% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Sharma:130552,
      author       = {S. Sharma and F. Poetz and M. Bruer and T. B. N. Ly-Hartig
                      and J. Schott and B. Séraphin and G. Stoecklin$^*$},
      title        = {{A}cetylation-{D}ependent {C}ontrol of {G}lobal {P}oly({A})
                      {RNA} {D}egradation by {CBP}/p300 and {HDAC}1/2.},
      journal      = {Molecular cell},
      volume       = {63},
      number       = {6},
      issn         = {1097-2765},
      address      = {[Cambridge, Mass.]},
      publisher    = {Cell Press},
      reportid     = {DKFZ-2017-05631},
      pages        = {927 - 938},
      year         = {2016},
      abstract     = {Acetylation of histones and transcription-related factors
                      is known to exert epigenetic and transcriptional control of
                      gene expression. Here we report that histone
                      acetyltransferases (HATs) and histone deacetylases (HDACs)
                      also regulate gene expression at the posttranscriptional
                      level by controlling poly(A) RNA stability. Inhibition of
                      HDAC1 and HDAC2 induces massive and widespread degradation
                      of normally stable poly(A) RNA in mammalian and Drosophila
                      cells. Acetylation-induced RNA decay depends on the HATs
                      p300 and CBP, which acetylate the exoribonuclease CAF1a, a
                      catalytic subunit of the CCR4-CAF1-NOT deadenlyase complex
                      and thereby contribute to accelerating poly(A) RNA
                      degradation. Taking adipocyte differentiation as a model, we
                      observe global stabilization of poly(A) RNA during
                      differentiation, concomitant with loss of CBP/p300
                      expression. Our study uncovers reversible acetylation as a
                      fundamental switch by which HATs and HDACs control the
                      overall turnover of poly(A) RNA.},
      keywords     = {CNOT8 protein, human (NLM Chemicals) / NR4A2 protein, human
                      (NLM Chemicals) / Nuclear Receptor Subfamily 4, Group A,
                      Member 2 (NLM Chemicals) / RNA, Messenger (NLM Chemicals) /
                      Transcription Factors (NLM Chemicals) / Poly A (NLM
                      Chemicals) / p300-CBP Transcription Factors (NLM Chemicals)
                      / p300-CBP-associated factor (NLM Chemicals) / HDAC1
                      protein, human (NLM Chemicals) / HDAC2 protein, human (NLM
                      Chemicals) / Histone Deacetylase 1 (NLM Chemicals) / Histone
                      Deacetylase 2 (NLM Chemicals)},
      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:27635759},
      doi          = {10.1016/j.molcel.2016.08.030},
      url          = {https://inrepo02.dkfz.de/record/130552},
}