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Caenorhabditis elegans BAF‐1 and its kinase VRK‐1 participate directly in post‐mitotic nuclear envelope assembly
Author(s) -
Gorjánácz Mátyás,
Klerkx Elke PF,
Galy Vincent,
Santarella Rachel,
LópezIglesias Carmen,
Askjaer Peter,
Mattaj Iain W
Publication year - 2007
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7601470
Subject(s) - biology , emerin , microbiology and biotechnology , chromatin , inner membrane , caenorhabditis elegans , lamin , mitosis , nuclear protein , rna interference , nuclear transport , cell nucleus , genetics , nucleus , gene , transcription factor , rna , mitochondrion
Barrier‐to‐autointegration factor (BAF) is an essential, highly conserved, metazoan protein. BAF interacts with LEM ( L AP2, e merin, M AN1) domain‐carrying proteins of the inner nuclear membrane. We analyzed the in vivo function of BAF in Caenorhabditis elegans embryos using both RNA interference and a temperature‐sensitive baf‐1 gene mutation and found that BAF is directly involved in nuclear envelope (NE) formation. NE defects were observed independent of and before the chromatin organization phenotype previously reported in BAF‐depleted worms and flies. We identified vaccinia‐related kinase (VRK) as a regulator of BAF phosphorylation and localization. VRK localizes both to the NE and chromatin in a cell‐cycle‐dependent manner. Depletion of VRK results in several mitotic defects, including impaired NE formation and BAF delocalization. We propose that phosphorylation of BAF by VRK plays an essential regulatory role in the association of BAF with chromatin and nuclear membrane proteins during NE formation.