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@ARTICLE{Rappe:126394,
      author       = {U. Rappe$^*$ and T. Schlechter$^*$ and M. Aschoff$^*$ and
                      A. Hotz-Wagenblatt$^*$ and I. Hofmann$^*$},
      title        = {{N}uclear {ARVCF} protein binds splicing factors and
                      contributes to the regulation of alternative splicing.},
      journal      = {The journal of biological chemistry},
      volume       = {289},
      number       = {18},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {DKFZ-2017-02423},
      pages        = {12421 - 12434},
      year         = {2014},
      abstract     = {The armadillo repeat protein ARVCF is a component of
                      adherens junctions. Similar to related proteins, such as
                      p120-catenin and β-catenin, with known signaling functions,
                      localization studies indicate a cytoplasmic and a nuclear
                      pool of ARVCF. We find that ARVCF interacts with different
                      proteins involved in mRNA-processing: the splicing factor
                      SRSF1 (SF2/ASF), the RNA helicase p68 (DDX5), and the
                      heterogeneous nuclear ribonucleoprotein hnRNP H2. All three
                      proteins bind to ARVCF in an RNA-independent manner.
                      Furthermore, ARVCF occurs in large RNA-containing complexes
                      that contain both spliced and unspliced mRNAs of
                      housekeeping genes. By domain analysis, we show that
                      interactions occur via the ARVCF C terminus. Overexpression
                      of ARVCF, p68, SRSF1, and hnRNP H2 induces a significant
                      increase in splicing activity of a reporter mRNA. Upon
                      depletion of ARVCF followed by RNA sequence analysis,
                      several alternatively spliced transcripts are significantly
                      changed. Therefore, we conclude that nuclear ARVCF
                      influences splicing of pre-mRNAs. We hypothesize that ARVCF
                      is involved in alternative splicing, generating proteomic
                      diversity, and its deregulation may contribute to diseased
                      states, such as cancer and neurological disorders.},
      keywords     = {ARVCF protein, human (NLM Chemicals) / Armadillo Domain
                      Proteins (NLM Chemicals) / Cell Adhesion Molecules (NLM
                      Chemicals) / HNRNPH2 protein, human (NLM Chemicals) /
                      Heterogeneous-Nuclear Ribonucleoprotein Group F-H (NLM
                      Chemicals) / Nuclear Proteins (NLM Chemicals) /
                      Phosphoproteins (NLM Chemicals) / Protein Isoforms (NLM
                      Chemicals) / RNA Precursors (NLM Chemicals) / RNA, Messenger
                      (NLM Chemicals) / RNA-Binding Proteins (NLM Chemicals) /
                      Green Fluorescent Proteins (NLM Chemicals) / Serine-Arginine
                      Splicing Factors (NLM Chemicals) / Ddx5 protein, human (NLM
                      Chemicals) / DEAD-box RNA Helicases (NLM Chemicals)},
      cin          = {A190 / W180},
      ddc          = {570},
      cid          = {I:(DE-He78)A190-20160331 / I:(DE-He78)W180-20160331},
      pnm          = {311 - Signalling pathways, cell and tumor biology
                      (POF3-311)},
      pid          = {G:(DE-HGF)POF3-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24644279},
      pmc          = {pmc:PMC4007437},
      doi          = {10.1074/jbc.M113.530717},
      url          = {https://inrepo02.dkfz.de/record/126394},
}