PT  - JOURNAL ARTICLE
AU  - Dechat, Thomas
AU  - Gajewski, Andreas
AU  - Korbei, Barbara
AU  - Gerlich, Daniel
AU  - Daigle, Nathalie
AU  - Haraguchi, Tokuko
AU  - Furukawa, Kazuhiro
AU  - Ellenberg, Jan
AU  - Foisner, Roland
TI  - LAP2α and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly
AID  - 10.1242/jcs.01529
DP  - 2004 Dec 01
TA  - Journal of Cell Science
PG  - 6117--6128
VI  - 117
IP  - 25
4099  - http://jcs.biologists.org/content/117/25/6117.short
4100  - http://jcs.biologists.org/content/117/25/6117.full
SO  - J. Cell Sci.2004 Dec 01; 117
AB  - Lamina-associated polypeptide (LAP) 2α 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 LAP2α was mostly cytoplasmic in metaphase and associated with telomeres in anaphase. Telomeric LAP2α 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 LAP2α to the core region early on, whereas LAP2β, 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 LAP2α in vitro and in mitotic extracts, and subfractions of BAF relocalized to core structures with LAP2α. We propose that LAP2α 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.