Identification of phosphorylation sites on murine nuclear lamin C by RP‐HPLC and microsequencing

4 November 1991

journal article
Published by Wiley in FEBS Letters

Vol. 292 (1-2) , 205-209
https://doi.org/10.1016/0014-5793(91)80868-4

Abstract

Isolated interphase lamin C, obtained from Ehrlich ascites tumor cells, was digested by Lys‐C endoproteinase, the resulting peptides separated by reversed‐phase HPLC and subjected to microsequencing in order to identify phosphorylation sites in interphase and following phosphorylation in vitro by cdc2‐kinase, protein kinase C (PKC) and protein kinase A (PKA), respectively. Nuclear lamin C showed partial phosphorylation of Ser³⁹² and Ser⁴⁰⁹, and possibly Ser⁴⁰⁷ in interphase. Phosphorylation was increased in response to cdc2‐kinase at Ser³⁹⁰ and Ser³⁹² and to PKC at Ser⁵⁷². The N‐terminal peptide (aa 1–32) containing consensus sequences for the 3 kinases was phosphorylated by cdc2‐kinase, PKC and PKA. The sequence data suggests that multiple molecular switches via lamina modification control the dynamic behaviour of the nucleoskeleton during the cell cycle.

Keywords

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