Functional interactions between the p35 subunit of the Arp2/3 complex and calmodulin in yeast
The end9-1 (arc35-1) mutant was identified as an endocytosis mutant and is a mutant allele of ARC35 that encodes a subunit of the Arp2/3 complex. As for other mutants in the Arp2/3 complex, arc35-1 is defective for endocytosis and organization of the actin cytoskeleton. Both defects can be suppresse...
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| Veröffentlicht in: | Molecular biology of the cell 2000-04, Vol.11 (4), p.1113-1127 |
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| container_title | Molecular biology of the cell |
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| creator | Schaerer-Brodbeck, C Riezman, H |
| description | The end9-1 (arc35-1) mutant was identified as an endocytosis mutant and is a mutant allele of ARC35 that encodes a subunit of the Arp2/3 complex. As for other mutants in the Arp2/3 complex, arc35-1 is defective for endocytosis and organization of the actin cytoskeleton. Both defects can be suppressed by overexpression of calmodulin. Analysis of a collection of temperature-sensitive cmd1 mutants for their ability to suppress either the endocytic defect and/or the actin defect indicates that the two defects are tightly coupled. We demonstrate that Arc35p and Cmd1p interact and that Arc35p is required for cortical localization of calmodulin. This is the first report linking Arp2/3 complex function with calmodulin through which it exercises at least one of its endocytic functions. |
| doi_str_mv | 10.1091/mbc.11.4.1113 |
| format | Article |
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As for other mutants in the Arp2/3 complex, arc35-1 is defective for endocytosis and organization of the actin cytoskeleton. Both defects can be suppressed by overexpression of calmodulin. Analysis of a collection of temperature-sensitive cmd1 mutants for their ability to suppress either the endocytic defect and/or the actin defect indicates that the two defects are tightly coupled. We demonstrate that Arc35p and Cmd1p interact and that Arc35p is required for cortical localization of calmodulin. 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As for other mutants in the Arp2/3 complex, arc35-1 is defective for endocytosis and organization of the actin cytoskeleton. Both defects can be suppressed by overexpression of calmodulin. Analysis of a collection of temperature-sensitive cmd1 mutants for their ability to suppress either the endocytic defect and/or the actin defect indicates that the two defects are tightly coupled. We demonstrate that Arc35p and Cmd1p interact and that Arc35p is required for cortical localization of calmodulin. This is the first report linking Arp2/3 complex function with calmodulin through which it exercises at least one of its endocytic functions.</description><subject>Actin-Related Protein 2</subject><subject>Actin-Related Protein 3</subject><subject>Actins - genetics</subject><subject>Actins - metabolism</subject><subject>Alleles</subject><subject>Bridged Bicyclo Compounds, Heterocyclic - pharmacology</subject><subject>Calmodulin - genetics</subject><subject>Calmodulin - metabolism</subject><subject>Cytoskeletal Proteins</subject><subject>Cytoskeleton - metabolism</subject><subject>Endocytosis - physiology</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Microscopy, Fluorescence</subject><subject>Mutation</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Thiazoles - pharmacology</subject><subject>Thiazolidines</subject><subject>Two-Hybrid System Techniques</subject><subject>Yeasts - genetics</subject><subject>Yeasts - growth & development</subject><subject>Yeasts - metabolism</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUUlLxDAUDqK4jB69Sk7eOuY1adKCFxE3ELzoUUKavmqlTWqTuvx7M46IXt76vfUj5BDYElgFJ0NtlwBLkQTwDbILFa8yUZRyM9msqDIocrFD9kJ4YQyEkGqb7ABToqqg3CWPl7OzsfPO9LRzESfz7QVaY3xHdDQ-Ix15QcNcz66L1LffobNpzE84tX4Ye_ygxjXUmn7wzdx3LnWin2hC3CdbrekDHvzoBXm4vLg_v85u765uzs9uMytUGbNKlUpx09TI8rS_glKwJpdCoTBgeNsqoaSRlQLZFrK21qYDcom8TMI0OV-Q03Xfca4HbCy6OJlej1M3mOlTe9Pp_xnXPesn_6ZBlLxI5cc_5ZN_nTFEPXTBYt8bh34OWgHjjEmVgNkaaCcfwoTt7whgekWHTnRoAC30io6EP_q71x_0-v_8C3fphww</recordid><startdate>20000401</startdate><enddate>20000401</enddate><creator>Schaerer-Brodbeck, C</creator><creator>Riezman, H</creator><general>The American Society for Cell Biology</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000401</creationdate><title>Functional interactions between the p35 subunit of the Arp2/3 complex and calmodulin in yeast</title><author>Schaerer-Brodbeck, C ; Riezman, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c478t-978773adbe0219371840d2647e4a1a3ff7476a69716f56bccc10726e3826ead23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Actin-Related Protein 2</topic><topic>Actin-Related Protein 3</topic><topic>Actins - genetics</topic><topic>Actins - metabolism</topic><topic>Alleles</topic><topic>Bridged Bicyclo Compounds, Heterocyclic - pharmacology</topic><topic>Calmodulin - genetics</topic><topic>Calmodulin - metabolism</topic><topic>Cytoskeletal Proteins</topic><topic>Cytoskeleton - metabolism</topic><topic>Endocytosis - physiology</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Microscopy, Fluorescence</topic><topic>Mutation</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>Thiazoles - pharmacology</topic><topic>Thiazolidines</topic><topic>Two-Hybrid System Techniques</topic><topic>Yeasts - genetics</topic><topic>Yeasts - growth & development</topic><topic>Yeasts - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schaerer-Brodbeck, C</creatorcontrib><creatorcontrib>Riezman, H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schaerer-Brodbeck, C</au><au>Riezman, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional interactions between the p35 subunit of the Arp2/3 complex and calmodulin in yeast</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2000-04-01</date><risdate>2000</risdate><volume>11</volume><issue>4</issue><spage>1113</spage><epage>1127</epage><pages>1113-1127</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>The end9-1 (arc35-1) mutant was identified as an endocytosis mutant and is a mutant allele of ARC35 that encodes a subunit of the Arp2/3 complex. As for other mutants in the Arp2/3 complex, arc35-1 is defective for endocytosis and organization of the actin cytoskeleton. Both defects can be suppressed by overexpression of calmodulin. Analysis of a collection of temperature-sensitive cmd1 mutants for their ability to suppress either the endocytic defect and/or the actin defect indicates that the two defects are tightly coupled. We demonstrate that Arc35p and Cmd1p interact and that Arc35p is required for cortical localization of calmodulin. This is the first report linking Arp2/3 complex function with calmodulin through which it exercises at least one of its endocytic functions.</abstract><cop>United States</cop><pub>The American Society for Cell Biology</pub><pmid>10749918</pmid><doi>10.1091/mbc.11.4.1113</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular biology of the cell, 2000-04, Vol.11 (4), p.1113-1127 |
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| subjects | Actin-Related Protein 2 Actin-Related Protein 3 Actins - genetics Actins - metabolism Alleles Bridged Bicyclo Compounds, Heterocyclic - pharmacology Calmodulin - genetics Calmodulin - metabolism Cytoskeletal Proteins Cytoskeleton - metabolism Endocytosis - physiology Fungal Proteins - genetics Fungal Proteins - metabolism Microscopy, Fluorescence Mutation Precipitin Tests Protein Binding Thiazoles - pharmacology Thiazolidines Two-Hybrid System Techniques Yeasts - genetics Yeasts - growth & development Yeasts - metabolism |
| title | Functional interactions between the p35 subunit of the Arp2/3 complex and calmodulin in yeast |
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