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@ARTICLE{Manavski:128038,
      author       = {Y. Manavski and G. Carmona and K. Bennewitz and Z. Tang and
                      F. Zhang and A. Sakurai and A. M. Zeiher and J. S. Gutkind
                      and X. Li and J. Kroll$^*$ and S. Dimmeler and E. Chavakis},
      title        = {{B}rag2 differentially regulates β1- and
                      β3-integrin-dependent adhesion in endothelial cells and is
                      involved in developmental and pathological angiogenesis.},
      journal      = {Basic research in cardiology},
      volume       = {109},
      number       = {2},
      issn         = {0300-8428},
      address      = {Berlin},
      publisher    = {Springer65829},
      reportid     = {DKFZ-2017-04060},
      pages        = {404},
      year         = {2014},
      abstract     = {β1-Integrins are essential for angiogenesis. The
                      mechanisms regulating integrin function in endothelial cells
                      (EC) and their contribution to angiogenesis remain elusive.
                      Brag2 is a guanine nucleotide exchange factor for the small
                      Arf-GTPases Arf5 and Arf6. The role of Brag2 in EC and
                      angiogenesis and the underlying molecular mechanisms remain
                      unclear. siRNA-mediated Brag2-silencing reduced EC
                      angiogenic sprouting and migration. Brag2-siRNA transfection
                      differentially affected α5β1- and αVβ3-integrin
                      function: specifically, Brag2-silencing increased
                      focal/fibrillar adhesions and adhesion on β1-integrin
                      ligands (fibronectin and collagen), while reducing the
                      adhesion on the αVβ3-integrin ligand, vitronectin.
                      Consistent with these results, Brag2-silencing enhanced
                      surface expression of α5β1-integrin, while reducing
                      surface expression of αVβ3-integrin. Mechanistically,
                      Brag2-mediated αVβ3-integrin-recycling and β1-integrin
                      endocytosis and specifically of the active/matrix-bound
                      α5β1-integrin present in fibrillar/focal adhesions (FA),
                      suggesting that Brag2 contributes to the disassembly of FA
                      via β1-integrin endocytosis. Arf5 and Arf6 are promoting
                      downstream of Brag2 angiogenic sprouting, β1-integrin
                      endocytosis and the regulation of FA. In vivo silencing of
                      the Brag2-orthologues in zebrafish embryos using morpholinos
                      perturbed vascular development. Furthermore, in vivo
                      intravitreal injection of plasmids containing Brag2-shRNA
                      reduced pathological ischemia-induced retinal and choroidal
                      neovascularization. These data reveal that Brag2 is
                      essential for developmental and pathological angiogenesis by
                      promoting EC sprouting through regulation of adhesion by
                      mediating β1-integrin internalization and link for the
                      first time the process of β1-integrin endocytosis with
                      angiogenesis.},
      keywords     = {Antigens, CD29 (NLM Chemicals) / Guanine Nucleotide
                      Exchange Factors (NLM Chemicals) / IQSEC1 protein, human
                      (NLM Chemicals) / Integrin alphaVbeta3 (NLM Chemicals) /
                      Integrin beta3 (NLM Chemicals) / RNA, Small Interfering (NLM
                      Chemicals) / Receptors, Vitronectin (NLM Chemicals) / VEGFA
                      protein, human (NLM Chemicals) / Vascular Endothelial Growth
                      Factor A (NLM Chemicals) / integrin alphavbeta1 (NLM
                      Chemicals) / ADP-Ribosylation Factors (NLM Chemicals) /
                      ADP-ribosylation factor 6 (NLM Chemicals)},
      cin          = {A190},
      ddc          = {610},
      cid          = {I:(DE-He78)A190-20160331},
      pnm          = {311 - Signalling pathways, cell and tumor biology
                      (POF3-311)},
      pid          = {G:(DE-HGF)POF3-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:24522833},
      doi          = {10.1007/s00395-014-0404-2},
      url          = {https://inrepo02.dkfz.de/record/128038},
}