LINC complex alterations in DMD and EDMD/CMT fibroblastsCitation formats

  • External authors:
  • Surayya Taranum
  • Eva Vaylann
  • Peter Meinke
  • Liu Yang
  • Sascha Neumann
  • Iakowos Karakesisoglou
  • Manfred Wehnert
  • Angelika A. Noegel

Standard

LINC complex alterations in DMD and EDMD/CMT fibroblasts. / Taranum, Surayya; Vaylann, Eva; Meinke, Peter; Abraham, Sabu; Yang, Liu; Neumann, Sascha; Karakesisoglou, Iakowos; Wehnert, Manfred; Noegel, Angelika A.

In: European journal of cell biology, Vol. 91, No. 8, 08.2012, p. 614-628.

Research output: Contribution to journalArticle

Harvard

Taranum, S, Vaylann, E, Meinke, P, Abraham, S, Yang, L, Neumann, S, Karakesisoglou, I, Wehnert, M & Noegel, AA 2012, 'LINC complex alterations in DMD and EDMD/CMT fibroblasts', European journal of cell biology, vol. 91, no. 8, pp. 614-628. https://doi.org/10.1016/j.ejcb.2012.03.003

APA

Taranum, S., Vaylann, E., Meinke, P., Abraham, S., Yang, L., Neumann, S., ... Noegel, A. A. (2012). LINC complex alterations in DMD and EDMD/CMT fibroblasts. European journal of cell biology, 91(8), 614-628. https://doi.org/10.1016/j.ejcb.2012.03.003

Vancouver

Taranum S, Vaylann E, Meinke P, Abraham S, Yang L, Neumann S et al. LINC complex alterations in DMD and EDMD/CMT fibroblasts. European journal of cell biology. 2012 Aug;91(8):614-628. https://doi.org/10.1016/j.ejcb.2012.03.003

Author

Taranum, Surayya ; Vaylann, Eva ; Meinke, Peter ; Abraham, Sabu ; Yang, Liu ; Neumann, Sascha ; Karakesisoglou, Iakowos ; Wehnert, Manfred ; Noegel, Angelika A. / LINC complex alterations in DMD and EDMD/CMT fibroblasts. In: European journal of cell biology. 2012 ; Vol. 91, No. 8. pp. 614-628.

Bibtex

@article{569d2715f0e840cd97c245be482c93d2,
title = "LINC complex alterations in DMD and EDMD/CMT fibroblasts",
abstract = "Emery-Dreifuss muscular dystrophy (EDMD) is a late onset-disease characterized by skeletal muscle wasting and heart defects with associated risk of sudden death. The autosomal dominant form of the disease is caused by mutations in the . LMNA gene encoding LaminA and C, the X-linked form results from mutations in the gene encoding the inner nuclear membrane protein Emerin (. STA). Both Emerin and LaminA/C interact with the nuclear envelope proteins Nesprin-1 and -2 and mutations in genes encoding C-terminal isoforms of Nesprin-1 and -2 have also been implicated in EDMD. Here we analyse primary fibroblasts from patients affected by either Duchenne muscular dystrophy (DMD) or Emery-Dreifuss muscular dystrophy/Charcot-Marie-Tooth syndrome (EDMD/CMT) that in addition to the disease causing mutations harbour mutations in the Nesprin-1 gene and in the SUN1 and SUN2 gene, respectively. SUN proteins together with the Nesprins form the core of the LINC complex which connects the nucleus with the cytoskeleton. The mutations are accompanied by changes in cell adhesion, cell migration, senescence, and stress response, as well as in nuclear shape and nuclear envelope composition which are changes characteristic for laminopathies. Our results point to a potential influence of mutations in components of the LINC complex on the clinical outcome and the molecular pathology in the patients. {\circledC} 2012 Elsevier GmbH.",
keywords = "EDMD, Laminopathy, Muscular dystrophy, Nesprins, Nuclear envelope, SUN2, SUN2 proteome",
author = "Surayya Taranum and Eva Vaylann and Peter Meinke and Sabu Abraham and Liu Yang and Sascha Neumann and Iakowos Karakesisoglou and Manfred Wehnert and Noegel, {Angelika A.}",
note = "WT 087244/Z/08/Z, Wellcome Trust, United Kingdom",
year = "2012",
month = "8",
doi = "10.1016/j.ejcb.2012.03.003",
language = "English",
volume = "91",
pages = "614--628",
journal = "European journal of cell biology",
issn = "0171-9335",
publisher = "Urban und Fischer Verlag GmbH",
number = "8",

}

RIS

TY - JOUR

T1 - LINC complex alterations in DMD and EDMD/CMT fibroblasts

AU - Taranum, Surayya

AU - Vaylann, Eva

AU - Meinke, Peter

AU - Abraham, Sabu

AU - Yang, Liu

AU - Neumann, Sascha

AU - Karakesisoglou, Iakowos

AU - Wehnert, Manfred

AU - Noegel, Angelika A.

N1 - WT 087244/Z/08/Z, Wellcome Trust, United Kingdom

PY - 2012/8

Y1 - 2012/8

N2 - Emery-Dreifuss muscular dystrophy (EDMD) is a late onset-disease characterized by skeletal muscle wasting and heart defects with associated risk of sudden death. The autosomal dominant form of the disease is caused by mutations in the . LMNA gene encoding LaminA and C, the X-linked form results from mutations in the gene encoding the inner nuclear membrane protein Emerin (. STA). Both Emerin and LaminA/C interact with the nuclear envelope proteins Nesprin-1 and -2 and mutations in genes encoding C-terminal isoforms of Nesprin-1 and -2 have also been implicated in EDMD. Here we analyse primary fibroblasts from patients affected by either Duchenne muscular dystrophy (DMD) or Emery-Dreifuss muscular dystrophy/Charcot-Marie-Tooth syndrome (EDMD/CMT) that in addition to the disease causing mutations harbour mutations in the Nesprin-1 gene and in the SUN1 and SUN2 gene, respectively. SUN proteins together with the Nesprins form the core of the LINC complex which connects the nucleus with the cytoskeleton. The mutations are accompanied by changes in cell adhesion, cell migration, senescence, and stress response, as well as in nuclear shape and nuclear envelope composition which are changes characteristic for laminopathies. Our results point to a potential influence of mutations in components of the LINC complex on the clinical outcome and the molecular pathology in the patients. © 2012 Elsevier GmbH.

AB - Emery-Dreifuss muscular dystrophy (EDMD) is a late onset-disease characterized by skeletal muscle wasting and heart defects with associated risk of sudden death. The autosomal dominant form of the disease is caused by mutations in the . LMNA gene encoding LaminA and C, the X-linked form results from mutations in the gene encoding the inner nuclear membrane protein Emerin (. STA). Both Emerin and LaminA/C interact with the nuclear envelope proteins Nesprin-1 and -2 and mutations in genes encoding C-terminal isoforms of Nesprin-1 and -2 have also been implicated in EDMD. Here we analyse primary fibroblasts from patients affected by either Duchenne muscular dystrophy (DMD) or Emery-Dreifuss muscular dystrophy/Charcot-Marie-Tooth syndrome (EDMD/CMT) that in addition to the disease causing mutations harbour mutations in the Nesprin-1 gene and in the SUN1 and SUN2 gene, respectively. SUN proteins together with the Nesprins form the core of the LINC complex which connects the nucleus with the cytoskeleton. The mutations are accompanied by changes in cell adhesion, cell migration, senescence, and stress response, as well as in nuclear shape and nuclear envelope composition which are changes characteristic for laminopathies. Our results point to a potential influence of mutations in components of the LINC complex on the clinical outcome and the molecular pathology in the patients. © 2012 Elsevier GmbH.

KW - EDMD

KW - Laminopathy

KW - Muscular dystrophy

KW - Nesprins

KW - Nuclear envelope

KW - SUN2

KW - SUN2 proteome

U2 - 10.1016/j.ejcb.2012.03.003

DO - 10.1016/j.ejcb.2012.03.003

M3 - Article

VL - 91

SP - 614

EP - 628

JO - European journal of cell biology

JF - European journal of cell biology

SN - 0171-9335

IS - 8

ER -