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@ARTICLE{ffing:1026361,
      author       = {Üffing, Alina and Gold, Lisa and Gensch, Thomas and
                      Weiergräber, Oliver H. and Hoffmann, Silke and Willbold,
                      Dieter},
      title        = {{H}ighlighting the hidden: monitoring the avidity-driven
                      association of a fluorescent {GABARAP} tandem with
                      microtubules in living cells},
      journal      = {Autophagy reports},
      volume       = {3},
      number       = {1},
      issn         = {2769-4127},
      address      = {London},
      publisher    = {Taylor $\&$ Francis Group},
      reportid     = {FZJ-2024-03392},
      pages        = {2348899},
      year         = {2024},
      note         = {This is an Open Access article distributed under the terms
                      of the Creative Commons Attribution License
                      (http://creativecommons.org/licenses/by/4.0/), which permits
                      unrestricted use, distribution, and reproduction in any
                      medium, provided the original work is properly cited. The
                      terms on which this article has been published allow the
                      posting of the Accepted Manuscript in a repository by the
                      author(s) or with their consent.},
      abstract     = {GABARAP, like other ATG8 proteins, is a ubiquitin-like
                      modifier and its C-terminal lipid conjugation enables
                      association with cellular membranes. To prevent interference
                      with the lipidation process, N-terminal fluorescent protein
                      (FP) tagging strategies have become the standard for
                      studying ATG8 localization and function in living cells,
                      significantly contributing to our understanding of this
                      protein family’s multifaceted roles. We employed live cell
                      imaging with particular emphasis on a GABARAP split-tandem
                      construct, GABARAP(G116A)-mTagBFP2-GABARAP (G-B-G), which
                      retains both a free N-terminus and a lipidation-competent
                      c-terminus, while bivalence creates a gain in affinity
                      conferred by avidity. Notably, reminiscent of early in vitro
                      studies demonstrating an interaction of GABARAP and tubulin,
                      our results revealed a robust association of G-B-G with the
                      microtubule network in living cells. We show that the
                      presence of several basic residues in the amino-terminal
                      helical subdomain of GABARAP and avidity emerged as
                      essential for robust MT association, whereas lipidation
                      ability was not decisive. Interestingly, while the position
                      of the FP-tag had little influence on the result, the nature
                      of the FP itself was crucial, with mTagBFP2 being required
                      for tracking GABARAP tandems in the vicinity of MTs. Though
                      artificial effects cannot be excluded, we assume that G-B-G,
                      with its increased avidity, can give visibility to processes
                      that are based on inherently weak interactions, and thus can
                      help elucidate potential roles of GABARAP e.g. in
                      microtubule-associated processes that are integral to
                      autophagy-related and -unrelated cellular transport.},
      cin          = {IBI-7 / IBI-1},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)IBI-1-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / SFB 1208 B02 - Spezifische Rollen von Atg8s im
                      Vesikeltransport (B02) (289554527)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(GEPRIS)289554527},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1080/27694127.2024.2348899},
      url          = {https://juser.fz-juelich.de/record/1026361},
}