Identification of a conserved phosphorylation site modulating nuclear lamin polymerization.
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.
Stuurman
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Department of Pharmacological Sciences, SUNY at Stony Brook, NY 11794-8651, USA. Stuurman@ubaclu.unibas.ch
D000595:Amino Acid Sequence; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D004330:Drosophila; D029721:Drosophila Proteins; D004926:Escherichia coli; D006801:Humans; D034882:Lamins; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D029721:Drosophila Proteins; C440328:Lam protein, Drosophila; D034882:Lamins; D009687:Nuclear Proteins; D010446:Peptide Fragments; D011994:Recombinant Proteins; D017868:Cyclic AMP-Dependent Protein Kinases