title: In vitro interaction of the carboxy-terminal domain of lamin A with actin.
abstract: The nuclear lamina formed by lamins is localized between the inner nuclear membrane and chromatin. Lamins are thought to be implicated in the higher order chromatin structure. Interactions of lamins with chromatin 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 interacting proteins, we have found that this domain of lamin A binds to nuclear actin. This result suggests that an actin-based molecular motor linked to the lamina could be involved in the movement of chromatin domains.
authors.affiliation: Centre de Recherche du Centre Hospitalier de l'Université de Montréal and Institut du Cancer de Montréal, Qué., Canada.
authors.forename: A M
authors.initials: AM
authors.lastname: Sasseville
authors.forename: Y
authors.initials: Y
authors.lastname: Langelier
mesh_terms: D000199:Actins / Q000378:metabolism*; D002458:Cell Fractionation; D002843:Chromatin / Q000378:metabolism; D006801:Humans; D034904:Lamin Type A; D034882:Lamins; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014407:Tumor Cells, Cultured
chemical_list: D000199:Actins; D002843:Chromatin; D034904:Lamin Type A; D034882:Lamins; D009687:Nuclear Proteins; D011993:Recombinant Fusion Proteins