Heterodimerization with LBP-1b is necessary for nuclear localization of LBP-1a and LBP-1c

Fuyuhiko Sato, Ken Ichi Yasumoto, Kota Kimura, Keiko Numayama-Tsuruta, Kazuhiro Sogawa

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


The LBP-1 family consists of four proteins, which act as transcription factors in the formation of dimers with a member of this family. LBP-1a and LBP-1b are splicing variants from one gene, and LBP-1c and LBP-1d also arise from the alternative splicing of another gene. Investigation of subcellular localization of LBP-1 proteins fused to YFP revealed that the LBP-1b was localized in the nucleus, whereas LBP-1a and LBP-1c were exclusively localized in the cytosol. The peptide of 36 amino acids encoded by exon 6, a specific exon used only for LBP-1b, possessed the function of a nuclear localization signal (NLS). Nuclear localization of LBP-1a and LBP-1c occurred when LBP-1b was co-expressed, suggesting that heterodimerization of LBP-1a and LBP-1c with LBP-1b is important for their nuclear transport. Transiently expressed LBP-1 proteins in COS-7 cells formed speckles in the nucleus. Most speckles overlapped with the PML body. The activity of LBP-1a for accumulation in the PML body was mapped in the N-terminal region.

Original languageEnglish
Pages (from-to)861-870
Number of pages10
JournalGenes to Cells
Issue number9
Publication statusPublished - 2005 Sep

ASJC Scopus subject areas

  • Genetics
  • Cell Biology


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