A role for nuclear lamins in nuclear envelope assembly

Reynold I. Lopez-Soler, Robert D. Moir, Timothy P. Spann, Reimer Stick, Robert D. Goldman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

64 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)61-70
Number of pages10
JournalJournal of Cell Biology
Issue number1
StatePublished - Jul 9 2001


  • Nuclear assembly
  • Nuclear envelope
  • Nuclear lamins
  • Nuclear membrane
  • Nuclear pores

ASJC Scopus subject areas

  • Cell Biology


Dive into the research topics of 'A role for nuclear lamins in nuclear envelope assembly'. Together they form a unique fingerprint.

Cite this