RT Journal Article
SR Electronic
T1 LAP2α and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly
JF Journal of Cell Science
JO J. Cell Sci.
FD The Company of Biologists Ltd
SP 6117
OP 6128
DO 10.1242/jcs.01529
VO 117
IS 25
A1 Dechat, Thomas
A1 Gajewski, Andreas
A1 Korbei, Barbara
A1 Gerlich, Daniel
A1 Daigle, Nathalie
A1 Haraguchi, Tokuko
A1 Furukawa, Kazuhiro
A1 Ellenberg, Jan
A1 Foisner, Roland
YR 2004
UL http://jcs.biologists.org/content/117/25/6117.abstract
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.