Nuclear Localization of C-Terminal Domains of the Kinesin-like Protein MKLP-1
The successful execution of mitosis in mammalian cells requires the activities of numerous kinesin-like proteins. The Mitotic Kinesin-Like Protein-1 (MKLP-1) localizes to the spindle equator and is believed to participate in the separation of spindle poles during anaphase B. Injection of antibodies...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1999-07, Vol.260 (3), p.605-608 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Deavours, B.E. Walker, R.A. |
| description | The successful execution of mitosis in mammalian cells requires the activities of numerous kinesin-like proteins. The Mitotic Kinesin-Like Protein-1 (MKLP-1) localizes to the spindle equator and is believed to participate in the separation of spindle poles during anaphase B. Injection of antibodies against MKLP-1 into dividing cells results in cell cycle arrest, suggesting that MKLP-1 is essential for mitosis. To further characterize MKLP-1, constructs encoding C-terminal domains of MKLP-1 were expressed as fusions to the green fluorescent protein and localized in HeLa cells. All constructs localized to the nucleus indicating the presence of at least one nuclear localization sequence in the C-terminus of the protein. C-terminal domains of MKLP-1 expressed in insect cells also localized to the nucleus as shown by subcellular fractionation. These proteins remained tightly associated with the nucleus following both detergent and salt extraction, suggesting a tight interaction with a component of the nucleus. |
| doi_str_mv | 10.1006/bbrc.1999.0952 |
| format | Article |
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The Mitotic Kinesin-Like Protein-1 (MKLP-1) localizes to the spindle equator and is believed to participate in the separation of spindle poles during anaphase B. Injection of antibodies against MKLP-1 into dividing cells results in cell cycle arrest, suggesting that MKLP-1 is essential for mitosis. To further characterize MKLP-1, constructs encoding C-terminal domains of MKLP-1 were expressed as fusions to the green fluorescent protein and localized in HeLa cells. All constructs localized to the nucleus indicating the presence of at least one nuclear localization sequence in the C-terminus of the protein. C-terminal domains of MKLP-1 expressed in insect cells also localized to the nucleus as shown by subcellular fractionation. 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The Mitotic Kinesin-Like Protein-1 (MKLP-1) localizes to the spindle equator and is believed to participate in the separation of spindle poles during anaphase B. Injection of antibodies against MKLP-1 into dividing cells results in cell cycle arrest, suggesting that MKLP-1 is essential for mitosis. To further characterize MKLP-1, constructs encoding C-terminal domains of MKLP-1 were expressed as fusions to the green fluorescent protein and localized in HeLa cells. All constructs localized to the nucleus indicating the presence of at least one nuclear localization sequence in the C-terminus of the protein. C-terminal domains of MKLP-1 expressed in insect cells also localized to the nucleus as shown by subcellular fractionation. These proteins remained tightly associated with the nucleus following both detergent and salt extraction, suggesting a tight interaction with a component of the nucleus.</description><subject>Animals</subject><subject>Biological Transport</subject><subject>Cell Fractionation</subject><subject>Cell Line</subject><subject>Cell Nucleus - metabolism</subject><subject>Detergents</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>kinesin</subject><subject>microtubule</subject><subject>Microtubule-Associated Proteins - chemistry</subject><subject>Microtubule-Associated Proteins - genetics</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>mitosis</subject><subject>motor</subject><subject>nuclear localization</subject><subject>Nuclear Localization Signals</subject><subject>Nuclear Matrix - metabolism</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Salts</subject><subject>Sequence Deletion</subject><subject>Spodoptera - cytology</subject><subject>Spodoptera - genetics</subject><subject>Transfection</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0EoqWwMqJMbAm2k9jxiMqnmkKHIrFZjnMRhiQGO0GCX0-idGBBTHe697l3eBA6JTgiGLOLonA6IkKICIuU7qE5wQKHlOBkH83xQIRUkOcZOvL-FWNCEiYO0WyIcZyReI7WD72uQbkgt1rV5lt1xraBrYJluAXXmFbVwZVtlGn9eO1eIFiZFrxpw9q8QbBxtgPTButVvgnJMTqoVO3hZDcX6Onmeru8C_PH2_vlZR7qmJMupABVAgUrM6VZxQA05arQqcgo5wIzBkRnpBClSFNRlDoWoioyrpNhIVpU8QKdT73vzn704DvZGK-hrlULtveSiSzjLE7-BQmnjKWUD2A0gdpZ7x1U8t2ZRrkvSbAcTcvRtBxNy9H08HC2a-6LBspf-KR2ALIJgEHEpwEnvTbQaiiNA93J0pq_un8AnLCMEQ</recordid><startdate>19990714</startdate><enddate>19990714</enddate><creator>Deavours, B.E.</creator><creator>Walker, R.A.</creator><general>Elsevier Inc</general><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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19990714</creationdate><title>Nuclear Localization of C-Terminal Domains of the Kinesin-like Protein MKLP-1</title><author>Deavours, B.E. ; Walker, R.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c371t-2eef4eb6d8ac6f6eec27abc5982779066e1c81b9d9559bdc399fb87c43991c9f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Biological Transport</topic><topic>Cell Fractionation</topic><topic>Cell Line</topic><topic>Cell Nucleus - metabolism</topic><topic>Detergents</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>kinesin</topic><topic>microtubule</topic><topic>Microtubule-Associated Proteins - chemistry</topic><topic>Microtubule-Associated Proteins - genetics</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>mitosis</topic><topic>motor</topic><topic>nuclear localization</topic><topic>Nuclear Localization Signals</topic><topic>Nuclear Matrix - metabolism</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Salts</topic><topic>Sequence Deletion</topic><topic>Spodoptera - cytology</topic><topic>Spodoptera - genetics</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Deavours, B.E.</creatorcontrib><creatorcontrib>Walker, R.A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Deavours, B.E.</au><au>Walker, R.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nuclear Localization of C-Terminal Domains of the Kinesin-like Protein MKLP-1</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1999-07-14</date><risdate>1999</risdate><volume>260</volume><issue>3</issue><spage>605</spage><epage>608</epage><pages>605-608</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The successful execution of mitosis in mammalian cells requires the activities of numerous kinesin-like proteins. 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These proteins remained tightly associated with the nucleus following both detergent and salt extraction, suggesting a tight interaction with a component of the nucleus.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10403813</pmid><doi>10.1006/bbrc.1999.0952</doi><tpages>4</tpages></addata></record> |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Biological Transport Cell Fractionation Cell Line Cell Nucleus - metabolism Detergents HeLa Cells Humans kinesin microtubule Microtubule-Associated Proteins - chemistry Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism mitosis motor nuclear localization Nuclear Localization Signals Nuclear Matrix - metabolism Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Salts Sequence Deletion Spodoptera - cytology Spodoptera - genetics Transfection |
| title | Nuclear Localization of C-Terminal Domains of the Kinesin-like Protein MKLP-1 |
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