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@ARTICLE{Cao:94235,
      author       = {Cao, X. and Coskun, Ü. and Rössle, M. and Buschhorn, S.
                      B. and Grzybek, M. and Dafforn, T. R. and Lenoir, M. and
                      Overduin, M. and Simons, K. and DESY},
      title        = {{G}olgi protein {FAPP}2 tubulates membranes},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {106},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {Academy},
      reportid     = {PHPPUBDB-12319},
      pages        = {21121-21125},
      year         = {2009},
      abstract     = {The Golgi-associated four-phosphate adaptor protein 2
                      (FAPP2) has been shown to possess transfer activity for
                      glucosylceramide both in vitro and in cells. We have
                      previously shown that FAPP2 is involved in apical transport
                      from the Golgi complex in epithelial MDCK cells. In this
                      paper we assign an unknown activity for the protein as well
                      as providing structural insight into protein assembly and a
                      low-resolution envelope structure. By applying analytical
                      ultracentrifugation and small-angle x-ray scattering, we
                      show that FAPP2 is a dimeric protein in solution, having a
                      curved shape 30 nm in length. The purified FAPP2 protein has
                      the capability to form tubules from membrane sheets in
                      vitro. This activity is dependent on the
                      phosphoinositide-binding activity of the PH domain of FAPP2.
                      These data suggest that FAPP2 functions directly in the
                      formation of apical carriers in the trans-Golgi network.},
      keywords     = {Adaptor Proteins, Signal Transducing: chemistry / Adaptor
                      Proteins, Signal Transducing: metabolism / Adaptor Proteins,
                      Signal Transducing: physiology / Animals / Cell Line / Dogs
                      / Lipid Bilayers: metabolism / Phosphatidylinositols:
                      metabolism / Protein Binding / Protein Conformation /
                      Protein Multimerization / Solutions / trans-Golgi Network /
                      Adaptor Proteins, Signal Transducing (NLM Chemicals) / Lipid
                      Bilayers (NLM Chemicals) / PLEKHA8 protein, human (NLM
                      Chemicals) / Phosphatidylinositols (NLM Chemicals) /
                      Solutions (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {000},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF1-550)},
      pid          = {G:(DE-H253)POF1-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19940249},
      pmc          = {pmc:PMC2795549},
      UT           = {WOS:000272795300022},
      doi          = {10.1073/pnas.0911789106},
      url          = {https://bib-pubdb1.desy.de/record/94235},
}