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@ARTICLE{Thakur:139998,
      author       = {Thakur, H. C. and Singh, M. and Nagel-Steger, L. and
                      Kremer, J. and Prumbaum, D. and Kalawy Fansa, E. and
                      Ezzahoini, H. and Nouri, K. and Gremer, L. and Abts, A. and
                      Schmitt, L. and Raunser, S. and Ahmadian, M. R. and Piekorz,
                      R. P.},
      title        = {{T}he centrosomal adaptor {TACC}3 and the microtubule
                      polymerase ch{TOG} interact via defined {C}-terminal
                      subdomains in an {A}urora-{A} kinase independent manner},
      journal      = {The journal of biological chemistry},
      volume       = {-},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2013-05965},
      pages        = {-},
      year         = {2013},
      abstract     = {The cancer-associated, centrosomal adaptor protein TACC3
                      (Transforming Acidic Coiled-Coil 3) and its direct effector,
                      the microtubule polymerase chTOG (colonic and hepatic tumor
                      overexpressed gene), play a crucial function in
                      centrosome-driven mitotic spindle assembly. It is unclear
                      how TACC3 interacts with chTOG. Here, we show that the
                      C-terminal TACC domain of TACC3 and a C-terminal fragment
                      adjacent to the TOG domains of chTOG mediate the interaction
                      between these two proteins. Interestingly, the TACC domain
                      consists of two functionally distinct subdomains, CC1 (aa
                      414-530) and CC2 (aa 530-630). Whereas CC1 is responsible
                      for the interaction with chTOG, CC2 performs an intradomain
                      interaction with the central repeat region of TACC3, thereby
                      masking the TACC domain prior to effector binding. Contrary
                      to previous findings, our data clearly demonstrate that
                      Aurora-A kinase does not regulate TACC3-chTOG complex
                      formation, indicating that Aurora-A solely functions as a
                      recruitment factor for the TACC3-chTOG complex to
                      centrosomes and proximal mitotic spindles. We identified
                      with CC1 and CC2 two functionally diverse modules within the
                      TACC domain of TACC3 which mediate and modulate,
                      respectively, TACC3 interaction with chTOG required for
                      spindle assembly and microtubule dynamics during mitotic
                      cell division.},
      cin          = {ICS-6},
      ddc          = {570},
      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:000329370900007},
      doi          = {10.1074/jbc.M113.532333},
      url          = {https://juser.fz-juelich.de/record/139998},
}