Identification of a conserved phosphorylation site modulating nuclear lamin polymerization

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Abstract
Mitotic lamin disassembly results from phosphorylation at specific sites. In vitro, lamins can form head‐to‐tail polymers that disassemble upon phosphorylation by cdc2 kinase. A co‐immunoprecipitation assay, employing Drosophila nuclear lamin Dm0 fragments was used to study the effect of phosphorylation on head‐to‐tail binding. Phosphorylation of serine‐50 by cAMP‐dependent kinase inhibited head‐to‐tail binding in the same manner as phosphorylation of serine‐42 by cdc2 kinase. Results suggest that multiple pathways may be employed to disassemble nuclear lamins in vivo.