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Auteur Duband-Goulet I
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Duband-Goulet I
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ASC-1 Is a Cell Cycle Regulator Associated with Severe and Mild Forms of Myopathy
Villar-Quiles RN, Catervi F, Cabet E, et al.
Annals of neurology, 2019
Revue : Annals of neurology Titre : ASC-1 Is a Cell Cycle Regulator Associated with Severe and Mild Forms of Myopathy Type de document : Article Auteurs : Villar-Quiles RN ; Catervi F ; Cabet E ; Juntas-Morales R ; Genetti CA ; Gidaro T ; Koparir A ; Yuksel A ; Coppens S ; Deconinck N ; Pierce-Hoffman E ; Lornage X ; Durigneux J ; Laporte J ; Rendu J ; Romero NB ; Beggs AH ; Servais L ; Cossée M ; Olivé M ; Böhm J ; Duband-Goulet I ; Ferreiro A Editeur : United States Année de publication : 12/2019 Langues : Anglais (eng) Mots-clés : complexe ASC-1 ; corrélation génotype-phénotype ; étude rétrospective ; gène TRIP4 ; maladie neuromusculaire ; physiopathologie Pubmed / DOI : Pubmed : 31794073 / DOI : 10.1002/ana.25660
N° Profil MNM : 2019121 En ligne : http://www.ncbi.nlm.nih.gov/pubmed/31794073 Avis des lecteurs Aucun avis, ajoutez le vôtre !
(mauvais) 15 (excellent)
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The transcription coactivator ASC-1 is a regulator of skeletal myogenesis, and its deficiency causes a novel form of congenital muscle disease
Davignon L, Chauveau C, Julien C, et al.
Human molecular genetics, 2016, 25, 8, p 1559
Revue : Human molecular genetics, 25, 8 Titre : The transcription coactivator ASC-1 is a regulator of skeletal myogenesis, and its deficiency causes a novel form of congenital muscle disease Type de document : Article Auteurs : Davignon L, Auteur ; Chauveau C ; Julien C ; Dill C ; Duband-Goulet I ; Cabet E ; Buendia B ; Lilienbaum A ; Rendu J ; Minot MC ; Guichet A ; Allamand V ; Vadrot N ; Fauré J ; Odent S ; Lazaro L ; Leroy JP ; Marcorelles P ; Dubourg O ; Ferreiro A Année de publication : 2016 Pages : p 1559 Langues : Anglais (eng) Pubmed / DOI : DOI : 10.1093/hmg/ddw033 / Pubmed : 27008887
En ligne : http://www.ncbi.nlm.nih.gov/pubmed/27008887 Avis des lecteurs Aucun avis, ajoutez le vôtre !
(mauvais) 15 (excellent)
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SREBP1 function depends on a-type lamin expression levels (poster)
Buendia B, Attanda W, Duband-Goulet I, et al.
Congrès : 4th International Congress of Myology, 4ème colloque international de Myologie (9-13 mai 2011; Lille (France))
2011, p. 71
Titre : SREBP1 function depends on a-type lamin expression levels (poster) Type de document : Article Auteurs : Attanda W ; Duband-Goulet I ; Vadrot N ; Cabet E ; Ostlund C ; Worman H ; Zinn-Justin S Congrès : 4th International Congress of Myology, 4ème colloque international de Myologie (9-13 mai 2011; Lille (France)) Editeur : AFM-TELETHON Année de publication : 2011 Pages : p. 71 Langues : Anglais (eng) Mots-clés : colloque Résumé : Prelamin A and mature lamin A are A-type lamins, nuclear intermediate filament proteins that play a role in organizing the chromatin structure and gene expression. Lamin A results from the proteolytic processing of prelamin A. It is shorter (646 aa instead of 664) and unfarnesylated, due to the cleavage of its c-terminal end by the enzyme Zmpste (Young et al. 2006). The sterol regulatory element binding protein 1 (SREBP1), a member of the basic-helix-loop-helix (bHLH)-leucine zipper family of transcription factors, has been reported to bind to lamin A. After binding to its specific DNA sequences (E-Box and SRE sequences), SREBP1 dimers induce the expression of target genes involved in adipogenesis and membrane biogenesis (Nohturfft et al., 2009). A SREBP1 polypeptide (aa 227-487) interacts with the c-terminal region of prelamin A (aa 389-664) in vitro (Lloyd et al. 2002). In cells from patients with lamin A/C gene mutations causing lipodystrophy, prelamin A accumulates because of inefficient processing and associates with SREBP1 (Capanni et al. 2005).Here we asked whether high levels of prelamin A would directly impact SREBP1 function. We therefore designed a gene reporter assay, based on SREBP1-mediated activation of a promoter containing sterol regulatory elements (SREs) driving the expression of a Firefly luciferase gene. The transcriptional activity of SREBP1 was determined in HeLa cells co-expressing ectopic SREBP1 and prelamin A. We compared the impact of the wild-type prelamin A, which is processed into mature lamin A to that of the mutant variant L647R which can not be processed. Our data show that the transcriptional activity of HA-SREBP1 is significantly reduced when it is co-expressed with either wild-type or mutant ectopic prelamin A. In addition, we observed that i) the subnuclear distribution of the lamin-binding SREBP1 polypeptide (aa 227-487) varies upon prelamin A overexpression and that ii) this SREBP1 polypeptide co-immunoprecipitates with both ectopic prelamin A and lamin A.Our data support a model in which the negative impact of A-type lamins on the function of SREBP1 is a consequence of the interaction between these two proteins. They further suggest that the expression level of A-type lamins is critical for the regulation of SREBP1 function. Avis des lecteurs Aucun avis, ajoutez le vôtre !
(mauvais) 15 (excellent)
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The R439C mutation in LMNA causes lamin oligomerization and susceptibility to oxidative stress
Verstraeten VLRM, Caputo S, van Steensel MAM, et al.
Journal of cellular and molecular medicine, 2009, 13, 5, p. 959-971
Avis des lecteurs Aucun avis, ajoutez le vôtre !
(mauvais) 15 (excellent)