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Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleation
Formins associate with other nucleators and nucleation-promoting factors (NPFs) to stimulate collaborative actin assembly, but the mechanisms regulating these interactions have been unclear. Yeast Bud6 has an established role as an NPF for the formin Bni1, but whether it also directly regulates the...
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| Published in: | The Journal of cell biology 2013-05, Vol.201 (4), p.595-611 |
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| Main Authors: | , , , , |
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| cites | cdi_FETCH-LOGICAL-c415t-ab5b52cf0057e65f3992d95c16d4c228e7fa82fbfcad91bfe28f4d9219c061e3 |
| container_end_page | 611 |
| container_issue | 4 |
| container_start_page | 595 |
| container_title | The Journal of cell biology |
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| creator | Graziano, Brian R Jonasson, Erin M Pullen, Jessica G Gould, Christopher J Goode, Bruce L |
| description | Formins associate with other nucleators and nucleation-promoting factors (NPFs) to stimulate collaborative actin assembly, but the mechanisms regulating these interactions have been unclear. Yeast Bud6 has an established role as an NPF for the formin Bni1, but whether it also directly regulates the formin Bnr1 has remained enigmatic. In this paper, we analyzed NPF-impaired alleles of bud6 in a bni1Δ background and found that Bud6 stimulated Bnr1 activity in vivo. Furthermore, Bud6 bound directly to Bnr1, but its NPF effects were masked by a short regulatory sequence, suggesting that additional factors may be required for activation. We isolated a novel in vivo binding partner of Bud6, Yor304c-a/Bil1, which colocalized with Bud6 and functioned in the Bnr1 pathway for actin assembly. Purified Bil1 bound to the regulatory sequence in Bud6 and triggered NPF effects on Bnr1. These observations define a new mode of formin regulation, which has important implications for understanding NPF-nucleator pairs in diverse systems. |
| doi_str_mv | 10.1083/jcb.201212059 |
| format | article |
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Yeast Bud6 has an established role as an NPF for the formin Bni1, but whether it also directly regulates the formin Bnr1 has remained enigmatic. In this paper, we analyzed NPF-impaired alleles of bud6 in a bni1Δ background and found that Bud6 stimulated Bnr1 activity in vivo. Furthermore, Bud6 bound directly to Bnr1, but its NPF effects were masked by a short regulatory sequence, suggesting that additional factors may be required for activation. We isolated a novel in vivo binding partner of Bud6, Yor304c-a/Bil1, which colocalized with Bud6 and functioned in the Bnr1 pathway for actin assembly. Purified Bil1 bound to the regulatory sequence in Bud6 and triggered NPF effects on Bnr1. 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Yeast Bud6 has an established role as an NPF for the formin Bni1, but whether it also directly regulates the formin Bnr1 has remained enigmatic. In this paper, we analyzed NPF-impaired alleles of bud6 in a bni1Δ background and found that Bud6 stimulated Bnr1 activity in vivo. Furthermore, Bud6 bound directly to Bnr1, but its NPF effects were masked by a short regulatory sequence, suggesting that additional factors may be required for activation. We isolated a novel in vivo binding partner of Bud6, Yor304c-a/Bil1, which colocalized with Bud6 and functioned in the Bnr1 pathway for actin assembly. Purified Bil1 bound to the regulatory sequence in Bud6 and triggered NPF effects on Bnr1. These observations define a new mode of formin regulation, which has important implications for understanding NPF-nucleator pairs in diverse systems.</description><subject>Actins - chemistry</subject><subject>Animals</subject><subject>Binding sites</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - physiology</subject><subject>Cells</subject><subject>Cytoskeletal Proteins - genetics</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>Gene Expression Regulation, Fungal</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>Kinetics</subject><subject>Ligands</subject><subject>Mass Spectrometry</subject><subject>Microfilament Proteins - genetics</subject><subject>Microfilament Proteins - metabolism</subject><subject>Microfilament Proteins - physiology</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Mutation</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Rabbits</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - physiology</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - physiology</subject><subject>Yeast</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNpdkb1vFDEUxC0EIkegpEWWaGg2vGevfd4GCUUJQToBRURref0RfNqzD3v3JP57fCScAtUr5jejNxpCXiNcICj-fmvHCwbIkIEYnpAVih46hT08JSsAht0gmDgjL2rdAkC_7vlzcsa4XCNHtiLfN_HOJNfF5BbrHTV2jgczx5xoDtTQkMsupu7Lt2u6N7HQyRtX6ZypzdNkxlwae_B_bImmxTb9aH5JngUzVf_q4Z6T2-ur28ubbvP10-fLj5vO9ijmzoxiFMwGALH2UgQ-DMwNwqJ0vWVM-XUwioUxWOMGHINnKvRuYDhYkOj5OflwH7tfxp131qe5mEnvS9yZ8ktnE_W_Soo_9F0-aC4F55K3gHcPASX_XHyd9S5W61u15PNSNXKBEpRSsqFv_0O3eSmptTtSDJTgEhvV3VO25FqLD6dnEPRxMN0G06fBGv_mcYMT_Xch_hscapIL</recordid><startdate>20130513</startdate><enddate>20130513</enddate><creator>Graziano, Brian R</creator><creator>Jonasson, Erin M</creator><creator>Pullen, Jessica G</creator><creator>Gould, Christopher J</creator><creator>Goode, Bruce L</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>20130513</creationdate><title>Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleation</title><author>Graziano, Brian R ; Jonasson, Erin M ; Pullen, Jessica G ; Gould, Christopher J ; Goode, Bruce L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-ab5b52cf0057e65f3992d95c16d4c228e7fa82fbfcad91bfe28f4d9219c061e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Actins - chemistry</topic><topic>Animals</topic><topic>Binding sites</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - physiology</topic><topic>Cells</topic><topic>Cytoskeletal Proteins - genetics</topic><topic>Cytoskeletal Proteins - metabolism</topic><topic>Gene Expression Regulation, Fungal</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>Kinetics</topic><topic>Ligands</topic><topic>Mass Spectrometry</topic><topic>Microfilament Proteins - genetics</topic><topic>Microfilament Proteins - metabolism</topic><topic>Microfilament Proteins - physiology</topic><topic>Muscle, Skeletal - metabolism</topic><topic>Mutation</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Rabbits</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - physiology</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - physiology</topic><topic>Yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Graziano, Brian R</creatorcontrib><creatorcontrib>Jonasson, Erin M</creatorcontrib><creatorcontrib>Pullen, Jessica G</creatorcontrib><creatorcontrib>Gould, Christopher J</creatorcontrib><creatorcontrib>Goode, Bruce L</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>Graziano, Brian R</au><au>Jonasson, Erin M</au><au>Pullen, Jessica G</au><au>Gould, Christopher J</au><au>Goode, Bruce L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleation</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2013-05-13</date><risdate>2013</risdate><volume>201</volume><issue>4</issue><spage>595</spage><epage>611</epage><pages>595-611</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Formins associate with other nucleators and nucleation-promoting factors (NPFs) to stimulate collaborative actin assembly, but the mechanisms regulating these interactions have been unclear. Yeast Bud6 has an established role as an NPF for the formin Bni1, but whether it also directly regulates the formin Bnr1 has remained enigmatic. In this paper, we analyzed NPF-impaired alleles of bud6 in a bni1Δ background and found that Bud6 stimulated Bnr1 activity in vivo. Furthermore, Bud6 bound directly to Bnr1, but its NPF effects were masked by a short regulatory sequence, suggesting that additional factors may be required for activation. We isolated a novel in vivo binding partner of Bud6, Yor304c-a/Bil1, which colocalized with Bud6 and functioned in the Bnr1 pathway for actin assembly. Purified Bil1 bound to the regulatory sequence in Bud6 and triggered NPF effects on Bnr1. These observations define a new mode of formin regulation, which has important implications for understanding NPF-nucleator pairs in diverse systems.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>23671312</pmid><doi>10.1083/jcb.201212059</doi><tpages>17</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Actins - chemistry Animals Binding sites Carrier Proteins - genetics Carrier Proteins - physiology Cells Cytoskeletal Proteins - genetics Cytoskeletal Proteins - metabolism Gene Expression Regulation, Fungal Green Fluorescent Proteins - metabolism Kinetics Ligands Mass Spectrometry Microfilament Proteins - genetics Microfilament Proteins - metabolism Microfilament Proteins - physiology Muscle, Skeletal - metabolism Mutation Protein Interaction Domains and Motifs Rabbits Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - physiology Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - physiology Yeast |
| title | Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleation |
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