The Chlamydomonas kinesin-like protein FLA10 is involved in motility associated with the flagellar membrane
The Chlamydomonas FLA10 gene was shown to encode a flagellar kinesin-like protein (Walther, Z., M. Vashishtha. and J.L. Hall. 1994. J. Cell Biol. 126:175-188). By using a temperature-sensitive allele of FLA10, we have determined that the FLA10 protein is necessary for both the bidirectional movement...
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| Veröffentlicht in: | The Journal of cell biology 1995-12, Vol.131 (6), p.1517-1527 |
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| creator | Kozminski, Keith G. Beech, Peter L. Rosenbaum, Joel L. |
| description | The Chlamydomonas FLA10 gene was shown to encode a flagellar kinesin-like protein (Walther, Z., M. Vashishtha. and J.L. Hall. 1994. J. Cell Biol. 126:175-188). By using a temperature-sensitive allele of FLA10, we have determined that the FLA10 protein is necessary for both the bidirectional movement of polystyrene beads on the flagellar membrane and intraflagellar transport (IFT), the bidirectional movement of granule-like particles beneath the flagellar membrane (Kozminski, K.G., K.A. Johnson, P. Forscher, and J.L. Rosenbaum. 1993. Proc. Natl. Acad. Sci.(USA). 90:5519-5523). In addition, we have correlated the presence and position of the IFT particles visualized by light microscopy with that of the electron dense complexes (rafts) observed beneath the flagellar membrane by electron microscopy. A role for FLA10 in submembranous or flagellar surface motility is also strongly supported by the immunolocalization of FLA10 to the region between the axonemal outer doublet microtubules and the flagellar membrane. |
| doi_str_mv | 10.1083/jcb.131.6.1517 |
| format | Article |
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Vashishtha. and J.L. Hall. 1994. J. Cell Biol. 126:175-188). By using a temperature-sensitive allele of FLA10, we have determined that the FLA10 protein is necessary for both the bidirectional movement of polystyrene beads on the flagellar membrane and intraflagellar transport (IFT), the bidirectional movement of granule-like particles beneath the flagellar membrane (Kozminski, K.G., K.A. Johnson, P. Forscher, and J.L. Rosenbaum. 1993. Proc. Natl. Acad. Sci.(USA). 90:5519-5523). In addition, we have correlated the presence and position of the IFT particles visualized by light microscopy with that of the electron dense complexes (rafts) observed beneath the flagellar membrane by electron microscopy. A role for FLA10 in submembranous or flagellar surface motility is also strongly supported by the immunolocalization of FLA10 to the region between the axonemal outer doublet microtubules and the flagellar membrane.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.131.6.1517</identifier><identifier>PMID: 8522608</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Alleles ; Animals ; Antibodies ; Antibody Specificity ; Base Sequence ; Cell lines ; cell membranes ; Cell Movement - physiology ; cell structure ; Cells ; Cellular biology ; Chlamydomonas ; Chlamydomonas - cytology ; Chlamydomonas - physiology ; Chlamydomonas - ultrastructure ; chlorophyceae ; Electron microscopy ; estructura celular ; Flagella ; Flagella - chemistry ; Flagella - physiology ; Flagella - ultrastructure ; Freshwater ; Genes ; immunologie ; immunology ; inmunologia ; Kinesin - immunology ; Kinesin - physiology ; membranas celulares ; membrane cellulaire ; Membrane Proteins - physiology ; Microscopy ; Microscopy, Immunoelectron ; Microscopy, Video ; Microtubules ; Molecular Sequence Data ; mouvement ; movement ; movimiento ; P branes ; proteinas ; proteine ; Proteins ; Rafts ; structure cellulaire ; Temperature ; ultraestructura ; ultrastructure</subject><ispartof>The Journal of cell biology, 1995-12, Vol.131 (6), p.1517-1527</ispartof><rights>Copyright 1995 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Dec 1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c487t-6b1beb0459fc962b3474cfe97a157b0841f9860efa3867ffdc44318f08120983</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8522608$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kozminski, Keith G.</creatorcontrib><creatorcontrib>Beech, Peter L.</creatorcontrib><creatorcontrib>Rosenbaum, Joel L.</creatorcontrib><creatorcontrib>Yale University, New Haven, CT</creatorcontrib><title>The Chlamydomonas kinesin-like protein FLA10 is involved in motility associated with the flagellar membrane</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The Chlamydomonas FLA10 gene was shown to encode a flagellar kinesin-like protein (Walther, Z., M. Vashishtha. and J.L. Hall. 1994. J. Cell Biol. 126:175-188). By using a temperature-sensitive allele of FLA10, we have determined that the FLA10 protein is necessary for both the bidirectional movement of polystyrene beads on the flagellar membrane and intraflagellar transport (IFT), the bidirectional movement of granule-like particles beneath the flagellar membrane (Kozminski, K.G., K.A. Johnson, P. Forscher, and J.L. Rosenbaum. 1993. Proc. Natl. Acad. Sci.(USA). 90:5519-5523). In addition, we have correlated the presence and position of the IFT particles visualized by light microscopy with that of the electron dense complexes (rafts) observed beneath the flagellar membrane by electron microscopy. A role for FLA10 in submembranous or flagellar surface motility is also strongly supported by the immunolocalization of FLA10 to the region between the axonemal outer doublet microtubules and the flagellar membrane.</description><subject>Alleles</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibody Specificity</subject><subject>Base Sequence</subject><subject>Cell lines</subject><subject>cell membranes</subject><subject>Cell Movement - physiology</subject><subject>cell structure</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>Chlamydomonas</subject><subject>Chlamydomonas - cytology</subject><subject>Chlamydomonas - physiology</subject><subject>Chlamydomonas - ultrastructure</subject><subject>chlorophyceae</subject><subject>Electron microscopy</subject><subject>estructura celular</subject><subject>Flagella</subject><subject>Flagella - chemistry</subject><subject>Flagella - physiology</subject><subject>Flagella - ultrastructure</subject><subject>Freshwater</subject><subject>Genes</subject><subject>immunologie</subject><subject>immunology</subject><subject>inmunologia</subject><subject>Kinesin - immunology</subject><subject>Kinesin - physiology</subject><subject>membranas celulares</subject><subject>membrane cellulaire</subject><subject>Membrane Proteins - physiology</subject><subject>Microscopy</subject><subject>Microscopy, Immunoelectron</subject><subject>Microscopy, Video</subject><subject>Microtubules</subject><subject>Molecular Sequence Data</subject><subject>mouvement</subject><subject>movement</subject><subject>movimiento</subject><subject>P branes</subject><subject>proteinas</subject><subject>proteine</subject><subject>Proteins</subject><subject>Rafts</subject><subject>structure cellulaire</subject><subject>Temperature</subject><subject>ultraestructura</subject><subject>ultrastructure</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2P0zAQxSMEWsrClROgiAO3hJk4_rogrSoWkCpxoJwtJ7Vbt0lcbLeo_z2uWi0fF3yx5feb5xm_oniJUCMI8n7bdzUSrFmNFPmjYoa0hUpgC4-LGUCDlaQNfVo8i3ELAC1vyU1xI2jTMBCzYrfcmHK-GfR4WvnRTzqWOzeZ6KZqcDtT7oNPxk3l_eIOoXSxdNPRD0ezyody9MkNLp1KHaPvnU75-qdLmzJlUzvotRkGHcrRjF3Qk3lePLF6iObFdb8tlvcfl_PP1eLrpy_zu0XVt4KninXYmQ5aKm0vWdOR3HNvjeQaKe9AtGilYGCsJoJxa1d92xIUFgQ2IAW5LT5cbPeHbjSr3kwp6EHtgxt1OCmvnfpbmdxGrf1RNbmeMZkN3l0Ngv9xMDGp0cX-PMtk_CEqzjlBTth_QeRAORKSwbf_gFt_CFP-hPwox_OiGaovUB98jMHYh5YR1DlrlbNWOWvF1DnrXPD6z0Ef8Gu4WX910bcx-fDbjSFvBGT5zUW22iu9Di6q799QSgYgqQQgvwCGirgk</recordid><startdate>19951201</startdate><enddate>19951201</enddate><creator>Kozminski, Keith G.</creator><creator>Beech, Peter L.</creator><creator>Rosenbaum, Joel L.</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19951201</creationdate><title>The Chlamydomonas kinesin-like protein FLA10 is involved in motility associated with the flagellar membrane</title><author>Kozminski, Keith G. ; Beech, Peter L. ; Rosenbaum, Joel L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c487t-6b1beb0459fc962b3474cfe97a157b0841f9860efa3867ffdc44318f08120983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Alleles</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antibody Specificity</topic><topic>Base Sequence</topic><topic>Cell lines</topic><topic>cell membranes</topic><topic>Cell Movement - physiology</topic><topic>cell structure</topic><topic>Cells</topic><topic>Cellular biology</topic><topic>Chlamydomonas</topic><topic>Chlamydomonas - cytology</topic><topic>Chlamydomonas - physiology</topic><topic>Chlamydomonas - ultrastructure</topic><topic>chlorophyceae</topic><topic>Electron microscopy</topic><topic>estructura celular</topic><topic>Flagella</topic><topic>Flagella - chemistry</topic><topic>Flagella - physiology</topic><topic>Flagella - ultrastructure</topic><topic>Freshwater</topic><topic>Genes</topic><topic>immunologie</topic><topic>immunology</topic><topic>inmunologia</topic><topic>Kinesin - immunology</topic><topic>Kinesin - physiology</topic><topic>membranas celulares</topic><topic>membrane cellulaire</topic><topic>Membrane Proteins - physiology</topic><topic>Microscopy</topic><topic>Microscopy, Immunoelectron</topic><topic>Microscopy, Video</topic><topic>Microtubules</topic><topic>Molecular Sequence Data</topic><topic>mouvement</topic><topic>movement</topic><topic>movimiento</topic><topic>P branes</topic><topic>proteinas</topic><topic>proteine</topic><topic>Proteins</topic><topic>Rafts</topic><topic>structure cellulaire</topic><topic>Temperature</topic><topic>ultraestructura</topic><topic>ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kozminski, Keith G.</creatorcontrib><creatorcontrib>Beech, Peter L.</creatorcontrib><creatorcontrib>Rosenbaum, Joel L.</creatorcontrib><creatorcontrib>Yale University, New Haven, CT</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kozminski, Keith G.</au><au>Beech, Peter L.</au><au>Rosenbaum, Joel L.</au><aucorp>Yale University, New Haven, CT</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Chlamydomonas kinesin-like protein FLA10 is involved in motility associated with the flagellar membrane</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1995-12-01</date><risdate>1995</risdate><volume>131</volume><issue>6</issue><spage>1517</spage><epage>1527</epage><pages>1517-1527</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>The Chlamydomonas FLA10 gene was shown to encode a flagellar kinesin-like protein (Walther, Z., M. Vashishtha. and J.L. Hall. 1994. J. Cell Biol. 126:175-188). By using a temperature-sensitive allele of FLA10, we have determined that the FLA10 protein is necessary for both the bidirectional movement of polystyrene beads on the flagellar membrane and intraflagellar transport (IFT), the bidirectional movement of granule-like particles beneath the flagellar membrane (Kozminski, K.G., K.A. Johnson, P. Forscher, and J.L. Rosenbaum. 1993. Proc. Natl. Acad. Sci.(USA). 90:5519-5523). In addition, we have correlated the presence and position of the IFT particles visualized by light microscopy with that of the electron dense complexes (rafts) observed beneath the flagellar membrane by electron microscopy. A role for FLA10 in submembranous or flagellar surface motility is also strongly supported by the immunolocalization of FLA10 to the region between the axonemal outer doublet microtubules and the flagellar membrane.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>8522608</pmid><doi>10.1083/jcb.131.6.1517</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Alleles Animals Antibodies Antibody Specificity Base Sequence Cell lines cell membranes Cell Movement - physiology cell structure Cells Cellular biology Chlamydomonas Chlamydomonas - cytology Chlamydomonas - physiology Chlamydomonas - ultrastructure chlorophyceae Electron microscopy estructura celular Flagella Flagella - chemistry Flagella - physiology Flagella - ultrastructure Freshwater Genes immunologie immunology inmunologia Kinesin - immunology Kinesin - physiology membranas celulares membrane cellulaire Membrane Proteins - physiology Microscopy Microscopy, Immunoelectron Microscopy, Video Microtubules Molecular Sequence Data mouvement movement movimiento P branes proteinas proteine Proteins Rafts structure cellulaire Temperature ultraestructura ultrastructure |
| title | The Chlamydomonas kinesin-like protein FLA10 is involved in motility associated with the flagellar membrane |
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