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

Autor:	M, Eggert, N, Radomski, D, Tripier, P, Traub, E, Jost
Rok vydání:	1991
Předmět:	Molecular Sequence Data Nuclear Proteins Lamin Type A Lamins Mice CDC2 Protein Kinase Animals Autoradiography Electrophoresis Polyacrylamide Gel Amino Acid Sequence Phosphorylation Protein Kinases Chromatography High Pressure Liquid Protein Kinase C
Zdroj:	FEBS letters. 292(1-2)
ISSN:	0014-5793
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::a661b192d0c5f208bdd4da4e5598b58a https://pubmed.ncbi.nlm.nih.gov/1959608 Zobrazit plný text záznamu Plný text