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@ARTICLE{West:130863,
      author       = {G. West and J. Gullmets and L. Virtanen and S.-P. Li and A.
                      Keinänen and T. Shimi and M. Mauermann$^*$ and T. Heliö
                      and M. Kaartinen and L. Ollila and J. Kuusisto and J. E.
                      Eriksson and R. D. Goldman and H. Herrmann$^*$ and P.
                      Taimen},
      title        = {{D}eleterious assembly of the lamin {A}/{C} mutant
                      p.{S}143{P} causes {ER} stress in familial dilated
                      cardiomyopathy.},
      journal      = {Journal of cell science},
      volume       = {129},
      number       = {14},
      issn         = {1477-9137},
      address      = {Cambridge},
      publisher    = {Company of Biologists Limited},
      reportid     = {DKFZ-2017-05941},
      pages        = {2732 - 2743},
      year         = {2016},
      abstract     = {Mutation of the LMNA gene, encoding nuclear lamin A and
                      lamin C (hereafter lamin A/C), is a common cause of familial
                      dilated cardiomyopathy (DCM). Among Finnish DCM patients,
                      the founder mutation c.427T>C (p.S143P) is the most
                      frequently reported genetic variant. Here, we show that
                      p.S143P lamin A/C is more nucleoplasmic and soluble than
                      wild-type lamin A/C and accumulates into large intranuclear
                      aggregates in a fraction of cultured patient fibroblasts as
                      well as in cells ectopically expressing either FLAG- or
                      GFP-tagged p.S143P lamin A. In fluorescence loss in
                      photobleaching (FLIP) experiments, non-aggregated
                      EGFP-tagged p.S143P lamin A was significantly more dynamic.
                      In in vitro association studies, p.S143P lamin A failed to
                      form appropriate filament structures but instead assembled
                      into disorganized aggregates similar to those observed in
                      patient cell nuclei. A whole-genome expression analysis
                      revealed an elevated unfolded protein response (UPR) in
                      cells expressing p.S143P lamin A/C. Additional endoplasmic
                      reticulum (ER) stress induced by tunicamycin reduced the
                      viability of cells expressing mutant lamin further. In
                      summary, p.S143P lamin A/C affects normal lamina structure
                      and influences the cellular stress response, homeostasis and
                      viability.},
      keywords     = {Biomarkers (NLM Chemicals) / Lamin Type A (NLM Chemicals) /
                      Mutant Proteins (NLM Chemicals) / Protein Aggregates (NLM
                      Chemicals) / lamin C (NLM Chemicals) / Green Fluorescent
                      Proteins (NLM Chemicals)},
      cin          = {B062 / B060},
      ddc          = {570},
      cid          = {I:(DE-He78)B062-20160331 / I:(DE-He78)B060-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27235420},
      pmc          = {pmc:PMC4958296},
      doi          = {10.1242/jcs.184150},
      url          = {https://inrepo02.dkfz.de/record/130863},
}