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@ARTICLE{Lafarga:131785,
      author       = {V. Lafarga and O. Tapia and S. Sharma$^*$ and R. Bengoechea
                      and G. Stoecklin$^*$ and M. Lafarga and M. T. Berciano},
      title        = {{CBP}-mediated {SMN} acetylation modulates {C}ajal body
                      biogenesis and the cytoplasmic targeting of {SMN}.},
      journal      = {Cellular and molecular life sciences},
      volume       = {75},
      number       = {3},
      issn         = {1420-9071},
      address      = {Basel},
      publisher    = {Birkhäuser},
      reportid     = {DKFZ-2018-00082},
      pages        = {527 - 546},
      year         = {2018},
      note         = {DKFZ-ZMBH-Allianz},
      abstract     = {The survival of motor neuron (SMN) protein plays an
                      essential role in the biogenesis of spliceosomal snRNPs and
                      the molecular assembly of Cajal bodies (CBs). Deletion of or
                      mutations in the SMN1 gene cause spinal muscular atrophy
                      (SMA) with degeneration and loss of motor neurons. Reduced
                      SMN levels in SMA lead to deficient snRNP biogenesis with
                      consequent splicing pathology. Here, we demonstrate that SMN
                      is a novel and specific target of the acetyltransferase CBP
                      (CREB-binding protein). Furthermore, we identify lysine (K)
                      119 as the main acetylation site in SMN. Importantly, SMN
                      acetylation enhances its cytoplasmic localization, causes
                      depletion of CBs, and reduces the accumulation of snRNPs in
                      nuclear speckles. In contrast, the acetylation-deficient
                      SMNK119R mutant promotes formation of CBs and a novel
                      category of promyelocytic leukemia (PML) bodies enriched in
                      this protein. Acetylation increases the half-life of SMN
                      protein, reduces its cytoplasmic diffusion rate and modifies
                      its interactome. Hence, SMN acetylation leads to its
                      dysfunction, which explains the ineffectiveness of HDAC
                      (histone deacetylases) inhibitors in SMA therapy despite
                      their potential to increase SMN levels.},
      cin          = {A200},
      ddc          = {570},
      cid          = {I:(DE-He78)A200-20160331},
      pnm          = {311 - Signalling pathways, cell and tumor biology
                      (POF3-311)},
      pid          = {G:(DE-HGF)POF3-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28879433},
      doi          = {10.1007/s00018-017-2638-2},
      url          = {https://inrepo02.dkfz.de/record/131785},
}