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Characterization of A 54-kD protein of the inner nuclear membrane : evidence for cell cycle-dependent interaction with the nuclear lamina

Bailer, S. M. and Eppenberger, H. M. and Griffiths, G. and Nigg, E. A.. (1991) Characterization of A 54-kD protein of the inner nuclear membrane : evidence for cell cycle-dependent interaction with the nuclear lamina. The Journal of cell biology, Vol. 114, H. 3. S. 389-400.

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Official URL: http://edoc.unibas.ch/dok/A5249489

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Abstract

Using a mAb (R-7), we have characterized a 54-kD protein of the chicken nuclear envelope. Based on its biochemical properties and subnuclear distribution p54 is likely to be an integral membrane component specific to the inner nuclear membrane. Fractionation experiments indicate that p54 interacts, directly or indirectly, with the nuclear lamina, and analysis of p54 in cultured cells suggests that this interaction is controlled by cell cycle-dependent posttranslational modification, most likely phosphorylation. Modification of p54 results in a slightly reduced electrophoretic mobility, and it converts the protein from a detergent-resistant to a detergent-extractable form. Detergent solubilization of p54 can be induced in vivo by treating isolated nuclei or nuclear envelopes with highly purified cdc2 kinase, one of the most prominent kinases active in mitotic cells. These results suggest that mitotic phosphorylation of p54 might contribute to control nuclear envelope dynamics during mitosis in vivo.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum
05 Faculty of Science > Departement Biozentrum > Growth & Development > Cell Biology (Nigg)
UniBasel Contributors:Nigg, Erich A.
Item Type:Article, refereed
Bibsysno:Link to catalogue
Publisher:Rockefeller University Press
ISSN:0021-9525
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:05 Jan 2016 10:44
Deposited On:22 Mar 2012 13:17

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