The ZIP6/ZIP10 heteromer is essential for the zinc-mediated trigger of mitosis
Zinc has been known to be essential for cell division for over 40 years but the molecular pathways involved remain elusive. Cellular zinc import across biological membranes necessitates the help of zinc transporters such as the SLC39A family of ZIP transporters. We have discovered a molecular proces...
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| Veröffentlicht in: | Cellular and molecular life sciences : CMLS 2021-02, Vol.78 (4), p.1781-1798 |
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| creator | Nimmanon, Thirayost Ziliotto, Silvia Ogle, Olivia Burt, Anna Gee, Julia M. W. Andrews, Glen K. Kille, Pete Hogstrand, Christer Maret, Wolfgang Taylor, Kathryn M. |
| description | Zinc has been known to be essential for cell division for over 40 years but the molecular pathways involved remain elusive. Cellular zinc import across biological membranes necessitates the help of zinc transporters such as the SLC39A family of ZIP transporters. We have discovered a molecular process that explains why zinc is required for cell division, involving two highly regulated zinc transporters, as a heteromer of ZIP6 and ZIP10, providing the means of cellular zinc entry at a specific time of the cell cycle that initiates a pathway resulting in the onset of mitosis. Crucially, when the zinc influx across this heteromer is blocked by ZIP6 or ZIP10 specific antibodies, there is no evidence of mitosis, confirming the requirement for zinc influx as a trigger of mitosis. The zinc that influxes into cells to trigger mitosis additionally changes the phosphorylation state of STAT3 converting it from a transcription factor to a protein that complexes with this heteromer and pS
38
Stathmin, the form allowing microtubule rearrangement as required in mitosis. This discovery now explains the specific cellular role of ZIP6 and ZIP10 and how they have special importance in the mitosis process compared to other ZIP transporter family members. This finding offers new therapeutic opportunities for inhibition of cell division in the many proliferative diseases that exist, such as cancer. |
| doi_str_mv | 10.1007/s00018-020-03616-6 |
| format | Article |
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38
Stathmin, the form allowing microtubule rearrangement as required in mitosis. This discovery now explains the specific cellular role of ZIP6 and ZIP10 and how they have special importance in the mitosis process compared to other ZIP transporter family members. This finding offers new therapeutic opportunities for inhibition of cell division in the many proliferative diseases that exist, such as cancer.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-020-03616-6</identifier><identifier>PMID: 32797246</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Antibodies ; Biochemistry ; Biological membranes ; Biomedical and Life Sciences ; Biomedicine ; Carrier Proteins - genetics ; Cation Transport Proteins - genetics ; Cell Biology ; Cell cycle ; Cell division ; Gene Expression Regulation ; Humans ; Life Sciences ; MCF-7 Cells ; Mitosis ; Mitosis - genetics ; Original ; Original Article ; Phosphorylation ; Phosphorylation - genetics ; Protein Multimerization - genetics ; Signal Transduction - genetics ; Stat3 protein ; STAT3 Transcription Factor - genetics ; Zinc ; Zinc - chemistry ; Zinc - metabolism</subject><ispartof>Cellular and molecular life sciences : CMLS, 2021-02, Vol.78 (4), p.1781-1798</ispartof><rights>The Author(s) 2020</rights><rights>The Author(s) 2020. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-12858959193f32a6d9e03767c8577b2f0b333f57a1e8bc2766b3502210c53a283</citedby><cites>FETCH-LOGICAL-c474t-12858959193f32a6d9e03767c8577b2f0b333f57a1e8bc2766b3502210c53a283</cites><orcidid>0000-0002-9576-9490</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/PMC7904737/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7904737/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,41464,42533,51294,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32797246$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nimmanon, Thirayost</creatorcontrib><creatorcontrib>Ziliotto, Silvia</creatorcontrib><creatorcontrib>Ogle, Olivia</creatorcontrib><creatorcontrib>Burt, Anna</creatorcontrib><creatorcontrib>Gee, Julia M. W.</creatorcontrib><creatorcontrib>Andrews, Glen K.</creatorcontrib><creatorcontrib>Kille, Pete</creatorcontrib><creatorcontrib>Hogstrand, Christer</creatorcontrib><creatorcontrib>Maret, Wolfgang</creatorcontrib><creatorcontrib>Taylor, Kathryn M.</creatorcontrib><title>The ZIP6/ZIP10 heteromer is essential for the zinc-mediated trigger of mitosis</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell. Mol. Life Sci</addtitle><addtitle>Cell Mol Life Sci</addtitle><description>Zinc has been known to be essential for cell division for over 40 years but the molecular pathways involved remain elusive. Cellular zinc import across biological membranes necessitates the help of zinc transporters such as the SLC39A family of ZIP transporters. We have discovered a molecular process that explains why zinc is required for cell division, involving two highly regulated zinc transporters, as a heteromer of ZIP6 and ZIP10, providing the means of cellular zinc entry at a specific time of the cell cycle that initiates a pathway resulting in the onset of mitosis. Crucially, when the zinc influx across this heteromer is blocked by ZIP6 or ZIP10 specific antibodies, there is no evidence of mitosis, confirming the requirement for zinc influx as a trigger of mitosis. The zinc that influxes into cells to trigger mitosis additionally changes the phosphorylation state of STAT3 converting it from a transcription factor to a protein that complexes with this heteromer and pS
38
Stathmin, the form allowing microtubule rearrangement as required in mitosis. This discovery now explains the specific cellular role of ZIP6 and ZIP10 and how they have special importance in the mitosis process compared to other ZIP transporter family members. This finding offers new therapeutic opportunities for inhibition of cell division in the many proliferative diseases that exist, such as cancer.</description><subject>Antibodies</subject><subject>Biochemistry</subject><subject>Biological membranes</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Carrier Proteins - genetics</subject><subject>Cation Transport Proteins - genetics</subject><subject>Cell Biology</subject><subject>Cell cycle</subject><subject>Cell division</subject><subject>Gene Expression Regulation</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>MCF-7 Cells</subject><subject>Mitosis</subject><subject>Mitosis - genetics</subject><subject>Original</subject><subject>Original Article</subject><subject>Phosphorylation</subject><subject>Phosphorylation - genetics</subject><subject>Protein Multimerization - genetics</subject><subject>Signal Transduction - genetics</subject><subject>Stat3 protein</subject><subject>STAT3 Transcription Factor - genetics</subject><subject>Zinc</subject><subject>Zinc - chemistry</subject><subject>Zinc - metabolism</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kUlLBDEQhYMoLqN_wIM0ePHSWlk6y0WQwQ1EPYwgXkK6Jz0T6e5o0iPorzfjjOvBSxbqy8uregjtYjjEAOIoAgCWORDIgXLMc76CNjFLVwUCry7PXJL7DbQV42OiC0n4OtqgRChBGN9E16OpzR4ub_lRWjBkU9vb4FsbMhczG6PtemearPYh6xP55roqb-3Ymd6Osz64ySShvs5a1_vo4jZaq00T7c5yH6C7s9PR8CK_ujm_HJ5c5RUTrM8xkYVUhcKK1pQYPlYWqOCikoUQJamhpJTWhTDYyrIigvOSFkAIhqqghkg6QMcL3adZmexUyWYwjX4KrjXhVXvj9O9K56Z64l-0UMAEFUngYCkQ_PPMxl63Lla2aUxn_SxqwihjEjM1R_f_oI9-FrrUXqJUmqQkeO6ILKgq-BiDrb_MYNDzuPQiLp3i0h9xaZ4e7f1s4-vJZz4JoAsgplKXZv399z-y784ing8</recordid><startdate>20210201</startdate><enddate>20210201</enddate><creator>Nimmanon, Thirayost</creator><creator>Ziliotto, Silvia</creator><creator>Ogle, Olivia</creator><creator>Burt, Anna</creator><creator>Gee, Julia M. W.</creator><creator>Andrews, Glen K.</creator><creator>Kille, Pete</creator><creator>Hogstrand, Christer</creator><creator>Maret, Wolfgang</creator><creator>Taylor, Kathryn M.</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>C6C</scope><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>7X2</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>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-9576-9490</orcidid></search><sort><creationdate>20210201</creationdate><title>The ZIP6/ZIP10 heteromer is essential for the zinc-mediated trigger of mitosis</title><author>Nimmanon, Thirayost ; Ziliotto, Silvia ; Ogle, Olivia ; Burt, Anna ; Gee, Julia M. 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W.</au><au>Andrews, Glen K.</au><au>Kille, Pete</au><au>Hogstrand, Christer</au><au>Maret, Wolfgang</au><au>Taylor, Kathryn M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The ZIP6/ZIP10 heteromer is essential for the zinc-mediated trigger of mitosis</atitle><jtitle>Cellular and molecular life sciences : CMLS</jtitle><stitle>Cell. Mol. Life Sci</stitle><addtitle>Cell Mol Life Sci</addtitle><date>2021-02-01</date><risdate>2021</risdate><volume>78</volume><issue>4</issue><spage>1781</spage><epage>1798</epage><pages>1781-1798</pages><issn>1420-682X</issn><eissn>1420-9071</eissn><abstract>Zinc has been known to be essential for cell division for over 40 years but the molecular pathways involved remain elusive. Cellular zinc import across biological membranes necessitates the help of zinc transporters such as the SLC39A family of ZIP transporters. We have discovered a molecular process that explains why zinc is required for cell division, involving two highly regulated zinc transporters, as a heteromer of ZIP6 and ZIP10, providing the means of cellular zinc entry at a specific time of the cell cycle that initiates a pathway resulting in the onset of mitosis. Crucially, when the zinc influx across this heteromer is blocked by ZIP6 or ZIP10 specific antibodies, there is no evidence of mitosis, confirming the requirement for zinc influx as a trigger of mitosis. The zinc that influxes into cells to trigger mitosis additionally changes the phosphorylation state of STAT3 converting it from a transcription factor to a protein that complexes with this heteromer and pS
38
Stathmin, the form allowing microtubule rearrangement as required in mitosis. This discovery now explains the specific cellular role of ZIP6 and ZIP10 and how they have special importance in the mitosis process compared to other ZIP transporter family members. This finding offers new therapeutic opportunities for inhibition of cell division in the many proliferative diseases that exist, such as cancer.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>32797246</pmid><doi>10.1007/s00018-020-03616-6</doi><tpages>18</tpages><orcidid>https://orcid.org/0000-0002-9576-9490</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Antibodies Biochemistry Biological membranes Biomedical and Life Sciences Biomedicine Carrier Proteins - genetics Cation Transport Proteins - genetics Cell Biology Cell cycle Cell division Gene Expression Regulation Humans Life Sciences MCF-7 Cells Mitosis Mitosis - genetics Original Original Article Phosphorylation Phosphorylation - genetics Protein Multimerization - genetics Signal Transduction - genetics Stat3 protein STAT3 Transcription Factor - genetics Zinc Zinc - chemistry Zinc - metabolism |
| title | The ZIP6/ZIP10 heteromer is essential for the zinc-mediated trigger of mitosis |
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