Loading…
Spire localization via zinc finger—containing domain is crucial for the asymmetric division of mouse oocyte
ABSTRACT Zinc plays an essential role in mammalian oocyte maturation, fertilization, and early embryogenesis, and depletion of zinc impairs cell cycle control, asymmetric division, and cytokinesis in oocyte. We report that zinc, via the actin nucleator Spire, acts as an essential regulator of the ac...
Saved in:
| Published in: | The FASEB journal 2019-03, Vol.33 (3), p.4432-4447 |
|---|---|
| Main Authors: | , , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c389R-c950acc3d9d0d500d9bae06ce32c6e1f0a9ce749d5ba5d08c679164632ae64f3 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c389R-c950acc3d9d0d500d9bae06ce32c6e1f0a9ce749d5ba5d08c679164632ae64f3 |
| container_end_page | 4447 |
| container_issue | 3 |
| container_start_page | 4432 |
| container_title | The FASEB journal |
| container_volume | 33 |
| creator | Jo, Yu-Jin Lee, In-Won Jung, Seung-Min Kwon, Jeongwoo Kim, Nam-Hyung Namgoong, Suk |
| description | ABSTRACT
Zinc plays an essential role in mammalian oocyte maturation, fertilization, and early embryogenesis, and depletion of zinc impairs cell cycle control, asymmetric division, and cytokinesis in oocyte. We report that zinc, via the actin nucleator Spire, acts as an essential regulator of the actin cytoskeleton remodeling during mouse oocyte maturation and fertilization. Depletion of zinc in the mouse oocyte impaired cortical and cytoplasmic actin formation. Spire is colocalized with zinc‐containing vesicles via its zinc finger‐containing Fab1, YOTB, Vac 1, EEA1 (FYVE) domain. Improper localization of Spire by zinc depletion or mutations in the FYVE domain impair cytoplasmic actin mesh formations and asymmetric division and cytokinesis of oocyte. All 3 major domains of the Spire are required for its proper localization and activity. After fertilization or parthenogenetic activation, Spire localization was dramatically altered following zinc release from the oocyte. Collectively, our data reveal novel roles for zinc in the regulation of the actin nucleator Spire by controlling its localization in mammalian oocyte.—Jo, Y.‐J., Lee, I.‐W., Jung, S.‐M., Kwon, J., Kim, N.‐H., Namgoong, S. Spire localization via zinc finger—containing domain is crucial for the asymmetric division of mouse oocyte. FASEB J. 33, 4432–4447 (2019). www.fasebj.org |
| doi_str_mv | 10.1096/fj.201801905R |
| format | article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2158245019</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2158245019</sourcerecordid><originalsourceid>FETCH-LOGICAL-c389R-c950acc3d9d0d500d9bae06ce32c6e1f0a9ce749d5ba5d08c679164632ae64f3</originalsourceid><addsrcrecordid>eNp9kE1PGzEQQC0EgvBx7BX5yGXpeB07a3GiqCmtkCol3FfOeNw62l0HexMUTv0R_YX9JSwKhZ56mhnp6Wn0GPsg4FKA0R_98rIEUYEwoGZ7bCSUhEJXGvbZCCpTFlrL6ogd57wEAAFCH7IjCUpNQFYj1s5XIRFvItomPNk-xI5vguVPoUPuQ_eD0p9fvzF2vQ3dcHIX22HjIXNMawy24T4m3v8kbvO2balPAbkLm5BfVNHzNq4z8Rhx29MpO_C2yXT2Ok_Y_fTz_c1tcff9y9eb67sCZWVmBRoFFlE648ApAGcWlkAjyRI1CQ_WIE3GxqmFVQ4q1BMj9FjL0pIee3nCLnbaVYoPa8p93YaM1DS2o-GbuhSqKsdqaDagxQ7FFHNO5OtVCq1N21pA_RK49sv6PfDAn7-q14uW3Bv9t-gAXO2Ax9DQ9v-2ejr_VE6__aN_BmSSisg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2158245019</pqid></control><display><type>article</type><title>Spire localization via zinc finger—containing domain is crucial for the asymmetric division of mouse oocyte</title><source>Wiley</source><creator>Jo, Yu-Jin ; Lee, In-Won ; Jung, Seung-Min ; Kwon, Jeongwoo ; Kim, Nam-Hyung ; Namgoong, Suk</creator><creatorcontrib>Jo, Yu-Jin ; Lee, In-Won ; Jung, Seung-Min ; Kwon, Jeongwoo ; Kim, Nam-Hyung ; Namgoong, Suk</creatorcontrib><description>ABSTRACT
Zinc plays an essential role in mammalian oocyte maturation, fertilization, and early embryogenesis, and depletion of zinc impairs cell cycle control, asymmetric division, and cytokinesis in oocyte. We report that zinc, via the actin nucleator Spire, acts as an essential regulator of the actin cytoskeleton remodeling during mouse oocyte maturation and fertilization. Depletion of zinc in the mouse oocyte impaired cortical and cytoplasmic actin formation. Spire is colocalized with zinc‐containing vesicles via its zinc finger‐containing Fab1, YOTB, Vac 1, EEA1 (FYVE) domain. Improper localization of Spire by zinc depletion or mutations in the FYVE domain impair cytoplasmic actin mesh formations and asymmetric division and cytokinesis of oocyte. All 3 major domains of the Spire are required for its proper localization and activity. After fertilization or parthenogenetic activation, Spire localization was dramatically altered following zinc release from the oocyte. Collectively, our data reveal novel roles for zinc in the regulation of the actin nucleator Spire by controlling its localization in mammalian oocyte.—Jo, Y.‐J., Lee, I.‐W., Jung, S.‐M., Kwon, J., Kim, N.‐H., Namgoong, S. Spire localization via zinc finger—containing domain is crucial for the asymmetric division of mouse oocyte. FASEB J. 33, 4432–4447 (2019). www.fasebj.org</description><identifier>ISSN: 0892-6638</identifier><identifier>EISSN: 1530-6860</identifier><identifier>DOI: 10.1096/fj.201801905R</identifier><identifier>PMID: 30557038</identifier><language>eng</language><publisher>United States: Federation of American Societies for Experimental Biology</publisher><subject>Actin Cytoskeleton - physiology ; Actin Cytoskeleton - ultrastructure ; Amino Acid Sequence ; Animals ; Asymmetric Cell Division - physiology ; asymmetric division ; Cytokinesis ; Cytoplasmic Vesicles - metabolism ; Female ; Formins - metabolism ; Meiosis - physiology ; Mice ; Microfilament Proteins - antagonists & inhibitors ; Microfilament Proteins - chemistry ; Microfilament Proteins - genetics ; Microfilament Proteins - physiology ; Nerve Tissue Proteins - antagonists & inhibitors ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - metabolism ; Nerve Tissue Proteins - physiology ; Oocytes - cytology ; Oocytes - metabolism ; Parthenogenesis - drug effects ; Point Mutation ; Protein Interaction Mapping ; Protein Transport ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Soire ; Sperm Injections, Intracytoplasmic ; Spindle Apparatus - physiology ; Spindle Apparatus - ultrastructure ; Strontium - pharmacology ; Zinc - physiology ; zinc finger ; Zinc Fingers - physiology</subject><ispartof>The FASEB journal, 2019-03, Vol.33 (3), p.4432-4447</ispartof><rights>FASEB</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389R-c950acc3d9d0d500d9bae06ce32c6e1f0a9ce749d5ba5d08c679164632ae64f3</citedby><cites>FETCH-LOGICAL-c389R-c950acc3d9d0d500d9bae06ce32c6e1f0a9ce749d5ba5d08c679164632ae64f3</cites></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/30557038$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jo, Yu-Jin</creatorcontrib><creatorcontrib>Lee, In-Won</creatorcontrib><creatorcontrib>Jung, Seung-Min</creatorcontrib><creatorcontrib>Kwon, Jeongwoo</creatorcontrib><creatorcontrib>Kim, Nam-Hyung</creatorcontrib><creatorcontrib>Namgoong, Suk</creatorcontrib><title>Spire localization via zinc finger—containing domain is crucial for the asymmetric division of mouse oocyte</title><title>The FASEB journal</title><addtitle>FASEB J</addtitle><description>ABSTRACT
Zinc plays an essential role in mammalian oocyte maturation, fertilization, and early embryogenesis, and depletion of zinc impairs cell cycle control, asymmetric division, and cytokinesis in oocyte. We report that zinc, via the actin nucleator Spire, acts as an essential regulator of the actin cytoskeleton remodeling during mouse oocyte maturation and fertilization. Depletion of zinc in the mouse oocyte impaired cortical and cytoplasmic actin formation. Spire is colocalized with zinc‐containing vesicles via its zinc finger‐containing Fab1, YOTB, Vac 1, EEA1 (FYVE) domain. Improper localization of Spire by zinc depletion or mutations in the FYVE domain impair cytoplasmic actin mesh formations and asymmetric division and cytokinesis of oocyte. All 3 major domains of the Spire are required for its proper localization and activity. After fertilization or parthenogenetic activation, Spire localization was dramatically altered following zinc release from the oocyte. Collectively, our data reveal novel roles for zinc in the regulation of the actin nucleator Spire by controlling its localization in mammalian oocyte.—Jo, Y.‐J., Lee, I.‐W., Jung, S.‐M., Kwon, J., Kim, N.‐H., Namgoong, S. Spire localization via zinc finger—containing domain is crucial for the asymmetric division of mouse oocyte. FASEB J. 33, 4432–4447 (2019). www.fasebj.org</description><subject>Actin Cytoskeleton - physiology</subject><subject>Actin Cytoskeleton - ultrastructure</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Asymmetric Cell Division - physiology</subject><subject>asymmetric division</subject><subject>Cytokinesis</subject><subject>Cytoplasmic Vesicles - metabolism</subject><subject>Female</subject><subject>Formins - metabolism</subject><subject>Meiosis - physiology</subject><subject>Mice</subject><subject>Microfilament Proteins - antagonists & inhibitors</subject><subject>Microfilament Proteins - chemistry</subject><subject>Microfilament Proteins - genetics</subject><subject>Microfilament Proteins - physiology</subject><subject>Nerve Tissue Proteins - antagonists & inhibitors</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Nerve Tissue Proteins - physiology</subject><subject>Oocytes - cytology</subject><subject>Oocytes - metabolism</subject><subject>Parthenogenesis - drug effects</subject><subject>Point Mutation</subject><subject>Protein Interaction Mapping</subject><subject>Protein Transport</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Soire</subject><subject>Sperm Injections, Intracytoplasmic</subject><subject>Spindle Apparatus - physiology</subject><subject>Spindle Apparatus - ultrastructure</subject><subject>Strontium - pharmacology</subject><subject>Zinc - physiology</subject><subject>zinc finger</subject><subject>Zinc Fingers - physiology</subject><issn>0892-6638</issn><issn>1530-6860</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNp9kE1PGzEQQC0EgvBx7BX5yGXpeB07a3GiqCmtkCol3FfOeNw62l0HexMUTv0R_YX9JSwKhZ56mhnp6Wn0GPsg4FKA0R_98rIEUYEwoGZ7bCSUhEJXGvbZCCpTFlrL6ogd57wEAAFCH7IjCUpNQFYj1s5XIRFvItomPNk-xI5vguVPoUPuQ_eD0p9fvzF2vQ3dcHIX22HjIXNMawy24T4m3v8kbvO2balPAbkLm5BfVNHzNq4z8Rhx29MpO_C2yXT2Ok_Y_fTz_c1tcff9y9eb67sCZWVmBRoFFlE648ApAGcWlkAjyRI1CQ_WIE3GxqmFVQ4q1BMj9FjL0pIee3nCLnbaVYoPa8p93YaM1DS2o-GbuhSqKsdqaDagxQ7FFHNO5OtVCq1N21pA_RK49sv6PfDAn7-q14uW3Bv9t-gAXO2Ax9DQ9v-2ejr_VE6__aN_BmSSisg</recordid><startdate>201903</startdate><enddate>201903</enddate><creator>Jo, Yu-Jin</creator><creator>Lee, In-Won</creator><creator>Jung, Seung-Min</creator><creator>Kwon, Jeongwoo</creator><creator>Kim, Nam-Hyung</creator><creator>Namgoong, Suk</creator><general>Federation of American Societies for Experimental Biology</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>7X8</scope></search><sort><creationdate>201903</creationdate><title>Spire localization via zinc finger—containing domain is crucial for the asymmetric division of mouse oocyte</title><author>Jo, Yu-Jin ; Lee, In-Won ; Jung, Seung-Min ; Kwon, Jeongwoo ; Kim, Nam-Hyung ; Namgoong, Suk</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389R-c950acc3d9d0d500d9bae06ce32c6e1f0a9ce749d5ba5d08c679164632ae64f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Actin Cytoskeleton - physiology</topic><topic>Actin Cytoskeleton - ultrastructure</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Asymmetric Cell Division - physiology</topic><topic>asymmetric division</topic><topic>Cytokinesis</topic><topic>Cytoplasmic Vesicles - metabolism</topic><topic>Female</topic><topic>Formins - metabolism</topic><topic>Meiosis - physiology</topic><topic>Mice</topic><topic>Microfilament Proteins - antagonists & inhibitors</topic><topic>Microfilament Proteins - chemistry</topic><topic>Microfilament Proteins - genetics</topic><topic>Microfilament Proteins - physiology</topic><topic>Nerve Tissue Proteins - antagonists & inhibitors</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Nerve Tissue Proteins - physiology</topic><topic>Oocytes - cytology</topic><topic>Oocytes - metabolism</topic><topic>Parthenogenesis - drug effects</topic><topic>Point Mutation</topic><topic>Protein Interaction Mapping</topic><topic>Protein Transport</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Soire</topic><topic>Sperm Injections, Intracytoplasmic</topic><topic>Spindle Apparatus - physiology</topic><topic>Spindle Apparatus - ultrastructure</topic><topic>Strontium - pharmacology</topic><topic>Zinc - physiology</topic><topic>zinc finger</topic><topic>Zinc Fingers - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jo, Yu-Jin</creatorcontrib><creatorcontrib>Lee, In-Won</creatorcontrib><creatorcontrib>Jung, Seung-Min</creatorcontrib><creatorcontrib>Kwon, Jeongwoo</creatorcontrib><creatorcontrib>Kim, Nam-Hyung</creatorcontrib><creatorcontrib>Namgoong, Suk</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><jtitle>The FASEB journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jo, Yu-Jin</au><au>Lee, In-Won</au><au>Jung, Seung-Min</au><au>Kwon, Jeongwoo</au><au>Kim, Nam-Hyung</au><au>Namgoong, Suk</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Spire localization via zinc finger—containing domain is crucial for the asymmetric division of mouse oocyte</atitle><jtitle>The FASEB journal</jtitle><addtitle>FASEB J</addtitle><date>2019-03</date><risdate>2019</risdate><volume>33</volume><issue>3</issue><spage>4432</spage><epage>4447</epage><pages>4432-4447</pages><issn>0892-6638</issn><eissn>1530-6860</eissn><abstract>ABSTRACT
Zinc plays an essential role in mammalian oocyte maturation, fertilization, and early embryogenesis, and depletion of zinc impairs cell cycle control, asymmetric division, and cytokinesis in oocyte. We report that zinc, via the actin nucleator Spire, acts as an essential regulator of the actin cytoskeleton remodeling during mouse oocyte maturation and fertilization. Depletion of zinc in the mouse oocyte impaired cortical and cytoplasmic actin formation. Spire is colocalized with zinc‐containing vesicles via its zinc finger‐containing Fab1, YOTB, Vac 1, EEA1 (FYVE) domain. Improper localization of Spire by zinc depletion or mutations in the FYVE domain impair cytoplasmic actin mesh formations and asymmetric division and cytokinesis of oocyte. All 3 major domains of the Spire are required for its proper localization and activity. After fertilization or parthenogenetic activation, Spire localization was dramatically altered following zinc release from the oocyte. Collectively, our data reveal novel roles for zinc in the regulation of the actin nucleator Spire by controlling its localization in mammalian oocyte.—Jo, Y.‐J., Lee, I.‐W., Jung, S.‐M., Kwon, J., Kim, N.‐H., Namgoong, S. Spire localization via zinc finger—containing domain is crucial for the asymmetric division of mouse oocyte. FASEB J. 33, 4432–4447 (2019). www.fasebj.org</abstract><cop>United States</cop><pub>Federation of American Societies for Experimental Biology</pub><pmid>30557038</pmid><doi>10.1096/fj.201801905R</doi><tpages>16</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0892-6638 |
| ispartof | The FASEB journal, 2019-03, Vol.33 (3), p.4432-4447 |
| issn | 0892-6638 1530-6860 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2158245019 |
| source | Wiley |
| subjects | Actin Cytoskeleton - physiology Actin Cytoskeleton - ultrastructure Amino Acid Sequence Animals Asymmetric Cell Division - physiology asymmetric division Cytokinesis Cytoplasmic Vesicles - metabolism Female Formins - metabolism Meiosis - physiology Mice Microfilament Proteins - antagonists & inhibitors Microfilament Proteins - chemistry Microfilament Proteins - genetics Microfilament Proteins - physiology Nerve Tissue Proteins - antagonists & inhibitors Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism Nerve Tissue Proteins - physiology Oocytes - cytology Oocytes - metabolism Parthenogenesis - drug effects Point Mutation Protein Interaction Mapping Protein Transport Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid Soire Sperm Injections, Intracytoplasmic Spindle Apparatus - physiology Spindle Apparatus - ultrastructure Strontium - pharmacology Zinc - physiology zinc finger Zinc Fingers - physiology |
| title | Spire localization via zinc finger—containing domain is crucial for the asymmetric division of mouse oocyte |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T22%3A58%3A42IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Spire%20localization%20via%20zinc%20finger%E2%80%94containing%20domain%20is%20crucial%20for%20the%20asymmetric%20division%20of%20mouse%20oocyte&rft.jtitle=The%20FASEB%20journal&rft.au=Jo,%20Yu-Jin&rft.date=2019-03&rft.volume=33&rft.issue=3&rft.spage=4432&rft.epage=4447&rft.pages=4432-4447&rft.issn=0892-6638&rft.eissn=1530-6860&rft_id=info:doi/10.1096/fj.201801905R&rft_dat=%3Cproquest_cross%3E2158245019%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c389R-c950acc3d9d0d500d9bae06ce32c6e1f0a9ce749d5ba5d08c679164632ae64f3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2158245019&rft_id=info:pmid/30557038&rfr_iscdi=true |