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First published online January 10, 2008
doi: 10.1242/10.1242/jcs.022020
Research Article |
1 School of Biological and Biomedical Sciences, The University of Durham, South Road, Durham DH1 3LE, UK
2 Department of Cell Biology, University of Bremen, PO Box 33 04 40, 28334 Bremen, Germany
* Authors for correspondence (e-mail: m.w.goldberg{at}durham.ac.uk; stick{at}uni-bremen.de)
Accepted 22 October 2007
Lamins are intermediate filament proteins and the major component of the nuclear lamina. Current views of the lamina are based on the remarkably regular arrangement of lamin LIII in amphibian oocyte nuclei. We have re-examined the LIII lamina and propose a new interpretation of its organization. Rather than consisting of two perpendicular arrays of parallel filaments, we suggest that the oocyte lamina consists of parallel filaments that are interconnected in register to give the impression of a second set of perpendicular filaments. We have also used the oocyte system to investigate the organization of somatic lamins. Currently, it is not feasible to examine the organization of somatic lamins in situ because of their tight association with chromatin. It is also difficult to assemble vertebrate lamin filaments in vitro. Therefore, we have used the oocyte system, where exogenously expressed somatic B-type and A-type lamins assemble into filaments. Expression of B-type lamins induces the formation of intranuclear membranes that are covered by single filament layers. LIII filaments appear identical to the endogenous lamina, whereas lamin B2 assembles into filaments that are organized less precisely. Lamin A induces sheets of thicker filaments on the endogenous lamina and significantly increases the rigidity of the nuclear envelope.
Key words: Nuclear lamina, Lamin filaments, Xenopus oocyte, feSEM, Lamin A, B-type lamins
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