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Published online 30 May 2006. doi:10.1083/jcb.200512107
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 5, 685-694
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Article

 TPX2 is required for postmitotic nuclear assembly in cell-free Xenopus laevis egg extracts

Lori L. O'Brien and Christiane Wiese

Department of Biochemistry, University of Wisconsin–Madison, Madison, WI 53706

Correspondence to Christiane Wiese: wiese{at}biochem.wisc.edu

Cell division in many metazoa is accompanied by the disassembly of the nuclear envelope and the assembly of the mitotic spindle. These dramatic structural rearrangements are reversed after mitosis, when the mitotic spindle is dismantled and the nuclear envelope reassembles. The targeting protein for XKlp2 (TPX2) plays important roles in mitotic spindle assembly. We report that TPX2 depletion from nuclear assembly extracts prepared from Xenopus laevis eggs results in the formation of nuclei that are only about one fifth the size of control nuclei. TPX2-depleted nuclei assemble nuclear envelopes, nuclear pore complexes, and a lamina, and they perform nuclear-specific functions, including DNA replication. We show that TPX2 interacts with lamina-associated polypeptide 2 (LAP2), a protein known to be required for nuclear assembly in interphase extracts and in vitro. LAP2 localization is disrupted in TPX2-depleted nuclei, suggesting that the interaction between TPX2 and LAP2 is required for postmitotic nuclear reformation.

Abbreviations used in this paper: DHCC, 3,3'-dihexyloxacarbocyanine; IIF, indirect immunofluorescence; LAP, lamina-associated polypeptide; NE, nuclear envelope; NPC, nuclear pore complex.


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