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Identification of a conserved phosphorylation site modulating nuclear lamin polymerization
Author(s) -
Stuurman Nico
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01464-0
Subject(s) - phosphorylation , lamin , cyclin dependent kinase 1 , microbiology and biotechnology , serine , kinase , immunoprecipitation , protein phosphorylation , biology , mitosis , protein kinase a , phosphorylation cascade , nuclear protein , biochemistry , chemistry , transcription factor , cell cycle , gene , nucleus
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 Dm 0 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.