Dynamic Organization of the Actin Cytoskeleton During Meiosis and Spore Formation in Budding Yeast
During sporulation in Saccharomyces cerevisiae, the four daughter cells (spores) are formed inside the boundaries of the mother cell. Here, we investigated the dynamics of spore assembly and the actin cytoskeleton during this process, as well as the requirements for filamentous actin during the diff...
Gespeichert in:
Veröffentlicht in: | Traffic (Copenhagen, Denmark) Denmark), 2006-12, Vol.7 (12), p.1628-1642 |
---|---|
Hauptverfasser: | , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1642 |
---|---|
container_issue | 12 |
container_start_page | 1628 |
container_title | Traffic (Copenhagen, Denmark) |
container_volume | 7 |
creator | Taxis, Christof Maeder, Celine Reber, Simone Rathfelder, Nicole Miura, Kota Greger, Klaus Stelzer, Ernst H. K. Knop, Michael |
description | During sporulation in Saccharomyces cerevisiae, the four daughter cells (spores) are formed inside the boundaries of the mother cell. Here, we investigated the dynamics of spore assembly and the actin cytoskeleton during this process, as well as the requirements for filamentous actin during the different steps of spore formation. We found no evidence for a polarized actin cytoskeleton during sporulation. Instead, a highly dynamic network of non‐polarized actin cables is present underneath the plasma membrane of the mother cell. We found that a fraction of prospore membrane (PSM) precursors are transported along the actin cables. The velocity of PSM precursors is diminished if Myo2p or Tpm1/2p function is impaired. Filamentous actin is not essential for meiotic progression, for shaping of the PSMs or for post‐meiotic cytokinesis. However, actin is essential for spore wall formation. This requires the function of the Arp2/3p complex and involves large carbohydrate‐rich compartments, which may be chitosome analogous structures. |
doi_str_mv | 10.1111/j.1600-0854.2006.00496.x |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68173684</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>68173684</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5135-5793fd51ebedf78946d38ccc42b7fa3605ee0f58bbe9fcbd63a3987ef45fc29b3</originalsourceid><addsrcrecordid>eNqNkU9v1DAQxS0EoqXwFZBP3BLs-E9sicuypYBUVAnKgZPlOOPiJYkXOxFdPj0Ou4IjWCPZ0vzeWPMeQpiSmpbzcldTSUhFlOB1Q4isCeFa1vcP0PmfxsPyZlpVuqH6DD3JeUcIaQTnj9EZbSlVpc5Rd3mY7Bgcvkl3dgo_7RzihKPH81fAGzeHCW8Pc8zfYIC5dC6XFKY7_AFCzCFjO_X40z4mwFcxjUdxkbxe-n7FvoDN81P0yNshw7PTfYE-X7253b6rrm_evt9urisnKBOVaDXzvaDQQe9bpbnsmXLO8aZrvWWSCADiheo60N51vWS2rNeC58K7RnfsAr04zt2n-H2BPJsxZAfDYCeISzZS0ZZJxf8JUq0410wWUB1Bl2LOCbzZpzDadDCUmDUIszOr32b126xBmN9BmPsifX76Y-lG6P8KT84X4NUR-BEGOPz3YHP7cSOVYL8AzGGX2w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19844936</pqid></control><display><type>article</type><title>Dynamic Organization of the Actin Cytoskeleton During Meiosis and Spore Formation in Budding Yeast</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><source>IngentaConnect Free/Open Access Journals</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Wiley Online Library (Open Access Collection)</source><creator>Taxis, Christof ; Maeder, Celine ; Reber, Simone ; Rathfelder, Nicole ; Miura, Kota ; Greger, Klaus ; Stelzer, Ernst H. K. ; Knop, Michael</creator><creatorcontrib>Taxis, Christof ; Maeder, Celine ; Reber, Simone ; Rathfelder, Nicole ; Miura, Kota ; Greger, Klaus ; Stelzer, Ernst H. K. ; Knop, Michael</creatorcontrib><description>During sporulation in Saccharomyces cerevisiae, the four daughter cells (spores) are formed inside the boundaries of the mother cell. Here, we investigated the dynamics of spore assembly and the actin cytoskeleton during this process, as well as the requirements for filamentous actin during the different steps of spore formation. We found no evidence for a polarized actin cytoskeleton during sporulation. Instead, a highly dynamic network of non‐polarized actin cables is present underneath the plasma membrane of the mother cell. We found that a fraction of prospore membrane (PSM) precursors are transported along the actin cables. The velocity of PSM precursors is diminished if Myo2p or Tpm1/2p function is impaired. Filamentous actin is not essential for meiotic progression, for shaping of the PSMs or for post‐meiotic cytokinesis. However, actin is essential for spore wall formation. This requires the function of the Arp2/3p complex and involves large carbohydrate‐rich compartments, which may be chitosome analogous structures.</description><identifier>ISSN: 1398-9219</identifier><identifier>EISSN: 1600-0854</identifier><identifier>DOI: 10.1111/j.1600-0854.2006.00496.x</identifier><identifier>PMID: 17118118</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>actin ; Actin Cytoskeleton - metabolism ; Actin-Related Protein 2 - metabolism ; Actins - metabolism ; cell polarity ; Cytoskeleton - metabolism ; Meiosis ; Microscopy, Electron, Transmission ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - metabolism ; Spores, Fungal - cytology ; Spores, Fungal - metabolism ; sporulation ; vesicle movement ; yeast</subject><ispartof>Traffic (Copenhagen, Denmark), 2006-12, Vol.7 (12), p.1628-1642</ispartof><rights>2006 Munksgaard</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5135-5793fd51ebedf78946d38ccc42b7fa3605ee0f58bbe9fcbd63a3987ef45fc29b3</citedby><cites>FETCH-LOGICAL-c5135-5793fd51ebedf78946d38ccc42b7fa3605ee0f58bbe9fcbd63a3987ef45fc29b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1600-0854.2006.00496.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1600-0854.2006.00496.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17118118$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Taxis, Christof</creatorcontrib><creatorcontrib>Maeder, Celine</creatorcontrib><creatorcontrib>Reber, Simone</creatorcontrib><creatorcontrib>Rathfelder, Nicole</creatorcontrib><creatorcontrib>Miura, Kota</creatorcontrib><creatorcontrib>Greger, Klaus</creatorcontrib><creatorcontrib>Stelzer, Ernst H. K.</creatorcontrib><creatorcontrib>Knop, Michael</creatorcontrib><title>Dynamic Organization of the Actin Cytoskeleton During Meiosis and Spore Formation in Budding Yeast</title><title>Traffic (Copenhagen, Denmark)</title><addtitle>Traffic</addtitle><description>During sporulation in Saccharomyces cerevisiae, the four daughter cells (spores) are formed inside the boundaries of the mother cell. Here, we investigated the dynamics of spore assembly and the actin cytoskeleton during this process, as well as the requirements for filamentous actin during the different steps of spore formation. We found no evidence for a polarized actin cytoskeleton during sporulation. Instead, a highly dynamic network of non‐polarized actin cables is present underneath the plasma membrane of the mother cell. We found that a fraction of prospore membrane (PSM) precursors are transported along the actin cables. The velocity of PSM precursors is diminished if Myo2p or Tpm1/2p function is impaired. Filamentous actin is not essential for meiotic progression, for shaping of the PSMs or for post‐meiotic cytokinesis. However, actin is essential for spore wall formation. This requires the function of the Arp2/3p complex and involves large carbohydrate‐rich compartments, which may be chitosome analogous structures.</description><subject>actin</subject><subject>Actin Cytoskeleton - metabolism</subject><subject>Actin-Related Protein 2 - metabolism</subject><subject>Actins - metabolism</subject><subject>cell polarity</subject><subject>Cytoskeleton - metabolism</subject><subject>Meiosis</subject><subject>Microscopy, Electron, Transmission</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Spores, Fungal - cytology</subject><subject>Spores, Fungal - metabolism</subject><subject>sporulation</subject><subject>vesicle movement</subject><subject>yeast</subject><issn>1398-9219</issn><issn>1600-0854</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU9v1DAQxS0EoqXwFZBP3BLs-E9sicuypYBUVAnKgZPlOOPiJYkXOxFdPj0Ou4IjWCPZ0vzeWPMeQpiSmpbzcldTSUhFlOB1Q4isCeFa1vcP0PmfxsPyZlpVuqH6DD3JeUcIaQTnj9EZbSlVpc5Rd3mY7Bgcvkl3dgo_7RzihKPH81fAGzeHCW8Pc8zfYIC5dC6XFKY7_AFCzCFjO_X40z4mwFcxjUdxkbxe-n7FvoDN81P0yNshw7PTfYE-X7253b6rrm_evt9urisnKBOVaDXzvaDQQe9bpbnsmXLO8aZrvWWSCADiheo60N51vWS2rNeC58K7RnfsAr04zt2n-H2BPJsxZAfDYCeISzZS0ZZJxf8JUq0410wWUB1Bl2LOCbzZpzDadDCUmDUIszOr32b126xBmN9BmPsifX76Y-lG6P8KT84X4NUR-BEGOPz3YHP7cSOVYL8AzGGX2w</recordid><startdate>200612</startdate><enddate>200612</enddate><creator>Taxis, Christof</creator><creator>Maeder, Celine</creator><creator>Reber, Simone</creator><creator>Rathfelder, Nicole</creator><creator>Miura, Kota</creator><creator>Greger, Klaus</creator><creator>Stelzer, Ernst H. K.</creator><creator>Knop, Michael</creator><general>Blackwell Publishing Ltd</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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200612</creationdate><title>Dynamic Organization of the Actin Cytoskeleton During Meiosis and Spore Formation in Budding Yeast</title><author>Taxis, Christof ; Maeder, Celine ; Reber, Simone ; Rathfelder, Nicole ; Miura, Kota ; Greger, Klaus ; Stelzer, Ernst H. K. ; Knop, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5135-5793fd51ebedf78946d38ccc42b7fa3605ee0f58bbe9fcbd63a3987ef45fc29b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>actin</topic><topic>Actin Cytoskeleton - metabolism</topic><topic>Actin-Related Protein 2 - metabolism</topic><topic>Actins - metabolism</topic><topic>cell polarity</topic><topic>Cytoskeleton - metabolism</topic><topic>Meiosis</topic><topic>Microscopy, Electron, Transmission</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Spores, Fungal - cytology</topic><topic>Spores, Fungal - metabolism</topic><topic>sporulation</topic><topic>vesicle movement</topic><topic>yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Taxis, Christof</creatorcontrib><creatorcontrib>Maeder, Celine</creatorcontrib><creatorcontrib>Reber, Simone</creatorcontrib><creatorcontrib>Rathfelder, Nicole</creatorcontrib><creatorcontrib>Miura, Kota</creatorcontrib><creatorcontrib>Greger, Klaus</creatorcontrib><creatorcontrib>Stelzer, Ernst H. K.</creatorcontrib><creatorcontrib>Knop, Michael</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Traffic (Copenhagen, Denmark)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Taxis, Christof</au><au>Maeder, Celine</au><au>Reber, Simone</au><au>Rathfelder, Nicole</au><au>Miura, Kota</au><au>Greger, Klaus</au><au>Stelzer, Ernst H. K.</au><au>Knop, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dynamic Organization of the Actin Cytoskeleton During Meiosis and Spore Formation in Budding Yeast</atitle><jtitle>Traffic (Copenhagen, Denmark)</jtitle><addtitle>Traffic</addtitle><date>2006-12</date><risdate>2006</risdate><volume>7</volume><issue>12</issue><spage>1628</spage><epage>1642</epage><pages>1628-1642</pages><issn>1398-9219</issn><eissn>1600-0854</eissn><abstract>During sporulation in Saccharomyces cerevisiae, the four daughter cells (spores) are formed inside the boundaries of the mother cell. Here, we investigated the dynamics of spore assembly and the actin cytoskeleton during this process, as well as the requirements for filamentous actin during the different steps of spore formation. We found no evidence for a polarized actin cytoskeleton during sporulation. Instead, a highly dynamic network of non‐polarized actin cables is present underneath the plasma membrane of the mother cell. We found that a fraction of prospore membrane (PSM) precursors are transported along the actin cables. The velocity of PSM precursors is diminished if Myo2p or Tpm1/2p function is impaired. Filamentous actin is not essential for meiotic progression, for shaping of the PSMs or for post‐meiotic cytokinesis. However, actin is essential for spore wall formation. This requires the function of the Arp2/3p complex and involves large carbohydrate‐rich compartments, which may be chitosome analogous structures.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>17118118</pmid><doi>10.1111/j.1600-0854.2006.00496.x</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1398-9219 |
ispartof | Traffic (Copenhagen, Denmark), 2006-12, Vol.7 (12), p.1628-1642 |
issn | 1398-9219 1600-0854 |
language | eng |
recordid | cdi_proquest_miscellaneous_68173684 |
source | MEDLINE; Access via Wiley Online Library; IngentaConnect Free/Open Access Journals; EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection) |
subjects | actin Actin Cytoskeleton - metabolism Actin-Related Protein 2 - metabolism Actins - metabolism cell polarity Cytoskeleton - metabolism Meiosis Microscopy, Electron, Transmission Saccharomyces cerevisiae Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Spores, Fungal - cytology Spores, Fungal - metabolism sporulation vesicle movement yeast |
title | Dynamic Organization of the Actin Cytoskeleton During Meiosis and Spore Formation in Budding Yeast |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T21%3A21%3A13IST&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=Dynamic%20Organization%20of%20the%20Actin%20Cytoskeleton%20During%20Meiosis%20and%20Spore%20Formation%20in%20Budding%20Yeast&rft.jtitle=Traffic%20(Copenhagen,%20Denmark)&rft.au=Taxis,%20Christof&rft.date=2006-12&rft.volume=7&rft.issue=12&rft.spage=1628&rft.epage=1642&rft.pages=1628-1642&rft.issn=1398-9219&rft.eissn=1600-0854&rft_id=info:doi/10.1111/j.1600-0854.2006.00496.x&rft_dat=%3Cproquest_cross%3E68173684%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19844936&rft_id=info:pmid/17118118&rfr_iscdi=true |