Phosphorylation of the nuclear lamins during interphase and mitosis.
Phosphorylation of the nuclear lamins during interphase and mitosis.
复制标题
间期和有丝分裂期间核纤层蛋白的磷酸化。
DOI:
--
复制
发表时间:
1985
影响因子:
4.8
通讯作者:
L. Gerace
中科院分区:
文献类型:
--
作者:
Y. Ottaviano;L. Gerace
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.