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A correction to this article has been published: Anderson et al., J. Cell Biol. 186 (6) 929
Published online
doi:10.1083/jcb.200901106
The Journal of Cell Biology, Vol. 186, No. 2, 183-191
The Rockefeller University Press, 0021-9525 $30.00
© Anderson et al.
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Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo



Daniel J. Anderson, Jesse D. Vargas, Joshua P. Hsiao, and Martin W. Hetzer

Salk Institute for Biological Studies, Molecular and Cell Biology Laboratory, La Jolla, CA 92037

Correspondence to Martin W. Hetzer: hetzer{at}salk.edu

Formation of the nuclear envelope (NE) around segregated chromosomes occurs by the reshaping of the endoplasmic reticulum (ER), a reservoir for disassembled nuclear membrane components during mitosis. In this study, we show that inner nuclear membrane proteins such as lamin B receptor (LBR), MAN1, Lap2β, and the trans-membrane nucleoporins Ndc1 and POM121 drive the spreading of ER membranes into the emerging NE via their capacity to bind chromatin in a collaborative manner. Despite their redundant functions, decreasing the levels of any of these trans-membrane proteins by RNAi-mediated knockdown delayed NE formation, whereas increasing the levels of any of them had the opposite effect. Furthermore, acceleration of NE formation interferes with chromosome separation during mitosis, indicating that the time frame over which chromatin becomes membrane enclosed is physiologically relevant and regulated. These data suggest that functionally distinct classes of chromatin-interacting membrane proteins, which are present at nonsaturating levels, collaborate to rapidly reestablish the nuclear compartment at the end of mitosis.


D.J. Anderson and J.D. Vargas contributed equally to this paper.

Abbreviations used in this paper: BAF, barrier of autointegration factor; INM, inner nuclear membrane; LBR, lamin B receptor; LEM, Lap2/emerin/Man1; NE, nuclear envelope; NPC, nuclear pore complex; ONM, outer nuclear membrane.

© 2009 Anderson et al.
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