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Expression and functional analysis of cytoplasmic dynein during spermatogenesis in Portunus trituberculatus
The mechanism of acrosome formation in the crab sperm is a hot topic in crustacean reproduction research. Dynein is a motor protein that performs microtubule-dependent retrograde transport and plays an essential role in spermatogenesis. However, whether cytoplasmic dynein participates in acrosome fo...
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Published in: | Cell and tissue research 2021-10, Vol.386 (1), p.191-203 |
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description | The mechanism of acrosome formation in the crab sperm is a hot topic in crustacean reproduction research. Dynein is a motor protein that performs microtubule-dependent retrograde transport and plays an essential role in spermatogenesis. However, whether cytoplasmic dynein participates in acrosome formation in the crab sperm remains poorly understood. In this study, we cloned the cytoplasmic dynein intermediate chain gene (
Pt-DIC
) from
Portunus trituberculatus
testis. Pt-DIC is composed of a p150glued-binding domain, a dynein light chain (DLC)-binding domain, and a dynein heavy chain (DHC)-binding domain. The
Pt-DIC
gene is widely expressed in different tissues, showing the highest expression in the testis, and it is expressed in different stages of spermatid development, indicating important functions in spermatogenesis. We further observed the colocalization of Pt-DIC and Pt-DHC, Pt-DHC and tubulin, and Pt-DHC and GM130, and the results indicated that cytoplasmic dynein may participate in nuclear shaping and acrosome formation via vesicle transport. In addition, we examined the colocalization of Pt-DHC and a mitochondrion (MT) tracker and that of Pt-DHC and prohibitin (PHB). The results indicated that cytoplasmic dynein participated in mitochondrial transport and mitochondrial degradation. Taken together, these results support the hypothesis that cytoplasmic dynein participates in acrosome formation, nuclear shaping, and mitochondrial transport during spermiogenesis in
P. trituberculatus
. This study will provide valuable guidance for the artificial fertilization and reproduction of
P. trituberculatus
. |
doi_str_mv | 10.1007/s00441-021-03519-3 |
format | article |
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Pt-DIC
) from
Portunus trituberculatus
testis. Pt-DIC is composed of a p150glued-binding domain, a dynein light chain (DLC)-binding domain, and a dynein heavy chain (DHC)-binding domain. The
Pt-DIC
gene is widely expressed in different tissues, showing the highest expression in the testis, and it is expressed in different stages of spermatid development, indicating important functions in spermatogenesis. We further observed the colocalization of Pt-DIC and Pt-DHC, Pt-DHC and tubulin, and Pt-DHC and GM130, and the results indicated that cytoplasmic dynein may participate in nuclear shaping and acrosome formation via vesicle transport. In addition, we examined the colocalization of Pt-DHC and a mitochondrion (MT) tracker and that of Pt-DHC and prohibitin (PHB). The results indicated that cytoplasmic dynein participated in mitochondrial transport and mitochondrial degradation. Taken together, these results support the hypothesis that cytoplasmic dynein participates in acrosome formation, nuclear shaping, and mitochondrial transport during spermiogenesis in
P. trituberculatus
. This study will provide valuable guidance for the artificial fertilization and reproduction of
P. trituberculatus
.</description><identifier>ISSN: 0302-766X</identifier><identifier>EISSN: 1432-0878</identifier><identifier>DOI: 10.1007/s00441-021-03519-3</identifier><identifier>PMID: 34477967</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Analysis ; Animals ; Biomedical and Life Sciences ; Biomedicine ; Brachyura ; Crustaceans ; Cytoplasmic Dyneins - genetics ; Developmental stages ; Dynein ; Fertilization ; Human Genetics ; Mitochondria ; Molecular Medicine ; Portunus trituberculatus ; Prohibitin ; Proteomics ; Regular Article ; Retrograde transport ; Sperm ; Spermatogenesis ; Spermatogenesis - genetics ; Spermiogenesis ; Tubulin ; Tubulins</subject><ispartof>Cell and tissue research, 2021-10, Vol.386 (1), p.191-203</ispartof><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2021</rights><rights>2021. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.</rights><rights>COPYRIGHT 2021 Springer</rights><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c473t-ef0cb6a0f2a4633470621dbe1b03ab6618ca4ff734d3aa083d9ab5dc90e9b7a63</citedby><cites>FETCH-LOGICAL-c473t-ef0cb6a0f2a4633470621dbe1b03ab6618ca4ff734d3aa083d9ab5dc90e9b7a63</cites><orcidid>0000-0001-6630-6502</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34477967$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wei, Chao-Guang</creatorcontrib><creatorcontrib>Mu, Dan-Li</creatorcontrib><creatorcontrib>Tang, Dao-Jun</creatorcontrib><creatorcontrib>Zhu, Jun-Quan</creatorcontrib><creatorcontrib>Hou, Cong-Cong</creatorcontrib><title>Expression and functional analysis of cytoplasmic dynein during spermatogenesis in Portunus trituberculatus</title><title>Cell and tissue research</title><addtitle>Cell Tissue Res</addtitle><addtitle>Cell Tissue Res</addtitle><description>The mechanism of acrosome formation in the crab sperm is a hot topic in crustacean reproduction research. Dynein is a motor protein that performs microtubule-dependent retrograde transport and plays an essential role in spermatogenesis. However, whether cytoplasmic dynein participates in acrosome formation in the crab sperm remains poorly understood. In this study, we cloned the cytoplasmic dynein intermediate chain gene (
Pt-DIC
) from
Portunus trituberculatus
testis. Pt-DIC is composed of a p150glued-binding domain, a dynein light chain (DLC)-binding domain, and a dynein heavy chain (DHC)-binding domain. The
Pt-DIC
gene is widely expressed in different tissues, showing the highest expression in the testis, and it is expressed in different stages of spermatid development, indicating important functions in spermatogenesis. We further observed the colocalization of Pt-DIC and Pt-DHC, Pt-DHC and tubulin, and Pt-DHC and GM130, and the results indicated that cytoplasmic dynein may participate in nuclear shaping and acrosome formation via vesicle transport. In addition, we examined the colocalization of Pt-DHC and a mitochondrion (MT) tracker and that of Pt-DHC and prohibitin (PHB). The results indicated that cytoplasmic dynein participated in mitochondrial transport and mitochondrial degradation. Taken together, these results support the hypothesis that cytoplasmic dynein participates in acrosome formation, nuclear shaping, and mitochondrial transport during spermiogenesis in
P. trituberculatus
. This study will provide valuable guidance for the artificial fertilization and reproduction of
P. trituberculatus
.</description><subject>Analysis</subject><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Brachyura</subject><subject>Crustaceans</subject><subject>Cytoplasmic Dyneins - genetics</subject><subject>Developmental stages</subject><subject>Dynein</subject><subject>Fertilization</subject><subject>Human Genetics</subject><subject>Mitochondria</subject><subject>Molecular Medicine</subject><subject>Portunus trituberculatus</subject><subject>Prohibitin</subject><subject>Proteomics</subject><subject>Regular Article</subject><subject>Retrograde transport</subject><subject>Sperm</subject><subject>Spermatogenesis</subject><subject>Spermatogenesis - genetics</subject><subject>Spermiogenesis</subject><subject>Tubulin</subject><subject>Tubulins</subject><issn>0302-766X</issn><issn>1432-0878</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp9ktFqFTEQhoMo9lh9AS9kQRBvtiabbLJ7WUpbhYJeKHgXstnkNDUnWTMJ9Ly9WU-1VkRCCDP5_oGZ-RF6SfAJwVi8A4wZIy3u6qU9GVv6CG0Io12LBzE8RhtMcdcKzr8eoWcANxgTxvn4FB1RxoQYudigb-e3SzIALoZGhbmxJehcA-VrqPweHDTRNnqf4-IV7Jxu5n0wLjRzSS5sG1hM2qkctyaYFa4_n2LKJRRocnK5TCbp4lUu8Bw9scqDeXH3HqMvF-efz963Vx8vP5ydXrWaCZpbY7GeuMK2U4xTygTmHZknQyZM1cQ5GbRi1grKZqoUHug8qqmf9YjNOAnF6TF6e6i7pPi9GMhy50Ab71UwsYDsej7SgfYdrujrv9CbWFJtfKUG2pGhH_k9tVXeSBdszEnptag85XWOhIxkqNTJP6h6ZlPHFoOxruYfCN78Ibg2yudriL6s84eHYHcAdYoAyVi5JLdTaS8JlqsV5MEKslpB_rSCpFX06q61Mu3M_Fvya_cVoAcAlnWTJt33_p-yPwDIt78y</recordid><startdate>20211001</startdate><enddate>20211001</enddate><creator>Wei, Chao-Guang</creator><creator>Mu, Dan-Li</creator><creator>Tang, Dao-Jun</creator><creator>Zhu, Jun-Quan</creator><creator>Hou, Cong-Cong</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SS</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-6630-6502</orcidid></search><sort><creationdate>20211001</creationdate><title>Expression and functional analysis of cytoplasmic dynein during spermatogenesis in Portunus trituberculatus</title><author>Wei, Chao-Guang ; 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Dynein is a motor protein that performs microtubule-dependent retrograde transport and plays an essential role in spermatogenesis. However, whether cytoplasmic dynein participates in acrosome formation in the crab sperm remains poorly understood. In this study, we cloned the cytoplasmic dynein intermediate chain gene (
Pt-DIC
) from
Portunus trituberculatus
testis. Pt-DIC is composed of a p150glued-binding domain, a dynein light chain (DLC)-binding domain, and a dynein heavy chain (DHC)-binding domain. The
Pt-DIC
gene is widely expressed in different tissues, showing the highest expression in the testis, and it is expressed in different stages of spermatid development, indicating important functions in spermatogenesis. We further observed the colocalization of Pt-DIC and Pt-DHC, Pt-DHC and tubulin, and Pt-DHC and GM130, and the results indicated that cytoplasmic dynein may participate in nuclear shaping and acrosome formation via vesicle transport. In addition, we examined the colocalization of Pt-DHC and a mitochondrion (MT) tracker and that of Pt-DHC and prohibitin (PHB). The results indicated that cytoplasmic dynein participated in mitochondrial transport and mitochondrial degradation. Taken together, these results support the hypothesis that cytoplasmic dynein participates in acrosome formation, nuclear shaping, and mitochondrial transport during spermiogenesis in
P. trituberculatus
. This study will provide valuable guidance for the artificial fertilization and reproduction of
P. trituberculatus
.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>34477967</pmid><doi>10.1007/s00441-021-03519-3</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0001-6630-6502</orcidid></addata></record> |
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source | Springer Nature:Jisc Collections:Springer Nature Read and Publish 2023-2025: Springer Reading List |
subjects | Analysis Animals Biomedical and Life Sciences Biomedicine Brachyura Crustaceans Cytoplasmic Dyneins - genetics Developmental stages Dynein Fertilization Human Genetics Mitochondria Molecular Medicine Portunus trituberculatus Prohibitin Proteomics Regular Article Retrograde transport Sperm Spermatogenesis Spermatogenesis - genetics Spermiogenesis Tubulin Tubulins |
title | Expression and functional analysis of cytoplasmic dynein during spermatogenesis in Portunus trituberculatus |
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