A Role for Nuclear Lamins in Nuclear Envelope Assembly

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,...

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Bibliographic Details
Published in:The Journal of cell biology 2001-07, Vol.154 (1), p.61-70
Main Authors: Lopez-Soler, Reynold I., Moir, Robert D., Spann, Timothy P., Stick, Reimer, Goldman, Robert D.
Format: Article
Language:English
Subjects:
Animals
Antibodies
Cell division
Cell Nucleus - metabolism
Cellular biology
Chromatin
Chromatin - metabolism
Chromosomes - metabolism
Electrophoresis, Polyacrylamide Gel
Fluorescence
Immunoblotting
Intermediate Filament Proteins - chemistry
Intermediate Filament Proteins - physiology
Interphase
Lamin Type B
Lamins
Male
Membranes
Microscopy, Electron
Molecules
Nuclear Envelope - chemistry
Nuclear Envelope - metabolism
Nuclear lamina
Nuclear membrane
Nuclear pore
Nuclear Proteins - chemistry
Nuclear Proteins - physiology
P branes
Peptides
Protein Structure, Tertiary
Spermatozoa
Spermatozoa - metabolism
Xenopus - embryology
Xenopus - metabolism
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Summary: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.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.200101025