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@ARTICLE{Vetterkind:45390,
      author       = {Vetterkind, S. and Illenberger, S. and Kubicek, J. and
                      Boosen, M. and Appel, S. and Naim, H. Y. and Scheidtmann,
                      K.-H. and Preuss, U.},
      title        = {{B}inding of {P}ar-4 to the actin cytoskeleton is essential
                      for {P}ar-4/{D}lk-mediated apoptosis},
      journal      = {Experimental cell research},
      volume       = {305},
      issn         = {0014-4827},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PreJuSER-45390},
      pages        = {392 - 408},
      year         = {2005},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Prostate apoptosis response-4 (Par-4) is a 38-kDa protein
                      originally identified as a gene product upregulated in
                      prostate cancer cells undergoing apoptosis. Cell death
                      mediated by Par-4 and its interaction partner DAP like
                      kinase (Dlk) is characterized by dramatic changes of the
                      cytoskeleton. To uncover the role of the cytoskeleton in
                      Par-4/Dlk-mediated apoptosis, we analyzed Par-4 for a direct
                      association with cytoskeletal structures. Confocal
                      fluorescence microscopy revealed that endogenous Par-4 is
                      specifically associated with stress fibers in rat
                      fibroblasts. In vitro cosedimentation analyses and in vivo
                      FRET analyses showed that Par-4 directly binds to F-actin.
                      Actin binding is mediated by the N-terminal 266 amino acids,
                      but does not require the C-terminal region of Par-4
                      containing the leucine zipper and the death domain.
                      Furthermore, the interaction of Par-4 with actin filaments
                      leads to the formation of actin bundles in vitro and in
                      vivo. In rat fibroblasts, this microfilament association is
                      essential for the pro-apoptotic function of Par-4, since
                      both disruption of the actin cytoskeleton by cytochalasin D
                      treatment and overexpression of Par-4 constructs impaired in
                      actin binding result in a significant decrease of apoptosis
                      induction by Par-4 and Dlk. We propose a model, in which
                      Par-4 recruits Dlk to stress fibers, leading to enhanced
                      phosphorylation of the regulatory light chain of myosin II
                      (MLC) and to the induction of apoptosis.},
      keywords     = {Actin Cytoskeleton: chemistry / Actin Cytoskeleton:
                      metabolism / Actins: analysis / Actins: metabolism / Animals
                      / Apoptosis: physiology / Apoptosis Regulatory Proteins /
                      Calcium-Calmodulin-Dependent Protein Kinases / Cardiac
                      Myosins: metabolism / Cell Line, Tumor / Humans /
                      Intracellular Signaling Peptides and Proteins: analysis /
                      Intracellular Signaling Peptides and Proteins: genetics /
                      Intracellular Signaling Peptides and Proteins: metabolism /
                      MAP Kinase Kinase Kinases / Male / Mice / Mutation: genetics
                      / Myosin Light Chains: metabolism / Phosphorylation /
                      Protein-Serine-Threonine Kinases: metabolism / Rats /
                      Up-Regulation / Actins (NLM Chemicals) / Apoptosis
                      Regulatory Proteins (NLM Chemicals) / Intracellular
                      Signaling Peptides and Proteins (NLM Chemicals) / Myosin
                      Light Chains (NLM Chemicals) / myosin light chain 2 (NLM
                      Chemicals) / prostate apoptosis response-4 protein (NLM
                      Chemicals) / Protein-Serine-Threonine Kinases (NLM
                      Chemicals) / death-associated protein kinase (NLM Chemicals)
                      / Calcium-Calmodulin-Dependent Protein Kinases (NLM
                      Chemicals) / MAP Kinase Kinase Kinases (NLM Chemicals) /
                      mitogen-activated protein kinase kinase kinase 12 (NLM
                      Chemicals) / Cardiac Myosins (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Oncology / Cell Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15817164},
      UT           = {WOS:000228409100016},
      doi          = {10.1016/j.yexcr.2005.01.012},
      url          = {https://juser.fz-juelich.de/record/45390},
}