Microtubule‐organizing centers of Aspergillus nidulans are anchored at septa by a disordered protein
Summary Microtubule‐organizing centers (MTOCs) are large, multi‐subunit protein complexes. Schizosaccharomyces pombe harbors MTOCs at spindle pole bodies, transient MTOCs in the division plane (eMTOCs) and nuclear‐envelope associated MTOCs in interphase cells (iMTOCs). In the filamentous fungus Aspe...
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creator | Zhang, Ying Gao, Xiaolei Manck, Raphael Schmid, Marjorie Osmani, Aysha H. Osmani, Stephen A. Takeshita, Norio Fischer, Reinhard |
description | Summary
Microtubule‐organizing centers (MTOCs) are large, multi‐subunit protein complexes. Schizosaccharomyces pombe harbors MTOCs at spindle pole bodies, transient MTOCs in the division plane (eMTOCs) and nuclear‐envelope associated MTOCs in interphase cells (iMTOCs). In the filamentous fungus Aspergillus nidulans SPBs and septum‐associated MTOCs were described. Although comparable to S. pombe eMTOCs, A. nidulans sMTOCS are permanent septum‐associated structures. The composition of sMTOCs is poorly understood and how they are targeted to septa was unknown. Here, we show that in A. nidulans several SPB outer plaque proteins also locate to sMTOCs while other SPB proteins do not, including SfiA, a protein required for SPB duplication in Saccharomyces cerevisiae and S. pombe and PcpA, the anchor for γ‐TuSCs at the SPB inner plaque. The A. nidulans disordered protein Spa18Mto2 and the centrosomin‐domain containing protein ApsBMto1 were required for recruiting the γ‐TuRC component GcpC to sMTOCs and for seeding MT formation from septa. Testing different septum‐associated proteins for a role in sMTOC function, Spa10 was identified. It forms a septal pore disc structure, recruits Spa18 and ApsB to septa and is required for sMTOC activity. This is the first evidence for a septum‐specific protein, Spa10, as anchor for a specific class of MTOCs.
Microtubules are polymerized from large protein complexes with gamma tubulin as a central component. In fungi spindle pole bodies polymerize mitotic as well as cytoplasmic microtubules. There is good evidence that other microtubule‐organizing centers exist at septa of filamentous fungi. We studied the composition of septal MTOCs in Aspergillus nidulans and identified a disordered protein required for their anchorage. |
doi_str_mv | 10.1111/mmi.13763 |
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Microtubule‐organizing centers (MTOCs) are large, multi‐subunit protein complexes. Schizosaccharomyces pombe harbors MTOCs at spindle pole bodies, transient MTOCs in the division plane (eMTOCs) and nuclear‐envelope associated MTOCs in interphase cells (iMTOCs). In the filamentous fungus Aspergillus nidulans SPBs and septum‐associated MTOCs were described. Although comparable to S. pombe eMTOCs, A. nidulans sMTOCS are permanent septum‐associated structures. The composition of sMTOCs is poorly understood and how they are targeted to septa was unknown. Here, we show that in A. nidulans several SPB outer plaque proteins also locate to sMTOCs while other SPB proteins do not, including SfiA, a protein required for SPB duplication in Saccharomyces cerevisiae and S. pombe and PcpA, the anchor for γ‐TuSCs at the SPB inner plaque. The A. nidulans disordered protein Spa18Mto2 and the centrosomin‐domain containing protein ApsBMto1 were required for recruiting the γ‐TuRC component GcpC to sMTOCs and for seeding MT formation from septa. Testing different septum‐associated proteins for a role in sMTOC function, Spa10 was identified. It forms a septal pore disc structure, recruits Spa18 and ApsB to septa and is required for sMTOC activity. This is the first evidence for a septum‐specific protein, Spa10, as anchor for a specific class of MTOCs.
Microtubules are polymerized from large protein complexes with gamma tubulin as a central component. In fungi spindle pole bodies polymerize mitotic as well as cytoplasmic microtubules. There is good evidence that other microtubule‐organizing centers exist at septa of filamentous fungi. We studied the composition of septal MTOCs in Aspergillus nidulans and identified a disordered protein required for their anchorage.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/mmi.13763</identifier><identifier>PMID: 28787538</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence - genetics ; Aspergillus nidulans ; Aspergillus nidulans - metabolism ; Eukaryotes ; Fungal Proteins - metabolism ; Fungi ; Microtubule-Associated Proteins - metabolism ; Microtubule-Organizing Center - metabolism ; Microtubules - metabolism ; Protein Binding - physiology ; Protein Transport - genetics ; Proteins ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins - metabolism ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe Proteins - metabolism ; Septum ; Spindle Apparatus - metabolism ; Spindle pole bodies ; Tubulin - metabolism ; Yeast</subject><ispartof>Molecular microbiology, 2017-10, Vol.106 (2), p.285-303</ispartof><rights>2017 John Wiley & Sons Ltd</rights><rights>2017 John Wiley & Sons Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3883-257522e8468a6b34acc73f1ad5b97f2f39cc7ffdebd602dc4c37613d6b5efcd93</citedby><cites>FETCH-LOGICAL-c3883-257522e8468a6b34acc73f1ad5b97f2f39cc7ffdebd602dc4c37613d6b5efcd93</cites><orcidid>0000-0002-6704-2569</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fmmi.13763$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fmmi.13763$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,1434,27929,27930,45579,45580,46414,46838</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28787538$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Ying</creatorcontrib><creatorcontrib>Gao, Xiaolei</creatorcontrib><creatorcontrib>Manck, Raphael</creatorcontrib><creatorcontrib>Schmid, Marjorie</creatorcontrib><creatorcontrib>Osmani, Aysha H.</creatorcontrib><creatorcontrib>Osmani, Stephen A.</creatorcontrib><creatorcontrib>Takeshita, Norio</creatorcontrib><creatorcontrib>Fischer, Reinhard</creatorcontrib><title>Microtubule‐organizing centers of Aspergillus nidulans are anchored at septa by a disordered protein</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
Microtubule‐organizing centers (MTOCs) are large, multi‐subunit protein complexes. Schizosaccharomyces pombe harbors MTOCs at spindle pole bodies, transient MTOCs in the division plane (eMTOCs) and nuclear‐envelope associated MTOCs in interphase cells (iMTOCs). In the filamentous fungus Aspergillus nidulans SPBs and septum‐associated MTOCs were described. Although comparable to S. pombe eMTOCs, A. nidulans sMTOCS are permanent septum‐associated structures. The composition of sMTOCs is poorly understood and how they are targeted to septa was unknown. Here, we show that in A. nidulans several SPB outer plaque proteins also locate to sMTOCs while other SPB proteins do not, including SfiA, a protein required for SPB duplication in Saccharomyces cerevisiae and S. pombe and PcpA, the anchor for γ‐TuSCs at the SPB inner plaque. The A. nidulans disordered protein Spa18Mto2 and the centrosomin‐domain containing protein ApsBMto1 were required for recruiting the γ‐TuRC component GcpC to sMTOCs and for seeding MT formation from septa. Testing different septum‐associated proteins for a role in sMTOC function, Spa10 was identified. It forms a septal pore disc structure, recruits Spa18 and ApsB to septa and is required for sMTOC activity. This is the first evidence for a septum‐specific protein, Spa10, as anchor for a specific class of MTOCs.
Microtubules are polymerized from large protein complexes with gamma tubulin as a central component. In fungi spindle pole bodies polymerize mitotic as well as cytoplasmic microtubules. There is good evidence that other microtubule‐organizing centers exist at septa of filamentous fungi. We studied the composition of septal MTOCs in Aspergillus nidulans and identified a disordered protein required for their anchorage.</description><subject>Amino Acid Sequence - genetics</subject><subject>Aspergillus nidulans</subject><subject>Aspergillus nidulans - metabolism</subject><subject>Eukaryotes</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungi</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Microtubule-Organizing Center - metabolism</subject><subject>Microtubules - metabolism</subject><subject>Protein Binding - physiology</subject><subject>Protein Transport - genetics</subject><subject>Proteins</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Schizosaccharomyces - metabolism</subject><subject>Schizosaccharomyces pombe Proteins - metabolism</subject><subject>Septum</subject><subject>Spindle Apparatus - metabolism</subject><subject>Spindle pole bodies</subject><subject>Tubulin - metabolism</subject><subject>Yeast</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMtKJDEUQIM4aPtY-AMScKOL0iS3UpVaiqgj2MxmBtwVqeSmjdSjTaqQduUn-I1-ycRpx4VgNoHkcHJzCDng7JSnddZ1_pRDWcAGmXEoZCYqqTbJjFWSZaDE3TbZifGBMQ6sgC2yLVSpSglqRtzcmzCMUzO1-PbyOoSF7v2z7xfUYD9iiHRw9DwuMSx8206R9t5Ore4j1QGp7s39ENBSPdKIy1HTZkU1tT4OweL7xTLJ0fd75IfTbcT9j32X_Lm6_H3xM7v9dX1zcX6bGVAKMiFLKQSqvFC6aCDXxpTguLayqUonHFTpwDmLjS2YsCY36dccbNFIdMZWsEuO19707uOEcaw7Hw22aWIcpljzSpQFA5bLhB59QR-GKfRpukTlpWQCKkjUyZpKlWIM6Opl8J0Oq5qz-j1-neLX_-In9vDDODUd2k_yf-0EnK2BJ9_i6ntTPZ_frJV_AVBlkLY</recordid><startdate>201710</startdate><enddate>201710</enddate><creator>Zhang, Ying</creator><creator>Gao, Xiaolei</creator><creator>Manck, Raphael</creator><creator>Schmid, Marjorie</creator><creator>Osmani, Aysha H.</creator><creator>Osmani, Stephen A.</creator><creator>Takeshita, Norio</creator><creator>Fischer, Reinhard</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-6704-2569</orcidid></search><sort><creationdate>201710</creationdate><title>Microtubule‐organizing centers of Aspergillus nidulans are anchored at septa by a disordered protein</title><author>Zhang, Ying ; Gao, Xiaolei ; Manck, Raphael ; Schmid, Marjorie ; Osmani, Aysha H. ; Osmani, Stephen A. ; Takeshita, Norio ; Fischer, Reinhard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3883-257522e8468a6b34acc73f1ad5b97f2f39cc7ffdebd602dc4c37613d6b5efcd93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino Acid Sequence - genetics</topic><topic>Aspergillus nidulans</topic><topic>Aspergillus nidulans - metabolism</topic><topic>Eukaryotes</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungi</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>Microtubule-Organizing Center - metabolism</topic><topic>Microtubules - metabolism</topic><topic>Protein Binding - physiology</topic><topic>Protein Transport - genetics</topic><topic>Proteins</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Schizosaccharomyces - metabolism</topic><topic>Schizosaccharomyces pombe Proteins - metabolism</topic><topic>Septum</topic><topic>Spindle Apparatus - metabolism</topic><topic>Spindle pole bodies</topic><topic>Tubulin - metabolism</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Ying</creatorcontrib><creatorcontrib>Gao, Xiaolei</creatorcontrib><creatorcontrib>Manck, Raphael</creatorcontrib><creatorcontrib>Schmid, Marjorie</creatorcontrib><creatorcontrib>Osmani, Aysha H.</creatorcontrib><creatorcontrib>Osmani, Stephen A.</creatorcontrib><creatorcontrib>Takeshita, Norio</creatorcontrib><creatorcontrib>Fischer, Reinhard</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</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>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Ying</au><au>Gao, Xiaolei</au><au>Manck, Raphael</au><au>Schmid, Marjorie</au><au>Osmani, Aysha H.</au><au>Osmani, Stephen A.</au><au>Takeshita, Norio</au><au>Fischer, Reinhard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Microtubule‐organizing centers of Aspergillus nidulans are anchored at septa by a disordered protein</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2017-10</date><risdate>2017</risdate><volume>106</volume><issue>2</issue><spage>285</spage><epage>303</epage><pages>285-303</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
Microtubule‐organizing centers (MTOCs) are large, multi‐subunit protein complexes. Schizosaccharomyces pombe harbors MTOCs at spindle pole bodies, transient MTOCs in the division plane (eMTOCs) and nuclear‐envelope associated MTOCs in interphase cells (iMTOCs). In the filamentous fungus Aspergillus nidulans SPBs and septum‐associated MTOCs were described. Although comparable to S. pombe eMTOCs, A. nidulans sMTOCS are permanent septum‐associated structures. The composition of sMTOCs is poorly understood and how they are targeted to septa was unknown. Here, we show that in A. nidulans several SPB outer plaque proteins also locate to sMTOCs while other SPB proteins do not, including SfiA, a protein required for SPB duplication in Saccharomyces cerevisiae and S. pombe and PcpA, the anchor for γ‐TuSCs at the SPB inner plaque. The A. nidulans disordered protein Spa18Mto2 and the centrosomin‐domain containing protein ApsBMto1 were required for recruiting the γ‐TuRC component GcpC to sMTOCs and for seeding MT formation from septa. Testing different septum‐associated proteins for a role in sMTOC function, Spa10 was identified. It forms a septal pore disc structure, recruits Spa18 and ApsB to septa and is required for sMTOC activity. This is the first evidence for a septum‐specific protein, Spa10, as anchor for a specific class of MTOCs.
Microtubules are polymerized from large protein complexes with gamma tubulin as a central component. In fungi spindle pole bodies polymerize mitotic as well as cytoplasmic microtubules. There is good evidence that other microtubule‐organizing centers exist at septa of filamentous fungi. We studied the composition of septal MTOCs in Aspergillus nidulans and identified a disordered protein required for their anchorage.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>28787538</pmid><doi>10.1111/mmi.13763</doi><tpages>19</tpages><orcidid>https://orcid.org/0000-0002-6704-2569</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence - genetics Aspergillus nidulans Aspergillus nidulans - metabolism Eukaryotes Fungal Proteins - metabolism Fungi Microtubule-Associated Proteins - metabolism Microtubule-Organizing Center - metabolism Microtubules - metabolism Protein Binding - physiology Protein Transport - genetics Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins - metabolism Schizosaccharomyces - metabolism Schizosaccharomyces pombe Proteins - metabolism Septum Spindle Apparatus - metabolism Spindle pole bodies Tubulin - metabolism Yeast |
title | Microtubule‐organizing centers of Aspergillus nidulans are anchored at septa by a disordered protein |
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