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@ARTICLE{Wirth:137186,
      author       = {Wirth, Alexander and Chen-Wacker, Chen and Wu, Yao-Wen and
                      Gorinski, Nataliya and Filippov, Mikhail A and Pandey,
                      Ghanshyam and Ponimaskin, Evgeni},
      title        = {{D}ual lipidation of the brain-specific {C}dc42 isoform
                      regulates its functional properties.},
      journal      = {Biochemical journal},
      volume       = {456},
      number       = {3},
      issn         = {0264-6021},
      address      = {London},
      publisher    = {Portland Press67261},
      reportid     = {DZNE-2020-03508},
      pages        = {311-322},
      year         = {2013},
      abstract     = {Cdc42 (cell division cycle 42) is a member of the Rho
                      GTPase family which regulates a variety of cellular
                      activities by controlling actin cytoskeleton and gene
                      expression. Cdc42 is expressed in the form of two splice
                      variants. The canonical Cdc42 isoform is prenylated
                      (Cdc42-prenyl), whereas the brainspecific isoform can be
                      palmitoylated (Cdc42-palm). In the present study we have
                      demonstrated palmitoylation of endogenous Cdc42 in rodent
                      and human brains and identified Cys(188) and Cys(189) as
                      acylation sites of Cdc42-palm. Moreover, we have shown that
                      Cys(188) can also be prenylated. Analysis of
                      acylation-deficient mutants revealed that lipidation of
                      Cys(188) is essential for proper membrane binding of
                      Cdc42-palm as well as for Cdc42-mediated regulation of gene
                      transcription and induction of densely packed filopodia in
                      neuroblastoma cells. We also found that Cdc42-prenyl is a
                      dominant splice variant in a wide range of commonly used
                      cell lines as well as in the cerebellum, whereas Cdc42-palm
                      is the main Cdc42 isoform in hippocampus, where it is
                      critically involved in the formation of dendritic filopodia
                      and spines. Replacement of endogenous Cdc42 by its
                      acylation-deficient mutants revealed the importance of
                      Cdc42-palm lipidation for its morphogenic and synaptogenic
                      effects in neurons. These findings demonstrate that dual
                      lipidation of Cdc42-palm represents an important regulator
                      of morphogenic signalling in hippocampal neurons.},
      keywords     = {Animals / Cell Line, Tumor / Cerebellum: cytology /
                      Cerebellum: metabolism / Cysteine: genetics / Cysteine:
                      metabolism / Dendrites: genetics / Dendrites: metabolism /
                      Hippocampus: cytology / Hippocampus: metabolism / Humans /
                      Isoenzymes: genetics / Isoenzymes: metabolism / Lipoylation:
                      physiology / Mice / Organ Specificity: physiology / Protein
                      Prenylation: physiology / Pseudopodia: genetics /
                      Pseudopodia: metabolism / Transcription, Genetic: physiology
                      / cdc42 GTP-Binding Protein: genetics / cdc42 GTP-Binding
                      Protein: metabolism / Cdc42 protein, mouse (NLM Chemicals) /
                      Isoenzymes (NLM Chemicals) / cdc42 GTP-Binding Protein (NLM
                      Chemicals) / Cysteine (NLM Chemicals)},
      cin          = {AG Dityatev},
      ddc          = {540},
      cid          = {I:(DE-2719)1310007},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24059268},
      doi          = {10.1042/BJ20130788},
      url          = {https://pub.dzne.de/record/137186},
}