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First published online 16 November 2004
doi: 10.1242/jcs.01529

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

¹ Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, Department of Medical Biochemistry, Medical University of Vienna, 1030 Vienna, Austria
² Gene Expression and Cell Biology/Biophysics Programmes, European Molecular Biology Laboratory, 69117 Heidelberg, Germany
³ CREST of JST Kansai Advanced Research Center, Kobe 651-2492, Japan
⁴ Department of Chemistry, Faculty of Sciences, Niigata University, Niigata 950-2181, Japan

^* Author for correspondence (e-mail: roland.foisner{at}meduniwien.ac.at)

Accepted 10 September 2004

Lamina-associated polypeptide (LAP) 2 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 was mostly cytoplasmic in metaphase and associated with telomeres in anaphase. Telomeric LAP2 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 to the core region early on, whereas LAP2ß, 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 in vitro and in mitotic extracts, and subfractions of BAF relocalized to core structures with LAP2. We propose that LAP2 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.

Key words: Chromosomes, Lamins, Mitosis, Nuclear assembly, Nuclear envelope

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