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@ARTICLE{Lizarrondo:470981,
      author       = {Lizarrondo, Javier and Klebl, David P. and Niebling,
                      Stephan and Abella, Marc and Schroer, Martin A. and Mertens,
                      Haydyn D. T. and Veith, Katharina and Thuenauer, Roland and
                      Svergun, Dmitri I. and Skruzny, Michal and Sobott, Frank and
                      Muench, Stephen P. and Garcia-Alai, Maria M.},
      title        = {{S}tructure of the endocytic adaptor complex reveals the
                      basis for efficient membrane anchoring during
                      clathrin-mediated endocytosis},
      journal      = {Nature Communications},
      volume       = {12},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2021-04298},
      pages        = {2889 (1-15)},
      year         = {2021},
      abstract     = {During clathrin-mediated endocytosis, a complex and dynamic
                      network of protein-membrane interactions cooperate to
                      achieve membrane invagination. Throughout this process in
                      yeast, endocytic coat adaptors, Sla2 and Ent1, must remain
                      attached to the plasma membrane to transmit force from the
                      actin cytoskeleton required for successful membrane
                      invagination. Here, we present a cryo-EM structure of a
                      16-mer complex of the ANTH and ENTH membrane-binding domains
                      from Sla2 and Ent1 bound to PIP$_2$ that constitutes the
                      anchor to the plasma membrane. Detailed in vitro and in vivo
                      mutagenesis of the complex interfaces delineate the key
                      interactions for complex formation and deficient cell growth
                      phenotypes demonstrate its biological relevance. A
                      hetero-tetrameric unit binds PIP$_2$ molecules at the
                      ANTH-ENTH interfaces and can form larger assemblies to
                      contribute to membrane remodeling. Finally, a time-resolved
                      small-angle X-ray scattering study of the interaction of
                      these adaptor domains in vitro suggests that ANTH and ENTH
                      domains have evolved to achieve a fast subsecond timescale
                      assembly in the presence of PIP$_2$ and do not require
                      further proteins to form a stable complex. Together, these
                      findings provide a molecular understanding of an essential
                      piece in the molecular puzzle of clathrin-coated endocytic
                      sites.},
      cin          = {EMBL-User / CSSB-EMBL / EMBL / CSSB-CF-SPC},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814 /
                      I:(DE-H253)CSSB-EMBL-20141216 / I:(DE-H253)EMBL-20120731 /
                      I:(DE-H253)CSSB-CF-SPC-20210520},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34001871},
      UT           = {WOS:000658736500001},
      doi          = {10.1038/s41467-021-23151-7},
      url          = {https://bib-pubdb1.desy.de/record/470981},
}