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@ARTICLE{Nouri:823899,
      author       = {Nouri, Kazem and Fansa, Eyad K. and Amin, Ehsan and
                      Dvorsky, Radovan and Gremer, Lothar and Willbold, Dieter and
                      Schmitt, Lutz and Timson, David J. and Ahmadian, Mohammad
                      R.},
      title        = {{IQGAP}1 interaction with {RHO} family proteins revisited:
                      {K}inetic and equilibrium evidence for multiple distinct
                      binding sites},
      journal      = {The journal of biological chemistry},
      volume       = {291},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2016-06531},
      pages        = {26364-26376},
      year         = {2016},
      abstract     = {IQ motif-containing GTPase activating protein 1 (IQGAP1)
                      plays a central role in the physical assembly of relevant
                      signaling networks that are responsible for various cellular
                      processes, including cell adhesion, polarity and
                      transmigration. The RHO family proteins CDC42 and RAC1, have
                      been shown to mainly interact with the GAPrelated domain
                      (GRD) of IQGAP1. However, the role of its RASGAP C-terminal
                      (RGCT) and C-terminal (CT) domains in the interactions with
                      RHO proteins has remained obscure. Here, we demonstrate that
                      IQGAP1 interactions with RHO proteins underly a
                      multiple-step binding mechanism: (i) a high-affinity,
                      GTPdependent binding of RGCT to the switch regions of CDC42
                      or RAC1, and (ii) a very low-affinity binding of GRD and CT
                      adjacent to the switch regions. These data were confirmed by
                      phosphomimetic mutation of serine 1443 to glutamate within
                      RGCT, which led to a significant reduction of IQGAP1
                      affinity for CDC42 and RAC1, clearly disclosing the critical
                      role of RGCT for these interactions. Unlike CDC42, an
                      extremely low affinity was determined for the RAC1-GRD
                      interaction, suggesting that the molecular nature of IQGAP1
                      interaction with CDC42 partially differs from that of RAC1.
                      Our study provides new insights into the interaction
                      characteristics of IQGAP1 with RHO family proteins and
                      highlights the complementary importance of kinetic and
                      equilibrium analyses. We propose that the ability of IQGAP1
                      to interact with RHO proteins is based on a multiple-step
                      binding process, which is a prerequisite for the dynamic
                      functions of IQGAP1 as a scaffolding protein and a critical
                      mechanism in temporal regulation and integration of
                      IQGAP1-mediated cellular responses.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000391568200011},
      pubmed       = {pmid:27815503},
      doi          = {10.1074/jbc.M116.752121},
      url          = {https://juser.fz-juelich.de/record/823899},
}