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@ARTICLE{Lpez:454621,
      author       = {López, David Massa and Kählau, Lea and Jungnickel,
                      Katharina Esther Julia and Loew, Christian and Damme,
                      Markus},
      title        = {{C}haracterization of the complex of the lysosomal membrane
                      transporter {MFSD}1 and its accessory subunit {GLMP}},
      journal      = {The FASEB journal},
      volume       = {34},
      number       = {11},
      issn         = {1530-6860},
      address      = {Hoboken, NJ},
      publisher    = {Wiley},
      reportid     = {PUBDB-2021-00623},
      pages        = {14695 - 14709},
      year         = {2020},
      abstract     = {The two lysosomal integral membrane proteins MFSD1 and GLMP
                      form a tight complex that confers protection of both
                      interaction partners against lysosomal proteolysis. We here
                      refined the molecular interaction of the two proteins and
                      found that the luminal domain of GLMP alone, but not its
                      transmembrane domain or its short cytosolic tail, conveys
                      protection and mediates the interaction with MFSD1. Our data
                      support the finding that the interaction is essential for
                      the stabilization of the complex. These results are
                      complemented by the observation that N‐glycosylation of
                      GLMP in general, but not the type of N‐glycans
                      (high‐mannose‐type or complex‐type) or individual
                      N‐glycan chains, are essential for protection. We observed
                      that the interaction of both proteins already starts in the
                      endoplasmic reticulum, and quantitatively depends on each
                      other. Both proteins can affect vice versa their
                      intracellular trafficking to lysosomes in addition to the
                      protection from proteolysis. Finally, we provide evidence
                      that MFSD1 can form homodimers both in vitro and in vivo.
                      Our data refine the complex interplay between an intimate
                      couple of a lysosomal transporter and its accessory
                      subunit.},
      cin          = {CSSB-GS / CSSB-EMBL-CL},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-GS-20140311 /
                      I:(DE-H253)CSSB-EMBL-CL-20210806},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32959924},
      UT           = {WOS:000573860500001},
      doi          = {10.1096/fj.202000912RR},
      url          = {https://bib-pubdb1.desy.de/record/454621},
}