Transactivation activity of LBP-1 proteins and their dimerization in living cells

Ayako Katsura, Kota Kimura, Kentaro Hosoi, Yosuke Tomokuni, Masanori Nesori, Kenji Goryo, Keiko Numayama-Tsuruta, Satoru Torii, Ken ichi Yasumoto, Osamu Gotoh, Mamiko Takada, Hiroshi Fukumura, Kazuhiro Sogawa

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


LBP-1 proteins form dimers and act as transcription factors that activate a number of genes related to cell growth and differentiation. LBP-1a and LBP-1c are localized in the cytoplasm when transiently expressed in cultured cells, but translocated into the nucleus after forming heterodimers with LBP-1b, which is a splicing variant of LBP-1a with an intrinsic nuclear localization signal (NLS). Here, we report that LBP-1b showed potent transactivation activity, and that forcibly expressed LBP-1a and LBP-1c in the nucleus essentially exhibited very little or no transactivation activity. Mutations in the NLS that abolished the NLS activity of LBP-1b also abrogated the transactivation activity. We have found that LBP-1 proteins contain a putative sterile alpha motif domain indispensable for their dimerization capability in the C-terminal region. To demonstrate whether homo- and heterodimers composed of LBP-1a and/or LBP-1c are generated in the nucleus, we applied the FLIM-based fluorescence resonance energy transfer imaging technique to living cells. It revealed that dimers composed of LBP-1a and LBP-1c were re-formed probably by a partner-exchange of LBP-1b-containing heterodimers.

Original languageEnglish
Pages (from-to)1183-1196
Number of pages14
JournalGenes to Cells
Issue number10
Publication statusPublished - 2009 Oct

ASJC Scopus subject areas

  • Genetics
  • Cell Biology


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