The meiosis-specific Cdc20 family-member Ama1 promotes binding of the Ssp2 activator to the Smk1 MAP kinase
Smk1 is a meiosis-specific MAP kinase (MAPK) in budding yeast that is required for spore formation. It is localized to prospore membranes (PSMs), the structures that engulf haploid cells during meiosis II (MII). Similar to canonically activated MAPKs, Smk1 is controlled by phosphorylation of its act...
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| Veröffentlicht in: | Molecular biology of the cell 2018-01, Vol.29 (1), p.66-74 |
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| creator | Omerza, Gregory Tio, Chong Wai Philips, Timothy Diamond, Aviva Neiman, Aaron M Winter, Edward |
| description | Smk1 is a meiosis-specific MAP kinase (MAPK) in budding yeast that is required for spore formation. It is localized to prospore membranes (PSMs), the structures that engulf haploid cells during meiosis II (MII). Similar to canonically activated MAPKs, Smk1 is controlled by phosphorylation of its activation-loop threonine (T) and tyrosine (Y). However, activation loop phosphorylation occurs via a noncanonical two-step mechanism in which 1) the cyclin-dependent kinase activating kinase Cak1 phosphorylaytes T207 during MI, and 2) Smk1 autophosphorylates Y209 as MII draws to a close. Autophosphorylation of Y209 and catalytic activity for substrates require Ssp2, a meiosis-specific protein that is translationally repressed until anaphase of MII. Ama1 is a meiosis-specific targeting subunit of the anaphase-promoting complex/cyclosome that regulates multiple steps in meiotic development, including exit from MII. Here, we show that Ama1 activates autophosphorylation of Smk1 on Y209 by promoting formation of the Ssp2/Smk1 complex at PSMs. These findings link meiotic exit to Smk1 activation and spore wall assembly. |
| doi_str_mv | 10.1091/mbc.E17-07-0473 |
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It is localized to prospore membranes (PSMs), the structures that engulf haploid cells during meiosis II (MII). Similar to canonically activated MAPKs, Smk1 is controlled by phosphorylation of its activation-loop threonine (T) and tyrosine (Y). However, activation loop phosphorylation occurs via a noncanonical two-step mechanism in which 1) the cyclin-dependent kinase activating kinase Cak1 phosphorylaytes T207 during MI, and 2) Smk1 autophosphorylates Y209 as MII draws to a close. Autophosphorylation of Y209 and catalytic activity for substrates require Ssp2, a meiosis-specific protein that is translationally repressed until anaphase of MII. Ama1 is a meiosis-specific targeting subunit of the anaphase-promoting complex/cyclosome that regulates multiple steps in meiotic development, including exit from MII. Here, we show that Ama1 activates autophosphorylation of Smk1 on Y209 by promoting formation of the Ssp2/Smk1 complex at PSMs. These findings link meiotic exit to Smk1 activation and spore wall assembly.</description><identifier>ISSN: 1059-1524</identifier><identifier>EISSN: 1939-4586</identifier><identifier>DOI: 10.1091/mbc.E17-07-0473</identifier><identifier>PMID: 29118076</identifier><language>eng</language><publisher>United States: The American Society for Cell Biology</publisher><subject>Cdc20 Proteins - metabolism ; Cell Membrane - metabolism ; Enzyme Stability ; Meiosis ; Mitogen-Activated Protein Kinases - metabolism ; Models, Biological ; Mutation - genetics ; Phosphorylation ; Phosphotyrosine - metabolism ; Protein Binding ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - metabolism ; Spores, Fungal - metabolism</subject><ispartof>Molecular biology of the cell, 2018-01, Vol.29 (1), p.66-74</ispartof><rights>2018 Omerza et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).</rights><rights>2018 Omerza This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License ( ). 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-e9a05de4ebfafc7d4dc15e6ce8f73bda6b44067e4d33be4fcfa23ed8fe2dce2d3</citedby><cites>FETCH-LOGICAL-c393t-e9a05de4ebfafc7d4dc15e6ce8f73bda6b44067e4d33be4fcfa23ed8fe2dce2d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5746067/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5746067/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,725,778,782,883,27907,27908,53774,53776</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29118076$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Solomon, Mark J.</contributor><creatorcontrib>Omerza, Gregory</creatorcontrib><creatorcontrib>Tio, Chong Wai</creatorcontrib><creatorcontrib>Philips, Timothy</creatorcontrib><creatorcontrib>Diamond, Aviva</creatorcontrib><creatorcontrib>Neiman, Aaron M</creatorcontrib><creatorcontrib>Winter, Edward</creatorcontrib><title>The meiosis-specific Cdc20 family-member Ama1 promotes binding of the Ssp2 activator to the Smk1 MAP kinase</title><title>Molecular biology of the cell</title><addtitle>Mol Biol Cell</addtitle><description>Smk1 is a meiosis-specific MAP kinase (MAPK) in budding yeast that is required for spore formation. It is localized to prospore membranes (PSMs), the structures that engulf haploid cells during meiosis II (MII). Similar to canonically activated MAPKs, Smk1 is controlled by phosphorylation of its activation-loop threonine (T) and tyrosine (Y). However, activation loop phosphorylation occurs via a noncanonical two-step mechanism in which 1) the cyclin-dependent kinase activating kinase Cak1 phosphorylaytes T207 during MI, and 2) Smk1 autophosphorylates Y209 as MII draws to a close. Autophosphorylation of Y209 and catalytic activity for substrates require Ssp2, a meiosis-specific protein that is translationally repressed until anaphase of MII. Ama1 is a meiosis-specific targeting subunit of the anaphase-promoting complex/cyclosome that regulates multiple steps in meiotic development, including exit from MII. Here, we show that Ama1 activates autophosphorylation of Smk1 on Y209 by promoting formation of the Ssp2/Smk1 complex at PSMs. These findings link meiotic exit to Smk1 activation and spore wall assembly.</description><subject>Cdc20 Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Enzyme Stability</subject><subject>Meiosis</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Models, Biological</subject><subject>Mutation - genetics</subject><subject>Phosphorylation</subject><subject>Phosphotyrosine - metabolism</subject><subject>Protein Binding</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Spores, Fungal - metabolism</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkdtLBCEUhyWK7s-9hY-9TOno3F6CZdkuUBRUz-Locdd2HCedXdj_PmMrCo4ox9_5FD6Ezii5pKShV65VlzNaZSQVr9gOOqQNazJe1OVuOpOiyWiR8wN0FOM7IZTzstpHB3lDaU2q8hAtXxeAHVgfbcziAMoaq_BUq5xgI53tNpkD10LAEycpHoJ3foSIW9tr28-xN3hMhJc45Fiq0a7l6AMe_bbrlhQ_Tp7x0vYywgnaM7KLcPq9H6O3m9nr9C57eLq9n04eMsUaNmbQSFJo4NAaaVSluVa0gFJBbSrWalm2nJOyAq4Za4EbZWTOQNcGcq3SYsfoessdVq2D1OvHIDsxBOtk2Agvrfh_09uFmPu1KCpeJnICXHwDgv9YQRyFs1FB18ke_CoK2pQ5z2vCeYpebaMq-BgDmN9nKBFfikRSJJIiQVIlRWni_O_vfvM_TtgnKD-P6g</recordid><startdate>20180101</startdate><enddate>20180101</enddate><creator>Omerza, Gregory</creator><creator>Tio, Chong Wai</creator><creator>Philips, Timothy</creator><creator>Diamond, Aviva</creator><creator>Neiman, Aaron M</creator><creator>Winter, Edward</creator><general>The American Society for Cell 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><scope>5PM</scope></search><sort><creationdate>20180101</creationdate><title>The meiosis-specific Cdc20 family-member Ama1 promotes binding of the Ssp2 activator to the Smk1 MAP kinase</title><author>Omerza, Gregory ; Tio, Chong Wai ; Philips, Timothy ; Diamond, Aviva ; Neiman, Aaron M ; Winter, Edward</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-e9a05de4ebfafc7d4dc15e6ce8f73bda6b44067e4d33be4fcfa23ed8fe2dce2d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Cdc20 Proteins - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Enzyme Stability</topic><topic>Meiosis</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Models, Biological</topic><topic>Mutation - genetics</topic><topic>Phosphorylation</topic><topic>Phosphotyrosine - metabolism</topic><topic>Protein Binding</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Spores, Fungal - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Omerza, Gregory</creatorcontrib><creatorcontrib>Tio, Chong Wai</creatorcontrib><creatorcontrib>Philips, Timothy</creatorcontrib><creatorcontrib>Diamond, Aviva</creatorcontrib><creatorcontrib>Neiman, Aaron M</creatorcontrib><creatorcontrib>Winter, Edward</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Omerza, Gregory</au><au>Tio, Chong Wai</au><au>Philips, Timothy</au><au>Diamond, Aviva</au><au>Neiman, Aaron M</au><au>Winter, Edward</au><au>Solomon, Mark J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The meiosis-specific Cdc20 family-member Ama1 promotes binding of the Ssp2 activator to the Smk1 MAP kinase</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2018-01-01</date><risdate>2018</risdate><volume>29</volume><issue>1</issue><spage>66</spage><epage>74</epage><pages>66-74</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>Smk1 is a meiosis-specific MAP kinase (MAPK) in budding yeast that is required for spore formation. 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| subjects | Cdc20 Proteins - metabolism Cell Membrane - metabolism Enzyme Stability Meiosis Mitogen-Activated Protein Kinases - metabolism Models, Biological Mutation - genetics Phosphorylation Phosphotyrosine - metabolism Protein Binding Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Spores, Fungal - metabolism |
| title | The meiosis-specific Cdc20 family-member Ama1 promotes binding of the Ssp2 activator to the Smk1 MAP kinase |
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