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@ARTICLE{Guzman:862133,
      author       = {Guzman, Gustavo and Guzman, Raul and Jordan, Nadine and
                      Hidalgo, Patricia},
      title        = {{A} tripartite interaction among the calcium channel α1-
                      and β-subunits and {F}-actin increases the readily
                      releasable pool of vesicles and its recovery after
                      depletion},
      journal      = {Frontiers in cellular neuroscience},
      volume       = {13},
      issn         = {1662-5102},
      address      = {Lausanne},
      publisher    = {Frontiers Research Foundation},
      reportid     = {FZJ-2019-02487},
      pages        = {125},
      year         = {2019},
      abstract     = {Neurotransmitter release is initiated by the influx of Ca2+
                      via voltage-gated calcium channels. The accessory β-subunit
                      (CaVβ) of these channels shapes synaptic transmission by
                      associating with the pore-forming subunit (CaVα1) and
                      up-regulating presynaptic calcium currents. Besides CaVα1,
                      CaVβ interacts with several partners including actin
                      filaments (F-actin). These filaments are known to associate
                      with synaptic vesicles at the presynaptic terminals and
                      support their translocation within different pools, but the
                      role of CaVβ/F-actin association on synaptic transmission
                      has not yet been explored. We here study how CaVβ4, the
                      major calcium channel β isoform in mamalian brain, modifies
                      synaptic transmission in concert with F-actin in cultured
                      hippocampal neurons. We analysed the effect of exogenous
                      CaVβ4 before and after pharmacological disruption of the
                      actin cytoskeleton and dissected calcium channel-dependent
                      and -independent functions by comparing the effects of the
                      wild-type subunit with the one bearing a double mutation
                      that impairs binding to CaVα1. We found that exogenously
                      expressed wild-type CaVβ4 enhances spontaneous and
                      depolarization-evoked excitatory postsynaptic currents
                      without altering synaptogenesis. CaVβ4 increases the size
                      of the readily releasable pool (RRP) of synaptic vesicles at
                      resting conditions and accelerates their recovery after
                      depletion. The enhanced neurotransmitter release induced by
                      CaVβ4 is abolished upon disruption of the actin
                      cytoskeleton. The CaVα1 association-deficient CaVβ4 mutant
                      associates with actin filaments, but neither alters
                      postsynaptic responses nor the time course of the RRP
                      recovery. Furthermore, this mutant protein preserves the
                      ability to increase the RRP size. These results indicate
                      that the interplay between CaVβ4 and F-actin also support
                      recruitment of synaptic vesicles to the RRP in a
                      CaVα1-independent manner. Our studies show an emerging role
                      of CaVβ in determining synaptic vesicle maturation toward
                      the priming state and its replenishment after release. We
                      envision that this subunit plays a role in coupling
                      exocytosis to endocytosis during the vesicle cycle.},
      cin          = {ICS-4},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ICS-4-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000467474200001},
      doi          = {10.3389/fncel.2019.00125},
      url          = {https://juser.fz-juelich.de/record/862133},
}