IN-VITRO INTERACTION OF THE CARBOXY-TERMINAL DOMAIN OF LAMIN-A WITH ACTIN

Citation
Amj. Sasseville et Y. Langelier, IN-VITRO INTERACTION OF THE CARBOXY-TERMINAL DOMAIN OF LAMIN-A WITH ACTIN, FEBS letters, 425(3), 1998, pp. 485-489
Citations number
34
Categorie Soggetti
Biology,"Cell Biology",Biophysics
Journal title
ISSN journal
00145793
Volume
425
Issue
3
Year of publication
1998
Pages
485 - 489
Database
ISI
SICI code
0014-5793(1998)425:3<485:IIOTCD>2.0.ZU;2-H
Abstract
The nuclear lamina formed by lamins is localized between the inner nuc lear membrane and chromatin, Lamins are thought to be implicated in th e higher order chromatin structure. Interactions of lamins with chroma tin have been described but the molecular components directly involved in these interactions remain to be identified. Using a GST-C-terminal domain of lamin A fusion protein to probe cellular extracts for inter acting proteins, we have found that this domain of lamin A binds to nu clear actin. This result suggests that an actin-based molecular motor linked to the lamina could be involved in the movement of chromatin do mains. (C) 1998 Federation of European Biochemical Societies.