ; NUMA1 protein, human ; Tumor Suppressor Proteins ; Nocodazole (SH1WY3R615)
    Language English
    Publishing date 2019-07-16
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-019-46605-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: New frontiers: discovering cilia-independent functions of cilia proteins.

    Vertii, Anastassiia / Bright, Alison / Delaval, Benedicte / Hehnly, Heidi / Doxsey, Stephen

    EMBO reports

    2015  Volume 16, Issue 10, Page(s) 1275–1287

    Abstract: In most vertebrates, mitotic spindles and primary cilia arise from a common origin, the centrosome. In non-cycling cells, the centrosome is the template for primary cilia assembly and, thus, is crucial for their associated sensory and signaling functions. ...

    Abstract In most vertebrates, mitotic spindles and primary cilia arise from a common origin, the centrosome. In non-cycling cells, the centrosome is the template for primary cilia assembly and, thus, is crucial for their associated sensory and signaling functions. During mitosis, the duplicated centrosomes mature into spindle poles, which orchestrate mitotic spindle assembly, chromosome segregation, and orientation of the cell division axis. Intriguingly, both cilia and spindle poles are centrosome-based, functionally distinct structures that require the action of microtubule-mediated, motor-driven transport for their assembly. Cilia proteins have been found at non-cilia sites, where they have distinct functions, illustrating a diverse and growing list of cellular processes and structures that utilize cilia proteins for crucial functions. In this review, we discuss cilia-independent functions of cilia proteins and re-evaluate their potential contributions to "cilia" disorders.
    MeSH term(s) Animals ; Centrosome/physiology ; Chromosome Segregation ; Cilia/chemistry ; Cilia/pathology ; Cilia/physiology ; HeLa Cells ; Humans ; Microtubules/physiology ; Mitosis ; Proteins/physiology ; Spindle Apparatus/physiology
    Chemical Substances Proteins
    Language English
    Publishing date 2015-09-09
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.15252/embr.201540632
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Pericentrin in cellular function and disease.

    Delaval, Benedicte / Doxsey, Stephen J

    The Journal of cell biology

    2009  Volume 188, Issue 2, Page(s) 181–190

    Abstract: Pericentrin is an integral component of the centrosome that serves as a multifunctional scaffold for anchoring numerous proteins and protein complexes. Through these interactions, pericentrin contributes to a diversity of fundamental cellular processes. ... ...

    Abstract Pericentrin is an integral component of the centrosome that serves as a multifunctional scaffold for anchoring numerous proteins and protein complexes. Through these interactions, pericentrin contributes to a diversity of fundamental cellular processes. Recent studies link pericentrin to a growing list of human disorders. Studies on pericentrin at the cellular, molecular, and, more recently, organismal level, provide a platform for generating models to elucidate the etiology of these disorders. Although the complexity of phenotypes associated with pericentrin-mediated disorders is somewhat daunting, insights into the cellular basis of disease are beginning to come into focus. In this review, we focus on human conditions associated with loss or elevation of pericentrin and propose cellular and molecular models that might explain them.
    MeSH term(s) Animals ; Antigens/genetics ; Antigens/metabolism ; Cell Death/genetics ; Centrosome/metabolism ; Centrosome/ultrastructure ; Dwarfism/genetics ; Genetic Predisposition to Disease/genetics ; Humans ; Mental Disorders/genetics ; Microtubules/genetics ; Microtubules/metabolism ; Mitosis/genetics ; Neoplasms/genetics ; Spindle Apparatus/genetics ; Spindle Apparatus/metabolism
    Chemical Substances Antigens ; pericentrin
    Language English
    Publishing date 2009-12-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.200908114
    Database MEDical Literature Analysis and Retrieval System OnLINE

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