Molecular and Cellular Biochemistry

, Volume 320, Issue 1, pp 53–66

Truncated form of tenascin-X, XB-S, interacts with mitotic motor kinesin Eg5

  • Toshiya Endo
  • Hiroyoshi Ariga
  • Ken-ichi Matsumoto

DOI: 10.1007/s11010-008-9898-y

Cite this article as:
Endo, T., Ariga, H. & Matsumoto, K. Mol Cell Biochem (2009) 320: 53. doi:10.1007/s11010-008-9898-y


XB-S is a protein with an amino-terminal-truncated form of tenascin-X (TNXB). However, the precise roles of XB-S in vivo are unknown. In this study, to determine the role of XB-S in vivo, we screened XB-S-binding proteins. FLAG-tagged XB-S was transiently introduced into 293T cells. Then its associated proteins were purified by immunoprecipitation using an anti-FLAG antibody and its components were identified by mass spectrometric analyses. Mitotic motor kinesin Eg5 was identified in the immunoprecipitates. XB-S and Eg5 proteins were co-localized in the cytoplasm in interphase and mitosis, but XB-S did not localize on mitotic spindle microtubules, on which Eg5 prominently localized in mitosis. As for Eg5 binding to XB-S, glutathione S-transferase-fused XB-S expressed in vitro directly bound to full-length Eg5 translated in reticulocyte lysate, and the XB-S-binding region was located in the motor domain of Eg5. Furthermore, during cell cycle progression XB-S showed a similar expression profile to that of Eg5. These results suggest possible involvement of XB-S in the function of Eg5.



Copyright information

© Springer Science+Business Media, LLC. 2008

Authors and Affiliations

  • Toshiya Endo
    • 1
  • Hiroyoshi Ariga
    • 2
  • Ken-ichi Matsumoto
    • 3
  1. 1.Graduate School of Life ScienceHokkaido UniversitySapporoJapan
  2. 2.Department of Molecular Biology, Graduate School of Pharmaceutical SciencesHokkaido UniversitySapporoJapan
  3. 3.Laboratory of Molecular Biology, Faculty of Advanced Life ScienceHokkaido UniversitySapporoJapan