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@ARTICLE{Comini:910204,
      author       = {Comini, Maddalena and Sierra-Marquez, Juan and Guzman,
                      Gustavo and Franzen, Arne and Willuweit, Antje and Katona,
                      Istvan and Hidalgo, Patricia and Fahlke, Christoph and
                      Guzman, Raul E.},
      title        = {{CLC} {A}nion/{P}roton {E}xchangers {R}egulate {S}ecretory
                      {V}esicle {F}illing and {G}ranule {E}xocytosis in
                      {C}hromaffin {C}ells},
      journal      = {The journal of neuroscience},
      volume       = {42},
      number       = {15},
      issn         = {0270-6474},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2022-03681},
      pages        = {3080-3095},
      year         = {2022},
      abstract     = {ClC-3, ClC-4, and ClC-5 are electrogenic chloride/proton
                      exchangers that can be found in endosomal compartments of
                      mammalian cells. Although the association with genetic
                      diseases and the severe phenotype of knock-out animals
                      illustrate their physiological importance, the cellular
                      functions of these proteins have remained insufficiently
                      understood. We here study the role of two Clcn3 splice
                      variants, ClC-3b and ClC-3c, in granular exocytosis and
                      catecholamine accumulation of adrenal chromaffin cells using
                      a combination of high-resolution capacitance measurements,
                      amperometry, protein expression/gene knock out/down, rescue
                      experiments, and confocal microscopy. We demonstrate that
                      ClC-3c resides in immature as well as in mature secretory
                      granules, where it regulates catecholamine accumulation and
                      contributes to the establishment of the readily releasable
                      pool of secretory vesicles. The lysosomal splice variant
                      ClC-3b contributes to vesicle priming only with low
                      efficiency and leaves the vesicular catecholamine content
                      unaltered. The related Cl−/H+ antiporter ClC-5 undergoes
                      age-dependent downregulation in wild-type conditions. Its
                      upregulation in Clcn3−/− cells partially rescues the
                      exocytotic mutant defect. Our study demonstrates how
                      different CLC transporters with similar transport functions,
                      but distinct localizations can contribute to vesicle
                      functions in the regulated secretory pathway of granule
                      secretion in chromaffin cells.},
      cin          = {INM-4 / IBI-1 / IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)INM-4-20090406 / I:(DE-Juel1)IBI-1-20200312 /
                      I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5253 - Neuroimaging (POF4-525) / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5253 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35241492},
      UT           = {WOS:000789016600003},
      doi          = {10.1523/JNEUROSCI.2439-21.2022},
      url          = {https://juser.fz-juelich.de/record/910204},
}