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Published 9 July 2001. doi:10.1083/jcb.200101025
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© The Rockefeller University Press, 0021-9525/2001/7/61 $5.00
The Journal of Cell Biology, Volume 154, Number 1, July 9, 2001 61-70

Article

A role for nuclear lamins in nuclear envelope assembly



Reynold I. Lopez-Soler1, Robert D. Moir1, Timothy P. Spann1, Reimer Stick2 and Robert D. Goldman1

1 Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, IL 60611
2 Institut für Zellbiologie, Universität Bremen, D-28334 Bremen, Germany

Address correspondence to Robert D. Goldman, Department of Cell and Molecular Biology, Northwestern University Medical School, 303 East Chicago Avenue, Chicago, IL 60611. Tel.: (312) 503-4215. Fax: (312) 503-0954. E-mail: r-goldman{at}northwestern.edu

The molecular interactions responsible for nuclear envelope assembly after mitosis are not well understood. In this study, we demonstrate that a peptide consisting of the COOH-terminal domain of Xenopus lamin B3 (LB3T) prevents nuclear envelope assembly in Xenopus interphase extracts. Specifically, LB3T inhibits chromatin decondensation and blocks the formation of both the nuclear lamina–pore complex and nuclear membranes. Under these conditions, some vesicles bind to the peripheral regions of the chromatin. These "nonfusogenic" vesicles lack lamin B3 (LB3) and do not bind LB3T; however, "fusogenic" vesicles containing LB3 can bind LB3T, which blocks their association with chromatin and, subsequently, nuclear membrane assembly. LB3T also binds to chromatin in the absence of interphase extract, but only in the presence of purified LB3. Additionally, we show that LB3T inhibits normal lamin polymerization in vitro. These findings suggest that lamin polymerization is required for both chromatin decondensation and the binding of nuclear membrane precursors during the early stages of normal nuclear envelope assembly.

Key Words: nuclear envelope; nuclear lamins; nuclear membrane; nuclear pores; nuclear assembly


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