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@ARTICLE{Kleusch:885997,
      author       = {Kleusch, Christian and Monzel, Cornelia and Sridhar,
                      Krishna Chander and Hoffmann, Bernd and Csiszár, Agnes and
                      Merkel, Rudolf},
      title        = {{F}luorescence {C}orrelation {S}pectroscopy {R}eveals
                      {I}nteraction of {S}ome {M}icrodomain-{A}ssociated {L}ipids
                      with {C}ellular {F}ocal {A}dhesion {S}ites},
      journal      = {International journal of molecular sciences},
      volume       = {21},
      number       = {21},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2020-04219},
      pages        = {8149 -},
      year         = {2020},
      abstract     = {Cells adhere to the extracellular matrix at distinct
                      anchoring points, mostly focal adhesions. These are rich in
                      immobile transmembrane- and cytoskeletal-associated
                      proteins, some of which are known to interact with lipids of
                      the plasma membrane. To investigate their effect on lipid
                      mobility and molecular interactions, fluorescently labeled
                      lipids were incorporated into the plasma membranes of
                      primary myofibroblasts using fusogenic liposomes. With
                      fluorescence correlation spectroscopy, we tested mobilities
                      of labeled microdomain-associated lipids such as
                      sphingomyelin (SM), ganglioside (GM1), and cholesterol as
                      well as of a microdomain-excluded phospholipid (PC) and a
                      lipid-like molecule (DiIC18(7)) in focal adhesions (FAs) and
                      in neighboring non-adherent membrane areas. We found
                      significantly slower diffusion of SM and GM1 inside FAs but
                      no effect on cholesterol, PC, and DiIC18(7). These data were
                      compared to the molecular behavior in Lo/Ld-phase separated
                      giant unilamellar vesicles, which served as a model system
                      for microdomain containing lipid membranes. In contrast to
                      the model system, lipid mobility changes in FAs were
                      molecularly selective, and no particle enrichment occurred.
                      Our findings suggest that lipid behavior in FAs cannot be
                      described by Lo/Ld-phase separation. The observed slow-down
                      of some molecules in FAs is potentially due to transient
                      binding between lipids and some molecular constituent(s).},
      cin          = {IBI-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-2-20200312},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33142729},
      UT           = {WOS:000588962900001},
      doi          = {10.3390/ijms21218149},
      url          = {https://juser.fz-juelich.de/record/885997},
}