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@ARTICLE{Franke:126526,
      author       = {W. Franke$^*$ and S. Rickelt$^*$ and R. Zimbelmann$^*$ and
                      Y. Dörflinger$^*$ and C. Kuhn$^*$ and N. Frey and H.
                      Heid$^*$ and R. Rosin-Arbesfeld},
      title        = {{S}triatins as plaque molecules of zonulae adhaerentes in
                      simple epithelia, of tessellate junctions in stratified
                      epithelia, of cardiac composite junctions and of various
                      size classes of lateral adherens junctions in cultures of
                      epithelia- and carcinoma-derived cells.},
      journal      = {Cell $\&$ tissue research},
      volume       = {359},
      number       = {3},
      issn         = {1432-0878},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {DKFZ-2017-02554},
      pages        = {779 - 797},
      year         = {2015},
      abstract     = {Proteins of the striatin family (striatins 1-4; sizes
                      ranging from 90 to 110 kDa on SDS-polyacrylamide gel
                      electrophoresis) are highly homologous in their amino acid
                      sequences but can differ in their cell-type-specific gene
                      expression patterns and biological functions. In various
                      cell types, we have found one, two or three polypeptides of
                      this evolutionarily old and nearly ubiquitous family of
                      proteins known to serve as scaffold proteins for diverse
                      protein complexes. Light and electron microscopic
                      immunolocalization methods have revealed striatins in
                      mammalian cell-cell adherens junctions (AJs). In simple
                      epithelia, we have localized striatins as constitutive
                      components of the plaques of the subapical zonulae
                      adhaerentes of cells, including intestinal, glandular,
                      ductal and urothelial cells and hepatocytes. Striatins
                      colocalize with E-cadherin or E-N-cadherin heterodimers and
                      with the plaque proteins α- and β-catenin, p120 and p0071.
                      In some epithelia and carcinomas and in cultured cells
                      derived therefrom, striatins are also seen in lateral AJs.
                      In stratified epithelia and in corresponding squamous cell
                      carcinomas, striatins can be found in plaques of some forms
                      of tessellate junctions. Moreover, striatins are major
                      plaque proteins of composite junctions (CJs; areae
                      compositae) in the intercalated disks connecting
                      cardiomyocytes, colocalizing with other CJ molecules,
                      including plectin and ankyrin-G. We discuss the
                      'multimodulator' scaffold roles of striatins in the
                      initiation and regulation of the formation of various
                      complex particles and structures. We propose that striatins
                      are included in the diagnostic candidate list of proteins
                      that, in the CJs of human hearts, can occur in mutated forms
                      in the pathogeneses of hereditary cardiomyopathies, as seen
                      in some types of genetically determined heart damage in
                      boxer dogs.},
      keywords     = {Antibodies (NLM Chemicals) / Calmodulin-Binding Proteins
                      (NLM Chemicals) / Membrane Proteins (NLM Chemicals) / Nerve
                      Tissue Proteins (NLM Chemicals) / STRN protein, human (NLM
                      Chemicals)},
      cin          = {A991},
      ddc          = {570},
      cid          = {I:(DE-He78)A991-20160331},
      pnm          = {311 - Signalling pathways, cell and tumor biology
                      (POF3-311)},
      pid          = {G:(DE-HGF)POF3-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25501894},
      pmc          = {pmc:PMC4341017},
      doi          = {10.1007/s00441-014-2053-z},
      url          = {https://inrepo02.dkfz.de/record/126526},
}