Direct involvement of the isotype-specific C-terminus of beta tubulin in ciliary beating
In previous studies in Drosophila, Nielsen et al. hypothesized that the beta tubulin C-terminal axonemal motif ;EGEFXXX', where X is an acidic amino acid, is required for ciliary function and assembly (Nielsen et al., 2001, Curr. Biol. 11, 529-533). This motif is present in some but not all mam...
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creator | Vent, Julia Wyatt, Todd A Smith, D David Banerjee, Asok Ludueña, Richard F Sisson, Joseph H Hallworth, Richard |
description | In previous studies in Drosophila, Nielsen et al. hypothesized that the beta tubulin C-terminal axonemal motif ;EGEFXXX', where X is an acidic amino acid, is required for ciliary function and assembly (Nielsen et al., 2001, Curr. Biol. 11, 529-533). This motif is present in some but not all mammalian beta tubulin isotypes. We therefore investigated whether this motif is important in ciliary function in mammals. In a preparation of isolated, ATP-reactivated bovine tracheal cilia, we found that monoclonal antibodies directed against the C-terminus of betaI, betaIV and betaV tubulin blocked ciliary beating in a concentration dependent manner. Antibodies against other epitopes of beta tubulin were ineffective, as were antibodies against alpha tubulin. Peptides consisting of the axonemal motif and motif-like sequences of these isotypes blocked ciliary beating. These results suggest that the axonemal motif sequences of betaI, betaIV and betaV tubulin are essential for ciliary function. Peptides consisting of corresponding C-terminal sequences in alpha tubulin isotypes were also ineffective in blocking ciliary beating, which suggests that the C-terminus of alpha tubulin is not directly involved in cilia function in mammals. |
doi_str_mv | 10.1242/jcs.02550 |
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Biol. 11, 529-533). This motif is present in some but not all mammalian beta tubulin isotypes. We therefore investigated whether this motif is important in ciliary function in mammals. In a preparation of isolated, ATP-reactivated bovine tracheal cilia, we found that monoclonal antibodies directed against the C-terminus of betaI, betaIV and betaV tubulin blocked ciliary beating in a concentration dependent manner. Antibodies against other epitopes of beta tubulin were ineffective, as were antibodies against alpha tubulin. Peptides consisting of the axonemal motif and motif-like sequences of these isotypes blocked ciliary beating. These results suggest that the axonemal motif sequences of betaI, betaIV and betaV tubulin are essential for ciliary function. Peptides consisting of corresponding C-terminal sequences in alpha tubulin isotypes were also ineffective in blocking ciliary beating, which suggests that the C-terminus of alpha tubulin is not directly involved in cilia function in mammals.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.02550</identifier><identifier>PMID: 16159957</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Animals ; Antibodies - metabolism ; Cattle ; Cilia - metabolism ; Cilia - ultrastructure ; Epitopes ; Microtubules - metabolism ; Molecular Sequence Data ; Peptides - genetics ; Peptides - metabolism ; Protein Isoforms - chemistry ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Protein Structure, Secondary ; Respiratory Mucosa - cytology ; Tubulin - chemistry ; Tubulin - genetics ; Tubulin - metabolism</subject><ispartof>Journal of cell science, 2005-10, Vol.118 (Pt 19), p.4333-4341</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c303t-2535501f76e7d0de282de348d7b932f71da4b119790f8accb2de739ba8f95eec3</citedby><cites>FETCH-LOGICAL-c303t-2535501f76e7d0de282de348d7b932f71da4b119790f8accb2de739ba8f95eec3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,3665,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16159957$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vent, Julia</creatorcontrib><creatorcontrib>Wyatt, Todd A</creatorcontrib><creatorcontrib>Smith, D David</creatorcontrib><creatorcontrib>Banerjee, Asok</creatorcontrib><creatorcontrib>Ludueña, Richard F</creatorcontrib><creatorcontrib>Sisson, Joseph H</creatorcontrib><creatorcontrib>Hallworth, Richard</creatorcontrib><title>Direct involvement of the isotype-specific C-terminus of beta tubulin in ciliary beating</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>In previous studies in Drosophila, Nielsen et al. hypothesized that the beta tubulin C-terminal axonemal motif ;EGEFXXX', where X is an acidic amino acid, is required for ciliary function and assembly (Nielsen et al., 2001, Curr. Biol. 11, 529-533). This motif is present in some but not all mammalian beta tubulin isotypes. We therefore investigated whether this motif is important in ciliary function in mammals. In a preparation of isolated, ATP-reactivated bovine tracheal cilia, we found that monoclonal antibodies directed against the C-terminus of betaI, betaIV and betaV tubulin blocked ciliary beating in a concentration dependent manner. Antibodies against other epitopes of beta tubulin were ineffective, as were antibodies against alpha tubulin. Peptides consisting of the axonemal motif and motif-like sequences of these isotypes blocked ciliary beating. These results suggest that the axonemal motif sequences of betaI, betaIV and betaV tubulin are essential for ciliary function. Peptides consisting of corresponding C-terminal sequences in alpha tubulin isotypes were also ineffective in blocking ciliary beating, which suggests that the C-terminus of alpha tubulin is not directly involved in cilia function in mammals.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies - metabolism</subject><subject>Cattle</subject><subject>Cilia - metabolism</subject><subject>Cilia - ultrastructure</subject><subject>Epitopes</subject><subject>Microtubules - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Peptides - genetics</subject><subject>Peptides - metabolism</subject><subject>Protein Isoforms - chemistry</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Protein Structure, Secondary</subject><subject>Respiratory Mucosa - cytology</subject><subject>Tubulin - chemistry</subject><subject>Tubulin - genetics</subject><subject>Tubulin - metabolism</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkctOwzAQRS0EoqWw4AdQVkgsAn4kcbxBQuUpVWIDEjvLccatqyQusVOpf49LKx6rkTzHd-7MReic4GtCM3qz1P4a0zzHB2hMMs5TQRg_RGOMKUlFztgInXi_xBhzKvgxGpGC5ELkfIw-7m0POiS2W7tmDS10IXEmCQtIrHdhs4LUr0BbY3UyTQP0re0Gv0UqCCoJQzU0tovfE20bq_pNfFfBdvNTdGRU4-FsXyfo_fHhbfqczl6fXqZ3s1QzzEJKcxZ9E8ML4DWugZa0BpaVNa8Eo4aTWmUVIYILbEqldRXbnIlKlUbkAJpN0O1OdzVULdQ6LtCrRq5620Y30ikr_3c6u5Bzt5ZECJplLApc7gV69zmAD7K1XkPTqA7c4GVRxmOxAkfwagfq3nnfg_kZQrDc5iBjDvI7h8he_HX1S-4Pz74ADCqF3w</recordid><startdate>20051001</startdate><enddate>20051001</enddate><creator>Vent, Julia</creator><creator>Wyatt, Todd A</creator><creator>Smith, D David</creator><creator>Banerjee, Asok</creator><creator>Ludueña, Richard F</creator><creator>Sisson, Joseph H</creator><creator>Hallworth, Richard</creator><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><scope>5PM</scope></search><sort><creationdate>20051001</creationdate><title>Direct involvement of the isotype-specific C-terminus of beta tubulin in ciliary beating</title><author>Vent, Julia ; Wyatt, Todd A ; Smith, D David ; Banerjee, Asok ; Ludueña, Richard F ; Sisson, Joseph H ; Hallworth, Richard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c303t-2535501f76e7d0de282de348d7b932f71da4b119790f8accb2de739ba8f95eec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies - metabolism</topic><topic>Cattle</topic><topic>Cilia - metabolism</topic><topic>Cilia - ultrastructure</topic><topic>Epitopes</topic><topic>Microtubules - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Peptides - genetics</topic><topic>Peptides - metabolism</topic><topic>Protein Isoforms - chemistry</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Protein Structure, Secondary</topic><topic>Respiratory Mucosa - cytology</topic><topic>Tubulin - chemistry</topic><topic>Tubulin - genetics</topic><topic>Tubulin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vent, Julia</creatorcontrib><creatorcontrib>Wyatt, Todd A</creatorcontrib><creatorcontrib>Smith, D David</creatorcontrib><creatorcontrib>Banerjee, Asok</creatorcontrib><creatorcontrib>Ludueña, Richard F</creatorcontrib><creatorcontrib>Sisson, Joseph H</creatorcontrib><creatorcontrib>Hallworth, Richard</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vent, Julia</au><au>Wyatt, Todd A</au><au>Smith, D David</au><au>Banerjee, Asok</au><au>Ludueña, Richard F</au><au>Sisson, Joseph H</au><au>Hallworth, Richard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Direct involvement of the isotype-specific C-terminus of beta tubulin in ciliary beating</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2005-10-01</date><risdate>2005</risdate><volume>118</volume><issue>Pt 19</issue><spage>4333</spage><epage>4341</epage><pages>4333-4341</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>In previous studies in Drosophila, Nielsen et al. hypothesized that the beta tubulin C-terminal axonemal motif ;EGEFXXX', where X is an acidic amino acid, is required for ciliary function and assembly (Nielsen et al., 2001, Curr. Biol. 11, 529-533). This motif is present in some but not all mammalian beta tubulin isotypes. We therefore investigated whether this motif is important in ciliary function in mammals. In a preparation of isolated, ATP-reactivated bovine tracheal cilia, we found that monoclonal antibodies directed against the C-terminus of betaI, betaIV and betaV tubulin blocked ciliary beating in a concentration dependent manner. Antibodies against other epitopes of beta tubulin were ineffective, as were antibodies against alpha tubulin. Peptides consisting of the axonemal motif and motif-like sequences of these isotypes blocked ciliary beating. These results suggest that the axonemal motif sequences of betaI, betaIV and betaV tubulin are essential for ciliary function. Peptides consisting of corresponding C-terminal sequences in alpha tubulin isotypes were also ineffective in blocking ciliary beating, which suggests that the C-terminus of alpha tubulin is not directly involved in cilia function in mammals.</abstract><cop>England</cop><pmid>16159957</pmid><doi>10.1242/jcs.02550</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Antibodies - metabolism Cattle Cilia - metabolism Cilia - ultrastructure Epitopes Microtubules - metabolism Molecular Sequence Data Peptides - genetics Peptides - metabolism Protein Isoforms - chemistry Protein Isoforms - genetics Protein Isoforms - metabolism Protein Structure, Secondary Respiratory Mucosa - cytology Tubulin - chemistry Tubulin - genetics Tubulin - metabolism |
title | Direct involvement of the isotype-specific C-terminus of beta tubulin in ciliary beating |
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