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@ARTICLE{Zhang:172159,
      author       = {Zhang, Si-Cai and Gremer, Lothar and Heise, Henrike and
                      Janning, Petra and Shymanets, Aliaksei and Cirstea, Ion C.
                      and Krause, Eberhard and Nürnberg, Bernd and Ahmadian,
                      Mohammad Reza},
      title        = {{L}iposome {R}econstitution and {M}odulation of
                      {R}ecombinant {P}renylated {H}uman {R}ac1 by {GEF}s, {GDI}1
                      and {P}ak1},
      journal      = {PLoS one},
      volume       = {9},
      number       = {7},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2014-05669},
      pages        = {e102425},
      year         = {2014},
      abstract     = {Small Rho GTPases are well known to regulate a variety of
                      cellular processes by acting as molecular switches. The
                      regulatory function of Rho GTPases is critically dependent
                      on their posttranslational modification at the carboxyl
                      terminus by isoprenylation and association with proper
                      cellular membranes. Despite numerous studies, the mechanisms
                      of recycling and functional integration of Rho GTPases at
                      the biological membranes are largely unclear. In this study,
                      prenylated human Rac1, a prominent member of the Rho family,
                      was purified in large amount from baculovirus-infected
                      Spodoptera frugiperda insect cells using a systematic
                      detergent screening. In contrast to non-prenylated human
                      Rac1 purified from Escherichia coli, prenylated Rac1 from
                      insect cells was able to associate with synthetic liposomes
                      and to bind Rho-specific guanine nucleotide dissociation
                      inhibitor 1 (GDI1). Subsequent liposome reconstitution
                      experiments revealed that GDI1 efficiently extracts Rac1
                      from liposomes preferentially in the inactive GDP-bound
                      state. The extraction was prevented when Rac1 was activated
                      to its GTP-bound state by Rac-specific guanine nucleotide
                      exchange factors (GEFs), such as Vav2, Dbl, Tiam1, P-Rex1
                      and TrioN, and bound by the downstream effector Pak1. We
                      found that dissociation of Rac1-GDP from its complex with
                      GDI1 strongly correlated with two distinct activities of
                      especially Dbl and Tiam1, including liposome association and
                      the GDP/GTP exchange. Taken together, our results provided
                      first detailed insights into the advantages of the in vitro
                      liposome-based reconstitution system to study both the
                      integration of the signal transducing protein complexes and
                      the mechanisms of regulation and signaling of small GTPases
                      at biological membranes.},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000339378400096},
      pubmed       = {pmid:25014207},
      doi          = {10.1371/journal.pone.0102425},
      url          = {https://juser.fz-juelich.de/record/172159},
}