In vitro interaction of the carboxy-terminal domain of lamin A with actin
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 interactio...
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| Veröffentlicht in: | FEBS letters 1998-04, Vol.425 (3), p.485-489 |
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| container_title | FEBS letters |
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| creator | Sasseville, A.Marie-Josée Langelier, Yves |
| description | 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. |
| doi_str_mv | 10.1016/S0014-5793(98)00294-4 |
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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. 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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.</description><subject>Actin</subject><subject>Actins - metabolism</subject><subject>Cell Fractionation</subject><subject>Chromatin - metabolism</subject><subject>GST, glutathione S-transferase</subject><subject>Humans</subject><subject>Lamin</subject><subject>Lamin Type A</subject><subject>Lamins</subject><subject>mAb, monoclonal antibody</subject><subject>NP-40, Nonidet P-40</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - metabolism</subject><subject>Protein Binding - physiology</subject><subject>Protein interaction</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Tumor Cells, Cultured</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEtPxCAUhYnRjOPjJ5iwMrqoQoEWVkaNj0kmcaGuCdA7EdMWhY7j_HvbzsStrgj3O-fcm4PQCSUXlNDi8pkQyjNRKnam5DkhueIZ30FTKkuWMV7IXTT9leyjg5TeSf-XVE3QRImCCSqnaDZr8ZfvYsC-7SAa1_nQ4rDA3RtgZ6IN3-usB41vTY2r0Bg_4tr0E3yNV757w4OrPUJ7C1MnON6-h-j1_u7l9jGbPz3Mbq_nmeO54JlZcCGNcyAsy60AbqWklriyqDgUyjpHJRBOeMUYp4pRJwtuLSsJy4XljB2i003uRwyfS0idbnxyUNemhbBMulSSCpXLXig2QhdDShEW-iP6xsS1pkQPFeqxQj30o5XUY4Wa976T7YKlbaD6dW076_njhq98Dev_her7u5t8JANQchwPq642UdAX9uUh6uQ8tA4qH8F1ugr-j2N_AIuTk4Y</recordid><startdate>19980403</startdate><enddate>19980403</enddate><creator>Sasseville, A.Marie-Josée</creator><creator>Langelier, Yves</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19980403</creationdate><title>In vitro interaction of the carboxy-terminal domain of lamin A with actin</title><author>Sasseville, A.Marie-Josée ; Langelier, Yves</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4254-af458acce5b32b5e4b881b0c76d4e69bcc18e0404d3341931c864bb370325b433</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Actin</topic><topic>Actins - metabolism</topic><topic>Cell Fractionation</topic><topic>Chromatin - metabolism</topic><topic>GST, glutathione S-transferase</topic><topic>Humans</topic><topic>Lamin</topic><topic>Lamin Type A</topic><topic>Lamins</topic><topic>mAb, monoclonal antibody</topic><topic>NP-40, Nonidet P-40</topic><topic>Nuclear Proteins - chemistry</topic><topic>Nuclear Proteins - metabolism</topic><topic>Protein Binding - physiology</topic><topic>Protein interaction</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sasseville, A.Marie-Josée</creatorcontrib><creatorcontrib>Langelier, Yves</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sasseville, A.Marie-Josée</au><au>Langelier, Yves</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In vitro interaction of the carboxy-terminal domain of lamin A with actin</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1998-04-03</date><risdate>1998</risdate><volume>425</volume><issue>3</issue><spage>485</spage><epage>489</epage><pages>485-489</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The nuclear lamina formed by lamins is localized between the inner nuclear membrane and chromatin. 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| ispartof | FEBS letters, 1998-04, Vol.425 (3), p.485-489 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Actin Actins - metabolism Cell Fractionation Chromatin - metabolism GST, glutathione S-transferase Humans Lamin Lamin Type A Lamins mAb, monoclonal antibody NP-40, Nonidet P-40 Nuclear Proteins - chemistry Nuclear Proteins - metabolism Protein Binding - physiology Protein interaction Recombinant Fusion Proteins - metabolism Tumor Cells, Cultured |
| title | In vitro interaction of the carboxy-terminal domain of lamin A with actin |
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