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@ARTICLE{Schmitt:128277,
      author       = {M. Schmitt$^*$ and K. Leykauf$^*$ and E. Reinz$^*$ and H.
                      Cheng$^*$ and A. Alonso$^*$ and J. Schenkel$^*$},
      title        = {{M}utation of human connexin43 amino acids s279/s282
                      increases protein stability upon treatment with epidermal
                      growth factor.},
      journal      = {Cell biochemistry and biophysics},
      volume       = {69},
      number       = {2},
      issn         = {1559-0283},
      address      = {New York, NY},
      publisher    = {Springer},
      reportid     = {DKFZ-2017-04294},
      pages        = {379 - 384},
      year         = {2014},
      abstract     = {Connexins are the structural units of gap junctions,
                      structures allowing interchanging of information between the
                      adjacent cells. Connexin43 (Cx43) is the most abundant gap
                      junction protein. Cx43 can be degraded by lysosome- and
                      proteasome-mediated processes upon internalisation of the
                      entire structure. Only little is known about the role of
                      phosphorylation during the gap junction degradation. In
                      Cx43, a protein containing 14 amino acids susceptible to be
                      phosphorylated, amino acids S279 and S282 are phosphorylated
                      upon epidermal growth factor (EGF) treatment by erk1/2 MAP
                      kinases. Here, we show that the wild-type Cx43 protein, as
                      well as HeLa cells expressing the mutated Cx43 proteins
                      S279A, S282A, and S279A/S282A, is mainly located at the
                      plasma membrane. However, the protein stability is not
                      altered in the isolated single mutants, whereas the double
                      mutant S279A/S282A is strongly degradation impaired upon EGF
                      treatment. This effect is not due to the decreased Cx43
                      internalisation, but seems to be related to a reduced
                      ubiquitination.},
      keywords     = {Connexin 43 (NLM Chemicals) / Epidermal Growth Factor (NLM
                      Chemicals) / Mitogen-Activated Protein Kinase 1 (NLM
                      Chemicals) / Mitogen-Activated Protein Kinase 3 (NLM
                      Chemicals)},
      cin          = {F050 / W430},
      ddc          = {570},
      cid          = {I:(DE-He78)F050-20160331 / I:(DE-He78)W430-20160331},
      pnm          = {316 - Infections and cancer (POF3-316)},
      pid          = {G:(DE-HGF)POF3-316},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24399133},
      doi          = {10.1007/s12013-013-9811-5},
      url          = {https://inrepo02.dkfz.de/record/128277},
}