Cep128 associates with Odf2 to form the subdistal appendage of the centriole
The mother centriole in a cell has two appendages, the distal appendage (DA) and subdistal appendage (SDA), which have roles in generating cilia and organizing the cellular microtubular network, respectively. In the knockout (KO) cells of Odf2, the component of the DA and SDA, both appendages simult...
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Veröffentlicht in: | Genes to cells : devoted to molecular & cellular mechanisms 2019-03, Vol.24 (3), p.231-243 |
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creator | Kashihara, Hiroka Chiba, Shuhei Kanno, Shin‐ichiro Suzuki, Koya Yano, Tomoki Tsukita, Sachiko |
description | The mother centriole in a cell has two appendages, the distal appendage (DA) and subdistal appendage (SDA), which have roles in generating cilia and organizing the cellular microtubular network, respectively. In the knockout (KO) cells of Odf2, the component of the DA and SDA, both appendages simultaneously disappear. However, the molecular mechanisms by which the DA and SDA form independently but close to each other downstream of Odf2 are unknown. Here, using super‐resolution structured illumination microscopy (SR‐SIM), we found that the signal for GFP‐tagged Odf2 overlapped considerably with that of immunofluorescently labeled Cep128. We further found that Cep128 knockdown (KD) caused the dissociation of other SDA components from the centriole, including centriolin, Ndel1, ninein and Cep170, whereas Odf2 was still associated with the centriole. In contrast, the DA components remained associated with the centriole in Cep128 KD cells. Consistent with this observation, we identified Cep128 as an Odf2‐interacting protein by immunoprecipitation. Taken with the finding that Cep128 deletion decreased the stability of centriolar microtubules, our results indicate that Cep128 associates with Odf2 in the hierarchical assembly of SDA components to elicit the microtubule‐organizing function.
This study shows that Cep128 associates with Odf2 in the hierarchical assembly of subdistal appendage (SDA) components. Cep128 is essential for the SDA’s specific Odf2‐based construction and function on the mother centriole. |
doi_str_mv | 10.1111/gtc.12668 |
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This study shows that Cep128 associates with Odf2 in the hierarchical assembly of subdistal appendage (SDA) components. Cep128 is essential for the SDA’s specific Odf2‐based construction and function on the mother centriole.</description><identifier>ISSN: 1356-9597</identifier><identifier>EISSN: 1365-2443</identifier><identifier>DOI: 10.1111/gtc.12668</identifier><identifier>PMID: 30623524</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>centrosome ; Cilia ; Clonal deletion ; Immunoprecipitation ; Microtubules ; Molecular modelling ; Odf2 ; subdistal appendage ; super-resolution structured illumination microscopy</subject><ispartof>Genes to cells : devoted to molecular & cellular mechanisms, 2019-03, Vol.24 (3), p.231-243</ispartof><rights>2019 Molecular Biology Society of Japan and John Wiley & Sons Australia, Ltd</rights><rights>This article is protected by copyright. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3888-81cb150a3b0021dc84f5b1815c4faa07cb215c361b3b366b9d69cef034cf72703</citedby><cites>FETCH-LOGICAL-c3888-81cb150a3b0021dc84f5b1815c4faa07cb215c361b3b366b9d69cef034cf72703</cites><orcidid>0000-0002-6204-1348</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fgtc.12668$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fgtc.12668$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,778,782,1414,1430,27911,27912,45561,45562,46396,46820</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30623524$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kashihara, Hiroka</creatorcontrib><creatorcontrib>Chiba, Shuhei</creatorcontrib><creatorcontrib>Kanno, Shin‐ichiro</creatorcontrib><creatorcontrib>Suzuki, Koya</creatorcontrib><creatorcontrib>Yano, Tomoki</creatorcontrib><creatorcontrib>Tsukita, Sachiko</creatorcontrib><title>Cep128 associates with Odf2 to form the subdistal appendage of the centriole</title><title>Genes to cells : devoted to molecular & cellular mechanisms</title><addtitle>Genes Cells</addtitle><description>The mother centriole in a cell has two appendages, the distal appendage (DA) and subdistal appendage (SDA), which have roles in generating cilia and organizing the cellular microtubular network, respectively. In the knockout (KO) cells of Odf2, the component of the DA and SDA, both appendages simultaneously disappear. However, the molecular mechanisms by which the DA and SDA form independently but close to each other downstream of Odf2 are unknown. Here, using super‐resolution structured illumination microscopy (SR‐SIM), we found that the signal for GFP‐tagged Odf2 overlapped considerably with that of immunofluorescently labeled Cep128. We further found that Cep128 knockdown (KD) caused the dissociation of other SDA components from the centriole, including centriolin, Ndel1, ninein and Cep170, whereas Odf2 was still associated with the centriole. In contrast, the DA components remained associated with the centriole in Cep128 KD cells. Consistent with this observation, we identified Cep128 as an Odf2‐interacting protein by immunoprecipitation. Taken with the finding that Cep128 deletion decreased the stability of centriolar microtubules, our results indicate that Cep128 associates with Odf2 in the hierarchical assembly of SDA components to elicit the microtubule‐organizing function.
This study shows that Cep128 associates with Odf2 in the hierarchical assembly of subdistal appendage (SDA) components. Cep128 is essential for the SDA’s specific Odf2‐based construction and function on the mother centriole.</description><subject>centrosome</subject><subject>Cilia</subject><subject>Clonal deletion</subject><subject>Immunoprecipitation</subject><subject>Microtubules</subject><subject>Molecular modelling</subject><subject>Odf2</subject><subject>subdistal appendage</subject><subject>super-resolution structured illumination microscopy</subject><issn>1356-9597</issn><issn>1365-2443</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNp10E9LwzAYBvAgipvTg19AAl700C1_miw9StEpDHaZ55KkydbRNrVpGfv2Zuv0IPhe8kJ-PLw8ANxjNMVhZptOTzHhXFyAMaacRSSO6eVxZzxKWDIfgRvvdwhhShC7BiOKOKGMxGOwTE2DiYDSe6cL2RkP90W3havcEtg5aF1bwW5roO9VXvhOllA2jalzuTHQ2dOXNnXXFq40t-DKytKbu_M7AZ9vr-v0PVquFh_pyzLSVAgRCawVZkhShRDBuRaxZQoLzHRspURzrUjYKceKKsq5SnKeaGMRjbWdkzmiE_A05Dat--qN77Kq8NqUpayN631GMGeccyZEoI9_6M71bR2uCyqhIuaIH9XzoHTrvG-NzZq2qGR7yDDKjhVnoeLsVHGwD-fEXlUm_5U_nQYwG8C-KM3h_6RssU6HyG9VP4Lt</recordid><startdate>201903</startdate><enddate>201903</enddate><creator>Kashihara, Hiroka</creator><creator>Chiba, Shuhei</creator><creator>Kanno, Shin‐ichiro</creator><creator>Suzuki, Koya</creator><creator>Yano, Tomoki</creator><creator>Tsukita, Sachiko</creator><general>Wiley Subscription Services, Inc</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-6204-1348</orcidid></search><sort><creationdate>201903</creationdate><title>Cep128 associates with Odf2 to form the subdistal appendage of the centriole</title><author>Kashihara, Hiroka ; Chiba, Shuhei ; Kanno, Shin‐ichiro ; Suzuki, Koya ; Yano, Tomoki ; Tsukita, Sachiko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3888-81cb150a3b0021dc84f5b1815c4faa07cb215c361b3b366b9d69cef034cf72703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>centrosome</topic><topic>Cilia</topic><topic>Clonal deletion</topic><topic>Immunoprecipitation</topic><topic>Microtubules</topic><topic>Molecular modelling</topic><topic>Odf2</topic><topic>subdistal appendage</topic><topic>super-resolution structured illumination microscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kashihara, Hiroka</creatorcontrib><creatorcontrib>Chiba, Shuhei</creatorcontrib><creatorcontrib>Kanno, Shin‐ichiro</creatorcontrib><creatorcontrib>Suzuki, Koya</creatorcontrib><creatorcontrib>Yano, Tomoki</creatorcontrib><creatorcontrib>Tsukita, Sachiko</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kashihara, Hiroka</au><au>Chiba, Shuhei</au><au>Kanno, Shin‐ichiro</au><au>Suzuki, Koya</au><au>Yano, Tomoki</au><au>Tsukita, Sachiko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cep128 associates with Odf2 to form the subdistal appendage of the centriole</atitle><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle><addtitle>Genes Cells</addtitle><date>2019-03</date><risdate>2019</risdate><volume>24</volume><issue>3</issue><spage>231</spage><epage>243</epage><pages>231-243</pages><issn>1356-9597</issn><eissn>1365-2443</eissn><abstract>The mother centriole in a cell has two appendages, the distal appendage (DA) and subdistal appendage (SDA), which have roles in generating cilia and organizing the cellular microtubular network, respectively. In the knockout (KO) cells of Odf2, the component of the DA and SDA, both appendages simultaneously disappear. However, the molecular mechanisms by which the DA and SDA form independently but close to each other downstream of Odf2 are unknown. Here, using super‐resolution structured illumination microscopy (SR‐SIM), we found that the signal for GFP‐tagged Odf2 overlapped considerably with that of immunofluorescently labeled Cep128. We further found that Cep128 knockdown (KD) caused the dissociation of other SDA components from the centriole, including centriolin, Ndel1, ninein and Cep170, whereas Odf2 was still associated with the centriole. In contrast, the DA components remained associated with the centriole in Cep128 KD cells. Consistent with this observation, we identified Cep128 as an Odf2‐interacting protein by immunoprecipitation. Taken with the finding that Cep128 deletion decreased the stability of centriolar microtubules, our results indicate that Cep128 associates with Odf2 in the hierarchical assembly of SDA components to elicit the microtubule‐organizing function.
This study shows that Cep128 associates with Odf2 in the hierarchical assembly of subdistal appendage (SDA) components. Cep128 is essential for the SDA’s specific Odf2‐based construction and function on the mother centriole.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>30623524</pmid><doi>10.1111/gtc.12668</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0002-6204-1348</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | centrosome Cilia Clonal deletion Immunoprecipitation Microtubules Molecular modelling Odf2 subdistal appendage super-resolution structured illumination microscopy |
title | Cep128 associates with Odf2 to form the subdistal appendage of the centriole |
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