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@ARTICLE{Defelipe:619947,
      author       = {Defelipe, Lucas A. and Veith, Katharina and Burastero,
                      Osvaldo and Kupriianova, Tatiana and Bento, Isabel and
                      Skruzny, Michal and Koelbel, Knut and Uetrecht, Charlotte
                      and Thuenauer, Roland and García-Alai, Maria M.},
      title        = {{S}ubtleties in {C}lathrin heavy chain binding boxes
                      provide selectivity among adaptor proteins of budding yeast},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2024-08038},
      pages        = {9655},
      year         = {2024},
      abstract     = {Clathrin forms a triskelion, or three-legged, network that
                      regulates cellular processes by facilitating cargo
                      internalization and trafficking in eukaryotes. Its
                      N-terminal domain is crucial for interacting with adaptor
                      proteins, which link clathrin to the membrane and engage
                      with specific cargo. The N-terminal domain contains up to
                      four adaptor-binding sites, though their role in
                      preferential occupancy by adaptor proteins remains unclear.
                      In this study, we examine the binding hierarchy of adaptors
                      for clathrin, using integrative biophysical and structural
                      approaches, along with in vivo functional experiments. We
                      find that yeast epsin Ent5 has the highest affinity for
                      clathrin, highlighting its key role in cellular trafficking.
                      Epsins Ent1 and Ent2, crucial for endocytosis but thought to
                      have redundant functions, show distinct binding patterns.
                      Ent1 exhibits stronger interactions with clathrin than Ent2,
                      suggesting a functional divergence toward actin binding.
                      These results offer molecular insights into adaptor protein
                      selectivity, suggesting they competitively bind clathrin
                      while also targeting three different clathrin sites.},
      cin          = {CSSB-LIV/DESY-CU / CSSB-CF-ALFM / CSSB-CF-SPC},
      ddc          = {500},
      cid          = {$I:(DE-H253)CSSB-LIV_DESY-CU-20220525$ /
                      I:(DE-H253)CSSB-CF-ALFM-20210629 /
                      I:(DE-H253)CSSB-CF-SPC-20210520},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P13-20150101 / EXP:(DE-H253)P-P14-20150101 /
                      EXP:(DE-H253)SPC-20250101 / EXP:(DE-H253)ALFM-20250101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39511183},
      UT           = {WOS:001352440200007},
      doi          = {10.1038/s41467-024-54037-z},
      url          = {https://bib-pubdb1.desy.de/record/619947},
}