A novel patch assembly domain in Num1 mediates dynein anchoring at the cortex during spindle positioning
During mitosis in budding yeast, cortically anchored dynein generates pulling forces on astral microtubules to position the mitotic spindle across the mother-bud neck. The attachment molecule Num1 is required for dynein anchoring at the cell membrane, but how Num1 assembles into stationary cortical...
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| Veröffentlicht in: | The Journal of cell biology 2012-03, Vol.196 (6), p.743-756 |
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| container_title | The Journal of cell biology |
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| creator | Tang, Xianying Germain, Bryan St Lee, Wei-Lih |
| description | During mitosis in budding yeast, cortically anchored dynein generates pulling forces on astral microtubules to position the mitotic spindle across the mother-bud neck. The attachment molecule Num1 is required for dynein anchoring at the cell membrane, but how Num1 assembles into stationary cortical patches and interacts with dynein is unknown. We show that an N-terminal Bin/Amphiphysin/Rvs (BAR)-like domain in Num1 mediates the assembly of morphologically distinct patches and its interaction with dynein for spindle translocation into the bud. We name this domain patch assembly domain (PA; residues 1-303), as it was both necessary and sufficient for the formation of functional dynein-anchoring patches when it was attached to a pleckstrin homology domain or a CAAX motif. Distinct point mutations targeting the predicted BAR-like PA domain differentially disrupted patch assembly, dynein anchoring, and mitochondrial attachment functions of Num1. We also show that the PA domain is an elongated dimer and discuss the mechanism by which it drives patch assembly. |
| doi_str_mv | 10.1083/jcb.201112017 |
| format | Article |
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The attachment molecule Num1 is required for dynein anchoring at the cell membrane, but how Num1 assembles into stationary cortical patches and interacts with dynein is unknown. We show that an N-terminal Bin/Amphiphysin/Rvs (BAR)-like domain in Num1 mediates the assembly of morphologically distinct patches and its interaction with dynein for spindle translocation into the bud. We name this domain patch assembly domain (PA; residues 1-303), as it was both necessary and sufficient for the formation of functional dynein-anchoring patches when it was attached to a pleckstrin homology domain or a CAAX motif. Distinct point mutations targeting the predicted BAR-like PA domain differentially disrupted patch assembly, dynein anchoring, and mitochondrial attachment functions of Num1. 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The attachment molecule Num1 is required for dynein anchoring at the cell membrane, but how Num1 assembles into stationary cortical patches and interacts with dynein is unknown. We show that an N-terminal Bin/Amphiphysin/Rvs (BAR)-like domain in Num1 mediates the assembly of morphologically distinct patches and its interaction with dynein for spindle translocation into the bud. We name this domain patch assembly domain (PA; residues 1-303), as it was both necessary and sufficient for the formation of functional dynein-anchoring patches when it was attached to a pleckstrin homology domain or a CAAX motif. Distinct point mutations targeting the predicted BAR-like PA domain differentially disrupted patch assembly, dynein anchoring, and mitochondrial attachment functions of Num1. We also show that the PA domain is an elongated dimer and discuss the mechanism by which it drives patch assembly.</description><subject>Brain</subject><subject>Cell division</subject><subject>Cytoskeletal Proteins - genetics</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>Dyneins - genetics</subject><subject>Dyneins - metabolism</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Microtubules - metabolism</subject><subject>Morphology</subject><subject>Mutation</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae - ultrastructure</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Spindle Apparatus - physiology</subject><subject>Yeast</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc1rFTEUxYMo9vl06VaCG1dT8zWTyUYoxapQdKPrkGRuOnnMJGMyU_r-e2NbHyqEGzj3x-EkB6HXlJxT0vP3B2fPGaGU1iGfoB1tBWl6KshTtCOE0Ua1rD1DL0o5EEKEFPw5OmNMcCpbukPjBY7pFia8mNWN2JQCs52OeEizCRHX83WbKZ5hCGaFgodjhCqa6MaUQ7zBZsXrCNilvMIdHrZ7sSwhDhPgJZWwhhSr9hI982Yq8Orx3qMfVx-_X35urr99-nJ5cd04IdXadMKozg69J85K6gfvhONEGuBCDtZYAsxQy4yyysuemap6BT3x4CVQZ_kefXjwXTZbUzuIazaTXnKYTT7qZIL-dxPDqG_Sreac9J0S1eDdo0FOPzcoq55DcTBNJkLailZMtUSK-vd79PY_8pC2HOvrtBKsq3ZdW6HmAXI5lZLBn6JQon83qGuD-tRg5d_8nf9E_6mM_wL7npn5</recordid><startdate>20120319</startdate><enddate>20120319</enddate><creator>Tang, Xianying</creator><creator>Germain, Bryan St</creator><creator>Lee, Wei-Lih</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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><scope>5PM</scope></search><sort><creationdate>20120319</creationdate><title>A novel patch assembly domain in Num1 mediates dynein anchoring at the cortex during spindle positioning</title><author>Tang, Xianying ; Germain, Bryan St ; Lee, Wei-Lih</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c479t-64a96bd8f0cb71fdfc4c307ae347dbab0e2a1b2a9b9f782a47df9e80fef7e1cb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Brain</topic><topic>Cell division</topic><topic>Cytoskeletal Proteins - genetics</topic><topic>Cytoskeletal Proteins - metabolism</topic><topic>Dyneins - genetics</topic><topic>Dyneins - metabolism</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>Microtubules - metabolism</topic><topic>Morphology</topic><topic>Mutation</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae - ultrastructure</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Spindle Apparatus - physiology</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tang, Xianying</creatorcontrib><creatorcontrib>Germain, Bryan St</creatorcontrib><creatorcontrib>Lee, Wei-Lih</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tang, Xianying</au><au>Germain, Bryan St</au><au>Lee, Wei-Lih</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel patch assembly domain in Num1 mediates dynein anchoring at the cortex during spindle positioning</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2012-03-19</date><risdate>2012</risdate><volume>196</volume><issue>6</issue><spage>743</spage><epage>756</epage><pages>743-756</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>During mitosis in budding yeast, cortically anchored dynein generates pulling forces on astral microtubules to position the mitotic spindle across the mother-bud neck. The attachment molecule Num1 is required for dynein anchoring at the cell membrane, but how Num1 assembles into stationary cortical patches and interacts with dynein is unknown. We show that an N-terminal Bin/Amphiphysin/Rvs (BAR)-like domain in Num1 mediates the assembly of morphologically distinct patches and its interaction with dynein for spindle translocation into the bud. We name this domain patch assembly domain (PA; residues 1-303), as it was both necessary and sufficient for the formation of functional dynein-anchoring patches when it was attached to a pleckstrin homology domain or a CAAX motif. Distinct point mutations targeting the predicted BAR-like PA domain differentially disrupted patch assembly, dynein anchoring, and mitochondrial attachment functions of Num1. 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| subjects | Brain Cell division Cytoskeletal Proteins - genetics Cytoskeletal Proteins - metabolism Dyneins - genetics Dyneins - metabolism Fungal Proteins - genetics Fungal Proteins - metabolism Microtubule-Associated Proteins - metabolism Microtubules - metabolism Morphology Mutation Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Spindle Apparatus - physiology Yeast |
| title | A novel patch assembly domain in Num1 mediates dynein anchoring at the cortex during spindle positioning |
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