Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly

Tokuko Haraguchi*, Tomoko Kojidani, Takako Koujin, Takeshi Shimi, Hiroko Osakada, Chie Mori, Akitsugu Yamamoto, Yasushi Hiraoka

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

160 Scopus citations


Assembly of the nuclear envelope (NE) in telophase is essential for higher eukaryotic cells to re-establish a functional nucleus. Time-lapse, FRAP and FRET analyses in human cells showed that barrier-to-autointegration factor (BAF), a DNA-binding protein, assembled first at the distinct 'core' region of the telophase chromosome and formed an immobile complex by directly binding with other core-localizing NE proteins, such as lamin A and emerin. Correlative light and electron microscopy after five cell imaging, further showed that BAF formed an electron-dense structure on the chromosome surface of the core, close to spindle microtubules (MTs) prior to the attachment of precursor NE membranes, suggesting that MTs may mediate core assembly of BAN. Disruption of the spindle MTs consistently abolished BAF accumulation at the core. In addition, RNAi of BAF eliminated the core assembly of lamin A and emerin, caused abnormal cytoplasmic accumulation of precursor nuclear membranes and resulted in a significant delay of NE assembly. These results suggest that the MT-mediated BAF accumulation at the core facilitates NE assembly at the end of mitosis.

Original languageEnglish (US)
Pages (from-to)2540-2554
Number of pages15
JournalJournal of cell science
Issue number15
StatePublished - Aug 1 2008


  • Barrier-to-autointegration factor
  • Chromatin
  • Emerin
  • Lamin A
  • Microtubule
  • Nuclear envelope

ASJC Scopus subject areas

  • Cell Biology


Dive into the research topics of 'Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly'. Together they form a unique fingerprint.

Cite this