A CUG-initiated CATSPERθ functions in the CatSper channel assembly and serves as a checkpoint for flagellar trafficking
Calcium signaling is critical for successful fertilization. In spermatozoa, calcium influx into the sperm flagella mediated by the sperm-specific CatSper calcium channel is necessary for hyperactivated motility and male fertility. CatSper is a macromolecular complex and is repeatedly arranged in zig...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2023-09, Vol.120 (39), p.e2304409120-e2304409120 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Huang, Xiaofang Miyata, Haruhiko Wang, Huafeng Mori, Giulia Iida-Norita, Rie Ikawa, Masahito Percudani, Riccardo Chung, Jean-Ju |
| description | Calcium signaling is critical for successful fertilization. In spermatozoa, calcium influx into the sperm flagella mediated by the sperm-specific CatSper calcium channel is necessary for hyperactivated motility and male fertility. CatSper is a macromolecular complex and is repeatedly arranged in zigzag rows within four linear nanodomains along the sperm flagella. Here, we report that the
-encoded transmembrane (TM) domain-containing protein, CATSPERθ is essential for the CatSper channel assembly during sperm tail formation. CATSPERθ facilitates the channel assembly by serving as a scaffold for a pore-forming subunit CATSPER4. CATSPERθ is specifically localized at the interface of a CatSper dimer and can self-interact, suggesting its potential role in CatSper dimer formation. Male mice lacking CATSPERθ are infertile because the sperm lack the entire CatSper channel from sperm flagella, rendering sperm unable to hyperactivate, regardless of their normal expression in the testis. In contrast, genetic abrogation of any of the other CatSper TM subunits results in loss of CATSPERθ protein in the spermatid cells during spermatogenesis. CATSPERθ might act as a checkpoint for the properly assembled CatSper channel complex to traffic to sperm flagella. This study provides insights into the CatSper channel assembly and elucidates the physiological role of CATSPERθ in sperm motility and male fertility. |
| doi_str_mv | 10.1073/pnas.2304409120 |
| format | Article |
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-encoded transmembrane (TM) domain-containing protein, CATSPERθ is essential for the CatSper channel assembly during sperm tail formation. CATSPERθ facilitates the channel assembly by serving as a scaffold for a pore-forming subunit CATSPER4. CATSPERθ is specifically localized at the interface of a CatSper dimer and can self-interact, suggesting its potential role in CatSper dimer formation. Male mice lacking CATSPERθ are infertile because the sperm lack the entire CatSper channel from sperm flagella, rendering sperm unable to hyperactivate, regardless of their normal expression in the testis. In contrast, genetic abrogation of any of the other CatSper TM subunits results in loss of CATSPERθ protein in the spermatid cells during spermatogenesis. CATSPERθ might act as a checkpoint for the properly assembled CatSper channel complex to traffic to sperm flagella. This study provides insights into the CatSper channel assembly and elucidates the physiological role of CATSPERθ in sperm motility and male fertility.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.2304409120</identifier><identifier>PMID: 37725640</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Animals ; Assembly ; Biological Sciences ; Calcium ; Calcium channels ; Calcium influx ; Calcium signalling ; Cell Membrane ; Dimers ; Fertility ; Fertilization ; Flagella ; Ion Channels ; Macromolecules ; Male ; Males ; Membrane Proteins - genetics ; Mice ; Motility ; Pore formation ; Proteins ; Semen ; Seminal Plasma Proteins ; Sperm ; Sperm Motility - genetics ; Sperm Tail ; Spermatogenesis ; Spermatozoa</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2023-09, Vol.120 (39), p.e2304409120-e2304409120</ispartof><rights>Copyright National Academy of Sciences Sep 26, 2023</rights><rights>Copyright © 2023 the Author(s). Published by PNAS. 2023</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-ab86c587e209b11a9e1bcb3b146a27294393912fe68f08570c8b461bd158ed283</citedby><cites>FETCH-LOGICAL-c422t-ab86c587e209b11a9e1bcb3b146a27294393912fe68f08570c8b461bd158ed283</cites><orcidid>0000-0003-4758-5803 ; 0000-0001-8452-1062 ; 0000-0003-1090-8349 ; 0000-0001-9859-6217 ; 0000-0002-2292-1711 ; 0000-0003-0104-1974 ; 0000-0002-7326-4379 ; 0000-0001-8018-1355</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10523455/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10523455/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37725640$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Huang, Xiaofang</creatorcontrib><creatorcontrib>Miyata, Haruhiko</creatorcontrib><creatorcontrib>Wang, Huafeng</creatorcontrib><creatorcontrib>Mori, Giulia</creatorcontrib><creatorcontrib>Iida-Norita, Rie</creatorcontrib><creatorcontrib>Ikawa, Masahito</creatorcontrib><creatorcontrib>Percudani, Riccardo</creatorcontrib><creatorcontrib>Chung, Jean-Ju</creatorcontrib><title>A CUG-initiated CATSPERθ functions in the CatSper channel assembly and serves as a checkpoint for flagellar trafficking</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Calcium signaling is critical for successful fertilization. In spermatozoa, calcium influx into the sperm flagella mediated by the sperm-specific CatSper calcium channel is necessary for hyperactivated motility and male fertility. CatSper is a macromolecular complex and is repeatedly arranged in zigzag rows within four linear nanodomains along the sperm flagella. Here, we report that the
-encoded transmembrane (TM) domain-containing protein, CATSPERθ is essential for the CatSper channel assembly during sperm tail formation. CATSPERθ facilitates the channel assembly by serving as a scaffold for a pore-forming subunit CATSPER4. CATSPERθ is specifically localized at the interface of a CatSper dimer and can self-interact, suggesting its potential role in CatSper dimer formation. Male mice lacking CATSPERθ are infertile because the sperm lack the entire CatSper channel from sperm flagella, rendering sperm unable to hyperactivate, regardless of their normal expression in the testis. In contrast, genetic abrogation of any of the other CatSper TM subunits results in loss of CATSPERθ protein in the spermatid cells during spermatogenesis. CATSPERθ might act as a checkpoint for the properly assembled CatSper channel complex to traffic to sperm flagella. This study provides insights into the CatSper channel assembly and elucidates the physiological role of CATSPERθ in sperm motility and male fertility.</description><subject>Animals</subject><subject>Assembly</subject><subject>Biological Sciences</subject><subject>Calcium</subject><subject>Calcium channels</subject><subject>Calcium influx</subject><subject>Calcium signalling</subject><subject>Cell Membrane</subject><subject>Dimers</subject><subject>Fertility</subject><subject>Fertilization</subject><subject>Flagella</subject><subject>Ion Channels</subject><subject>Macromolecules</subject><subject>Male</subject><subject>Males</subject><subject>Membrane Proteins - genetics</subject><subject>Mice</subject><subject>Motility</subject><subject>Pore formation</subject><subject>Proteins</subject><subject>Semen</subject><subject>Seminal Plasma Proteins</subject><subject>Sperm</subject><subject>Sperm Motility - genetics</subject><subject>Sperm Tail</subject><subject>Spermatogenesis</subject><subject>Spermatozoa</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkctu1DAUhi0EosPAmh2yxIZN2uNLHGeFRlEpSJVAtF1bjnMy4zbjBDup6JvxFDwTHrWUy8qWz-df59dHyGsGxwwqcTIFm465ACmhZhyekBXLl0LJGp6SFQCvCi25PCIvUroGgLrU8JwciaripZKwIt83tLk6K3zws7czdrTZXF58Of368wftl-BmP4ZEfaDzDmlj54sJI3U7GwIO1KaE-3a4ozZ0NGG8xZTfqM0Auptp9GGm_RhpP9gtDoONdI6277278WH7kjzr7ZDw1cO5JlcfTi-bj8X557NPzea8cJLzubCtVq7UFXKoW8Zsjax1rWiZVJZXvJaiFrl5j0r3oMsKnG6lYm3HSo0d12JN3t_nTku7x85hyEsMZop-b-OdGa03_06C35nteGsYlFzIsswJ7x4S4vhtwTSbvU_uUCjguCTDtVKVYirja_L2P_R6XGLI_TJVQTYhADJ1ck-5OKYUsX_choE5aDUHreaP1vzjzd8lHvnfHsUvlBefNA</recordid><startdate>20230926</startdate><enddate>20230926</enddate><creator>Huang, Xiaofang</creator><creator>Miyata, Haruhiko</creator><creator>Wang, Huafeng</creator><creator>Mori, Giulia</creator><creator>Iida-Norita, Rie</creator><creator>Ikawa, Masahito</creator><creator>Percudani, Riccardo</creator><creator>Chung, Jean-Ju</creator><general>National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</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>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-4758-5803</orcidid><orcidid>https://orcid.org/0000-0001-8452-1062</orcidid><orcidid>https://orcid.org/0000-0003-1090-8349</orcidid><orcidid>https://orcid.org/0000-0001-9859-6217</orcidid><orcidid>https://orcid.org/0000-0002-2292-1711</orcidid><orcidid>https://orcid.org/0000-0003-0104-1974</orcidid><orcidid>https://orcid.org/0000-0002-7326-4379</orcidid><orcidid>https://orcid.org/0000-0001-8018-1355</orcidid></search><sort><creationdate>20230926</creationdate><title>A CUG-initiated CATSPERθ functions in the CatSper channel assembly and serves as a checkpoint for flagellar trafficking</title><author>Huang, Xiaofang ; 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In spermatozoa, calcium influx into the sperm flagella mediated by the sperm-specific CatSper calcium channel is necessary for hyperactivated motility and male fertility. CatSper is a macromolecular complex and is repeatedly arranged in zigzag rows within four linear nanodomains along the sperm flagella. Here, we report that the
-encoded transmembrane (TM) domain-containing protein, CATSPERθ is essential for the CatSper channel assembly during sperm tail formation. CATSPERθ facilitates the channel assembly by serving as a scaffold for a pore-forming subunit CATSPER4. CATSPERθ is specifically localized at the interface of a CatSper dimer and can self-interact, suggesting its potential role in CatSper dimer formation. Male mice lacking CATSPERθ are infertile because the sperm lack the entire CatSper channel from sperm flagella, rendering sperm unable to hyperactivate, regardless of their normal expression in the testis. In contrast, genetic abrogation of any of the other CatSper TM subunits results in loss of CATSPERθ protein in the spermatid cells during spermatogenesis. CATSPERθ might act as a checkpoint for the properly assembled CatSper channel complex to traffic to sperm flagella. This study provides insights into the CatSper channel assembly and elucidates the physiological role of CATSPERθ in sperm motility and male fertility.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>37725640</pmid><doi>10.1073/pnas.2304409120</doi><orcidid>https://orcid.org/0000-0003-4758-5803</orcidid><orcidid>https://orcid.org/0000-0001-8452-1062</orcidid><orcidid>https://orcid.org/0000-0003-1090-8349</orcidid><orcidid>https://orcid.org/0000-0001-9859-6217</orcidid><orcidid>https://orcid.org/0000-0002-2292-1711</orcidid><orcidid>https://orcid.org/0000-0003-0104-1974</orcidid><orcidid>https://orcid.org/0000-0002-7326-4379</orcidid><orcidid>https://orcid.org/0000-0001-8018-1355</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Assembly Biological Sciences Calcium Calcium channels Calcium influx Calcium signalling Cell Membrane Dimers Fertility Fertilization Flagella Ion Channels Macromolecules Male Males Membrane Proteins - genetics Mice Motility Pore formation Proteins Semen Seminal Plasma Proteins Sperm Sperm Motility - genetics Sperm Tail Spermatogenesis Spermatozoa |
| title | A CUG-initiated CATSPERθ functions in the CatSper channel assembly and serves as a checkpoint for flagellar trafficking |
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