LAP2α and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly

Author:

Dechat Thomas1,Gajewski Andreas1,Korbei Barbara1,Gerlich Daniel2,Daigle Nathalie2,Haraguchi Tokuko3,Furukawa Kazuhiro4,Ellenberg Jan2,Foisner Roland1

Affiliation:

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

Abstract

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.

Publisher

The Company of Biologists

Subject

Cell Biology

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