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@ARTICLE{Conrad:892411,
      author       = {Conrad, Rachel and Kortzak, Daniel and Guzman, Gustavo A.
                      and Miranda-Laferte, Erick and Hidalgo, Patricia},
      title        = {{C}a {V} β controls the endocytic turnover of {C}a {V} 1
                      .2 {L}‐type calcium channel},
      journal      = {Traffic},
      volume       = {22},
      number       = {6},
      issn         = {1600-0854},
      address      = {Oxford},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2021-02069},
      pages        = {180-193},
      year         = {2021},
      abstract     = {Membrane depolarization activates the multisubunit CaV1.2
                      L-type calcium channel initiating various excitation
                      coupling responses. Intracellular trafficking into and out
                      of the plasma membrane regulates the channel's surface
                      expression and stability, and thus, the strength of
                      CaV1.2-mediated Ca2+ signals. The mechanisms regulating the
                      residency time of the channel at the cell membrane are
                      unclear. Here, we coexpressed the channel core complex
                      CaV1.2α1 pore-forming and auxiliary CaVβ subunits and
                      analyzed their trafficking dynamics from
                      single-particle-tracking trajectories. Speed histograms
                      obtained for each subunit were best fitted to a sum of
                      diffusive and directed motion terms. The same mean speed for
                      the highest-mobility state underlying directed motion was
                      found for all subunits. The frequency of this component
                      increased by covalent linkage of CaVβ to CaV1.2α1
                      suggesting that high-speed transport occurs in association
                      with CaVβ. Selective tracking of CaV1.2α1 along the
                      postendocytic pathway failed to show the highly mobile
                      state, implying CaVβ-independent retrograde transport.
                      Retrograde speeds of CaV1.2α1 are compatible with myosin
                      VI-mediated backward transport. Moreover, residency time at
                      the cell surface was significantly prolonged when CaV1.2α1
                      was covalently linked to CaVβ. Thus, CaVβ promotes fast
                      transport speed along anterograde trafficking and acts as a
                      molecular switch controlling the endocytic turnover of
                      L-type calcium channels.},
      cin          = {IBI-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-1-20200312},
      pnm          = {524 - Molecular and Cellular Information Processing
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-524},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33890356},
      UT           = {WOS:000647262700001},
      doi          = {10.1111/tra.12788},
      url          = {https://juser.fz-juelich.de/record/892411},
}