Cdc5-dependent asymmetric localization of bfa1 fine-tunes timely mitotic exit
In budding yeast, the major regulator of the mitotic exit network (MEN) is Tem1, a GTPase, which is inhibited by the GTPase-activating protein (GAP), Bfa1/Bub2. Asymmetric Bfa1 localization to the bud-directed spindle pole body (SPB) during metaphase also controls mitotic exit, but the molecular mec...
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description | In budding yeast, the major regulator of the mitotic exit network (MEN) is Tem1, a GTPase, which is inhibited by the GTPase-activating protein (GAP), Bfa1/Bub2. Asymmetric Bfa1 localization to the bud-directed spindle pole body (SPB) during metaphase also controls mitotic exit, but the molecular mechanism and function of this localization are not well understood, particularly in unperturbed cells. We identified four novel Cdc5 target residues within the Bfa1 C-terminus: (452)S, (453)S, (454)S, and (559)S. A Bfa1 mutant in which all of these residues had been changed to alanine (Bfa1(4A)) persisted on both SPBs at anaphase and was hypo-phosphorylated, despite retaining its GAP activity for Tem1. A Bfa1 phospho-mimetic mutant in which all of these residues were switched to aspartate (Bfa1(4D)) always localized asymmetrically to the SPB. These observations demonstrate that asymmetric localization of Bfa1 is tightly linked to its Cdc5-dependent phosphorylation, but not to its GAP activity. Consistent with this, in kinase-defective cdc5-2 cells Bfa1 was not phosphorylated and localized to both SPBs, whereas Bfa1(4D) was asymmetrically localized. BFA1(4A) cells progressed through anaphase normally but displayed delayed mitotic exit in unperturbed cell cycles, while BFA1(4D) cells underwent mitotic exit with the same kinetics as wild-type cells. We suggest that Cdc5 induces the asymmetric distribution of Bfa1 to the bud-directed SPB independently of Bfa1 GAP activity at anaphase and that Bfa1 asymmetry fine-tunes the timing of MEN activation in unperturbed cell cycles. |
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Asymmetric Bfa1 localization to the bud-directed spindle pole body (SPB) during metaphase also controls mitotic exit, but the molecular mechanism and function of this localization are not well understood, particularly in unperturbed cells. We identified four novel Cdc5 target residues within the Bfa1 C-terminus: (452)S, (453)S, (454)S, and (559)S. A Bfa1 mutant in which all of these residues had been changed to alanine (Bfa1(4A)) persisted on both SPBs at anaphase and was hypo-phosphorylated, despite retaining its GAP activity for Tem1. A Bfa1 phospho-mimetic mutant in which all of these residues were switched to aspartate (Bfa1(4D)) always localized asymmetrically to the SPB. These observations demonstrate that asymmetric localization of Bfa1 is tightly linked to its Cdc5-dependent phosphorylation, but not to its GAP activity. Consistent with this, in kinase-defective cdc5-2 cells Bfa1 was not phosphorylated and localized to both SPBs, whereas Bfa1(4D) was asymmetrically localized. BFA1(4A) cells progressed through anaphase normally but displayed delayed mitotic exit in unperturbed cell cycles, while BFA1(4D) cells underwent mitotic exit with the same kinetics as wild-type cells. We suggest that Cdc5 induces the asymmetric distribution of Bfa1 to the bud-directed SPB independently of Bfa1 GAP activity at anaphase and that Bfa1 asymmetry fine-tunes the timing of MEN activation in unperturbed cell cycles.</description><identifier>ISSN: 1553-7404</identifier><identifier>ISSN: 1553-7390</identifier><identifier>EISSN: 1553-7404</identifier><identifier>DOI: 10.1371/journal.pgen.1002450</identifier><identifier>PMID: 22253605</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Alanine - genetics ; Anaphase - genetics ; Aspartic Acid - genetics ; Biology ; Cell cycle ; Cell Cycle - genetics ; Cell Cycle Proteins - genetics ; Cell division ; Cyclin-dependent kinases ; Cytoskeletal Proteins - genetics ; GTPase-Activating Proteins - genetics ; Kinases ; Metaphase - genetics ; Mitosis - genetics ; Mutation ; Phosphorylation ; Protein Interaction Domains and Motifs - genetics ; Protein Kinases - genetics ; Protein-Serine-Threonine Kinases - genetics ; Proteins ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins - genetics ; Serine - genetics ; Spindle Apparatus - genetics</subject><ispartof>PLoS genetics, 2012-01, Vol.8 (1), p.e1002450-e1002450</ispartof><rights>2012 Kim et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Kim J, Luo G, Bahk YY, Song K (2012) Cdc5-Dependent Asymmetric Localization of Bfa1 Fine-Tunes Timely Mitotic Exit. PLoS Genet 8(1): e1002450. doi:10.1371/journal.pgen.1002450</rights><rights>Kim et al. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-c8b56f3f225f700ddd40dbdfa4317b001baa5005d37aff30c10eb75048b9973b3</citedby><cites>FETCH-LOGICAL-c557t-c8b56f3f225f700ddd40dbdfa4317b001baa5005d37aff30c10eb75048b9973b3</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/PMC3257293/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3257293/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22253605$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Cohen-Fix, Orna</contributor><creatorcontrib>Kim, Junwon</creatorcontrib><creatorcontrib>Luo, Guangming</creatorcontrib><creatorcontrib>Bahk, Young Yil</creatorcontrib><creatorcontrib>Song, Kiwon</creatorcontrib><title>Cdc5-dependent asymmetric localization of bfa1 fine-tunes timely mitotic exit</title><title>PLoS genetics</title><addtitle>PLoS Genet</addtitle><description>In budding yeast, the major regulator of the mitotic exit network (MEN) is Tem1, a GTPase, which is inhibited by the GTPase-activating protein (GAP), Bfa1/Bub2. Asymmetric Bfa1 localization to the bud-directed spindle pole body (SPB) during metaphase also controls mitotic exit, but the molecular mechanism and function of this localization are not well understood, particularly in unperturbed cells. We identified four novel Cdc5 target residues within the Bfa1 C-terminus: (452)S, (453)S, (454)S, and (559)S. A Bfa1 mutant in which all of these residues had been changed to alanine (Bfa1(4A)) persisted on both SPBs at anaphase and was hypo-phosphorylated, despite retaining its GAP activity for Tem1. A Bfa1 phospho-mimetic mutant in which all of these residues were switched to aspartate (Bfa1(4D)) always localized asymmetrically to the SPB. These observations demonstrate that asymmetric localization of Bfa1 is tightly linked to its Cdc5-dependent phosphorylation, but not to its GAP activity. Consistent with this, in kinase-defective cdc5-2 cells Bfa1 was not phosphorylated and localized to both SPBs, whereas Bfa1(4D) was asymmetrically localized. BFA1(4A) cells progressed through anaphase normally but displayed delayed mitotic exit in unperturbed cell cycles, while BFA1(4D) cells underwent mitotic exit with the same kinetics as wild-type cells. We suggest that Cdc5 induces the asymmetric distribution of Bfa1 to the bud-directed SPB independently of Bfa1 GAP activity at anaphase and that Bfa1 asymmetry fine-tunes the timing of MEN activation in unperturbed cell cycles.</description><subject>Alanine - genetics</subject><subject>Anaphase - genetics</subject><subject>Aspartic Acid - genetics</subject><subject>Biology</subject><subject>Cell cycle</subject><subject>Cell Cycle - genetics</subject><subject>Cell Cycle Proteins - genetics</subject><subject>Cell division</subject><subject>Cyclin-dependent kinases</subject><subject>Cytoskeletal Proteins - genetics</subject><subject>GTPase-Activating Proteins - genetics</subject><subject>Kinases</subject><subject>Metaphase - genetics</subject><subject>Mitosis - genetics</subject><subject>Mutation</subject><subject>Phosphorylation</subject><subject>Protein Interaction Domains and Motifs - genetics</subject><subject>Protein Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Proteins</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Serine - genetics</subject><subject>Spindle Apparatus - genetics</subject><issn>1553-7404</issn><issn>1553-7390</issn><issn>1553-7404</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqFkkuLFDEUhQtRnHH0H4gWuHBV7c2rUtkI0vgYGHGj65BnmyZVaZP0YPvrrbZrhhkRXCUk3z05OZymeY5ghQhHb7ZpnycVV7uNm1YIAFMGD5pzxBjpOAX68M7-rHlSyhaAsEHwx80ZxpiRHth583ltDeus27nJuqm2qhzG0dUcTBuTUTH8UjWkqU2-1V6h1ofJdXU_udLWMLp4aMdQU51x9zPUp80jr2Jxz5b1ovn24f3X9afu6svHy_W7q84wxmtnBs16T_zswnMAay0Fq61XlCCuAZBWigEwS7jynoBB4DRnQActBCeaXDQvT7q7mIpckigSEURYD6LvZ-LyRNiktnKXw6jyQSYV5J-DlDdS5dl2dHLolcdeDAN1gnJlB-yNEcb31nHC9FHr7fLaXo_OmjmnrOI90fs3U_guN-laEsw4FmQWeL0I5PRj70qVYyjGxagml_ZFCkyQ6AEP_ydRPzCK-dHUq7_If8dAT5TJqZTs_K1rBPJYo5speayRXGo0j724--PboZvekN-lDMY2</recordid><startdate>20120101</startdate><enddate>20120101</enddate><creator>Kim, Junwon</creator><creator>Luo, Guangming</creator><creator>Bahk, Young Yil</creator><creator>Song, Kiwon</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</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>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20120101</creationdate><title>Cdc5-dependent asymmetric localization of bfa1 fine-tunes timely mitotic exit</title><author>Kim, Junwon ; Luo, Guangming ; Bahk, Young Yil ; Song, Kiwon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c557t-c8b56f3f225f700ddd40dbdfa4317b001baa5005d37aff30c10eb75048b9973b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Alanine - genetics</topic><topic>Anaphase - genetics</topic><topic>Aspartic Acid - genetics</topic><topic>Biology</topic><topic>Cell cycle</topic><topic>Cell Cycle - genetics</topic><topic>Cell Cycle Proteins - genetics</topic><topic>Cell division</topic><topic>Cyclin-dependent kinases</topic><topic>Cytoskeletal Proteins - genetics</topic><topic>GTPase-Activating Proteins - genetics</topic><topic>Kinases</topic><topic>Metaphase - genetics</topic><topic>Mitosis - genetics</topic><topic>Mutation</topic><topic>Phosphorylation</topic><topic>Protein Interaction Domains and Motifs - genetics</topic><topic>Protein Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Proteins</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Serine - genetics</topic><topic>Spindle Apparatus - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Junwon</creatorcontrib><creatorcontrib>Luo, Guangming</creatorcontrib><creatorcontrib>Bahk, Young Yil</creatorcontrib><creatorcontrib>Song, Kiwon</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLoS genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Junwon</au><au>Luo, Guangming</au><au>Bahk, Young Yil</au><au>Song, Kiwon</au><au>Cohen-Fix, Orna</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cdc5-dependent asymmetric localization of bfa1 fine-tunes timely mitotic exit</atitle><jtitle>PLoS genetics</jtitle><addtitle>PLoS Genet</addtitle><date>2012-01-01</date><risdate>2012</risdate><volume>8</volume><issue>1</issue><spage>e1002450</spage><epage>e1002450</epage><pages>e1002450-e1002450</pages><issn>1553-7404</issn><issn>1553-7390</issn><eissn>1553-7404</eissn><abstract>In budding yeast, the major regulator of the mitotic exit network (MEN) is Tem1, a GTPase, which is inhibited by the GTPase-activating protein (GAP), Bfa1/Bub2. Asymmetric Bfa1 localization to the bud-directed spindle pole body (SPB) during metaphase also controls mitotic exit, but the molecular mechanism and function of this localization are not well understood, particularly in unperturbed cells. We identified four novel Cdc5 target residues within the Bfa1 C-terminus: (452)S, (453)S, (454)S, and (559)S. A Bfa1 mutant in which all of these residues had been changed to alanine (Bfa1(4A)) persisted on both SPBs at anaphase and was hypo-phosphorylated, despite retaining its GAP activity for Tem1. A Bfa1 phospho-mimetic mutant in which all of these residues were switched to aspartate (Bfa1(4D)) always localized asymmetrically to the SPB. These observations demonstrate that asymmetric localization of Bfa1 is tightly linked to its Cdc5-dependent phosphorylation, but not to its GAP activity. Consistent with this, in kinase-defective cdc5-2 cells Bfa1 was not phosphorylated and localized to both SPBs, whereas Bfa1(4D) was asymmetrically localized. BFA1(4A) cells progressed through anaphase normally but displayed delayed mitotic exit in unperturbed cell cycles, while BFA1(4D) cells underwent mitotic exit with the same kinetics as wild-type cells. We suggest that Cdc5 induces the asymmetric distribution of Bfa1 to the bud-directed SPB independently of Bfa1 GAP activity at anaphase and that Bfa1 asymmetry fine-tunes the timing of MEN activation in unperturbed cell cycles.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22253605</pmid><doi>10.1371/journal.pgen.1002450</doi><oa>free_for_read</oa></addata></record> |
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subjects | Alanine - genetics Anaphase - genetics Aspartic Acid - genetics Biology Cell cycle Cell Cycle - genetics Cell Cycle Proteins - genetics Cell division Cyclin-dependent kinases Cytoskeletal Proteins - genetics GTPase-Activating Proteins - genetics Kinases Metaphase - genetics Mitosis - genetics Mutation Phosphorylation Protein Interaction Domains and Motifs - genetics Protein Kinases - genetics Protein-Serine-Threonine Kinases - genetics Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - genetics Serine - genetics Spindle Apparatus - genetics |
title | Cdc5-dependent asymmetric localization of bfa1 fine-tunes timely mitotic exit |
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