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Phosphorylation of the nuclear lamins during interphase and mitosis

Academic Article
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Overview

authors

  • Ottaviano, Y.
  • Gerace, Larry

publication date

  • 1985

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The nuclear lamina is a polymeric protein assembly that is proposed to function as an architectural framework for the nuclear envelope. Previous work suggested that phosphorylation of the major polypeptides of the lamina (the "lamins") may induce disassembly of this structure during mitosis. To further investigate the possible involvement of phosphorylation in regulation of lamina structure, we characterized lamin phosphorylation occurring in mammalian tissue culture cells during interphase and mitosis. Phosphorylation occurs continuously throughout all interphase periods (coordinately with nuclear envelope growth), and takes place mainly on the assembled lamina. When the lamina is disassembled during cell division, the lamins are modified with approximately 1-2 molecules of associated phosphate. This level of mitotic phosphorylation is 4-7-fold higher than the average interphase level. Lamin phosphate occurs predominantly as phosphoserine, and is distributed over numerous tryptic peptides, many of which are modified during both interphase and mitotic periods. Significantly, phosphorylation is the only detectable charge-altering postsynthetic modification of the lamins that occurs specifically during mitosis. The results of this study support the notion that phosphorylation is important for regulation of interphase and mitotic lamina structure.

subject areas

  • Amino Acids
  • Animals
  • Cell Cycle
  • Cell Line
  • Cell Nucleus
  • Cricetinae
  • Cricetulus
  • Female
  • Interphase
  • Lamins
  • Mitosis
  • Nucleoproteins
  • Ovary
  • Peptide Fragments
  • Phosphorylation
  • Trypsin
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 3965465
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Additional Document Info

start page

  • 624

end page

  • 632

volume

  • 260

issue

  • 1

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