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First published online January 24, 2007
doi: 10.1242/10.1242/jcs.03355

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Lamin B receptor plays a role in stimulating nuclear envelope production and targeting membrane vesicles to chromatin during nuclear envelope assembly through direct interaction with importin β

The Key Laboratory of Cell Proliferation and Differentiation of Ministry of Education, The National Key Laboratory of Bio-membrane and Membrane Biotechnology, the College of Life Sciences, Peking University, Beijing 100871, China

^* Authors for correspondence (e-mail: qingjiang{at}pku.edu.cn; zhangcm{at}pku.edu.cn)

Accepted 21 November 2006

Lamin B receptor (LBR), a chromatin and lamin binding protein in the inner nuclear membrane, has been proposed to play a vital role in nuclear envelope (NE) assembly. But the specific role for LBR in NE assembly remains unknown. In the present study, we show that overexpression of LBR causes membrane overproduction, inducing NE invagination and membrane stack formation, and that these processes require the transmembrane domain of LBR. Biochemical analysis shows that the N-terminal domain of LBR directly interacts with importin β in a Ran sensitive and importin independent manner. Using an in vitro NE assembly assay, we also demonstrate that blocking full length LBR binding sites on importin β, by the addition of the LBR N-terminal domain inhibits the recruitment of LBR-containing vesicles to importin β- or Ran-coated beads to form NE structure. Our results suggest that LBR is recruited to chromatin through direct interaction with importin β to contribute to the fusion of membrane vesicles and formation of the NE.

Key words: Nuclear envelope assembly, Lamin B receptor, Importin β, Ran GTPase

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