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JCS ePress online publication date 16 Nov 2004
doi: 10.1242/jcs.01529

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Research Article

LAP2{alpha} and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly


Thomas Dechat, Andreas Gajewski, Barbara Korbei, Daniel Gerlich, Nathalie Daigle, Tokuko Haraguchi, Kazuhiro Furukawa, Jan Ellenberg, and Roland Foisner*
* Author for correspondence (e-mail: roland.foisner{at}meduniwien.ac.at)

Lamina-associated polypeptide (LAP) 2{alpha} is a LEM (lamina-associated polypeptide emerin MAN1) family protein associated with nucleoplasmic A-type lamins and chromatin. Using live cell imaging and fluorescence microscopy we demonstrate that LAP2{alpha} was mostly cytoplasmic in metaphase and associated with telomeres in anaphase. Telomeric LAP2{alpha} clusters grew in size, formed 'core' structures on chromatin adjacent to the spindle in telophase, and translocated to the nucleoplasm in G1 phase. A subfraction of lamin C and emerin followed LAP2{alpha} to the core region early on, whereas LAP2{beta}, lamin B receptor and lamin B initially bound to more peripheral regions of chromatin, before they spread to core structures with different kinetics. Furthermore, the DNA-crosslinking protein barrier-to-autointegration factor (BAF) bound to LAP2{alpha} in vitro and in mitotic extracts, and subfractions of BAF relocalized to core structures with LAP2{alpha}. We propose that LAP2{alpha} and a subfraction of BAF form defined complexes in chromatin core regions and may be involved in chromatin reorganization during early stages of nuclear assembly.


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