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Cell. 1990 May 18;61(4):579-89.

Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis.

Author information

1
Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, Massachusetts 02115.

Abstract

The nuclear envelope is a dynamic structure that completely disassembles in response to MPF/cdc2 activity in mitosis. A key feature of this process is the hyperphosphorylation of the major structural proteins of the envelope, the nuclear lamins A, B, and C. Two highly conserved serine residues of the lamin protein (Ser-22 and Ser-392 of lamins A and C) are symmetrically positioned 5 amino acids from the ends of the large alpha-helical domain and are shown in the accompanying paper by Ward and Kirschner to be among four sites phosphorylated during nuclear envelope breakdown. Mutations in Ser-22 and Ser-392 that prevent phosphorylation at these sites block the disassembly of the nuclear lamina during mitosis. We propose a model for the regulation of lamin assembly in which phosphorylation just outside the ends of the alpha-helical domain controls the assembly dynamics of the lamin coiled-coil dimers.

PMID:
2344612
DOI:
10.1016/0092-8674(90)90470-y
[Indexed for MEDLINE]

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