Program

Poster Presentations

Day 4, May 18（Fri.）　　Poster

4P-30　　PDF

Quantitative evaluation of the interaction of NF1 factor TCTP dimer with translation elongation factors by SWATH

(Kumamoto Univ.)
^oTakaho Tokuda, Daiki Kobayashi, Hiroki Okanishi, Norie Araki

Neurofibromatosis type 1 (NF1) is an autosomal dominant disease that predisposes individuals to developing benign neurofibromas and malignant peripheral nerve sheath tumors (MPNST). The mechanism of NF1-tumoigenesis or the curatives have not been established. We previously found that translationally controlled tumor protein (TCTP) is a novel biological target for NF1-associated tumors (Kobayashi et al. MCP 2013, JBC 2014). Moreover, TCTP-interacting proteins was identified and their biological function was studied to examine roles of TCTP in NF1-associated tumors in detail (Kobayashi et al. MCP 2018, submitted). These findings indicate that TCTP contribute to the unique protein translation machinery regulating the NF1-associated tumor cell growth. To investigate the significance of TCTP conformation for the translation machinery, we substituted Cys28 or Cys172, which mediates the TCTP dimer formation, to serine, and identified wild-type TCTP- or TCTP/C28S-, TCTP/C172S-interacting proteins by affinity purification using FLAG-tag system and SWATH. Consequently, the binding activity of TCTP/C28S with translation elongation factors, such as EF1B, EF1D, EF1G, and VARS is significantly reduced in compared with wild-type TCTP-interacting proteins. These findings suggest that TCTP Cys28-mediated dimer structure is important for the binding activities with translation elongation factors to form unique protein translation machinery regulating NF1-associated tumor cell growth.