Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion
The molecular mechanisms by which the Abelson (Abl) or Abl-related gene (Arg) kinases interface with the actin polymerization machinery to promote cell edge protrusions during cell-matrix adhesion are unclear. In this study, we show that interactions between Arg and the Arp2/3 complex regulator cort...
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| Veröffentlicht in: | The Journal of cell biology 2009-05, Vol.185 (3), p.503-519 |
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| container_title | The Journal of cell biology |
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| creator | Lapetina, Stefanie Mader, Christopher C Machida, Kazuya Mayer, Bruce J Koleske, Anthony J |
| description | The molecular mechanisms by which the Abelson (Abl) or Abl-related gene (Arg) kinases interface with the actin polymerization machinery to promote cell edge protrusions during cell-matrix adhesion are unclear. In this study, we show that interactions between Arg and the Arp2/3 complex regulator cortactin are essential to mediate actin-based cell edge protrusion during fibroblast adhesion to fibronectin. Arg-deficient and cortactin knockdown fibroblasts exhibit similar defects in adhesion-dependent cell edge protrusion, which can be restored via reexpression of Arg and cortactin. Arg interacts with cortactin via both binding and catalytic events. The cortactin Src homology (SH) 3 domain binds to a Pro-rich motif in the Arg C terminus. Arg mediates adhesion-dependent phosphorylation of cortactin, creating an additional binding site for the Arg SH2 domain. Mutation of residues that mediate Arg-cortactin interactions abrogate the abilities of both proteins to support protrusions, and the Nck adapter, which binds phosphocortactin, is also required. These results demonstrate that interactions between Arg, cortactin, and Nck1 are critical to promote adhesion-dependent cell edge protrusions. |
| doi_str_mv | 10.1083/jcb.200809085 |
| format | Article |
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In this study, we show that interactions between Arg and the Arp2/3 complex regulator cortactin are essential to mediate actin-based cell edge protrusion during fibroblast adhesion to fibronectin. Arg-deficient and cortactin knockdown fibroblasts exhibit similar defects in adhesion-dependent cell edge protrusion, which can be restored via reexpression of Arg and cortactin. Arg interacts with cortactin via both binding and catalytic events. The cortactin Src homology (SH) 3 domain binds to a Pro-rich motif in the Arg C terminus. Arg mediates adhesion-dependent phosphorylation of cortactin, creating an additional binding site for the Arg SH2 domain. Mutation of residues that mediate Arg-cortactin interactions abrogate the abilities of both proteins to support protrusions, and the Nck adapter, which binds phosphocortactin, is also required. These results demonstrate that interactions between Arg, cortactin, and Nck1 are critical to promote adhesion-dependent cell edge protrusions.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200809085</identifier><identifier>PMID: 19414610</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: The Rockefeller University Press</publisher><subject>Actins ; Actins - metabolism ; Adaptor Proteins, Signal Transducing ; Animals ; Binding Sites ; Cell adhesion ; Cell adhesion & migration ; Cell Adhesion - physiology ; Cell Membrane - physiology ; Cell Movement - physiology ; Cells ; Cortactin - metabolism ; Endothelial cells ; Fibroblasts ; Fibroblasts - cytology ; Fibroblasts - physiology ; Fibrosis ; Gene expression regulation ; Genes, abl ; Genes, Reporter ; Humans ; Kinases ; Kinetics ; Luminescent Proteins - genetics ; Mutation ; Oncogene Proteins - physiology ; Phosphorylation ; Polymerization ; Protein-Tyrosine Kinases - metabolism ; Proteins ; Studies</subject><ispartof>The Journal of cell biology, 2009-05, Vol.185 (3), p.503-519</ispartof><rights>Copyright Rockefeller University Press May 4, 2009</rights><rights>2009 Lapetina et al. 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-45e878c9ac95a15d816ca0f86fceb6bd91607846f1ed2ebd3c058b977b88d6d23</citedby><cites>FETCH-LOGICAL-c458t-45e878c9ac95a15d816ca0f86fceb6bd91607846f1ed2ebd3c058b977b88d6d23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19414610$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lapetina, Stefanie</creatorcontrib><creatorcontrib>Mader, Christopher C</creatorcontrib><creatorcontrib>Machida, Kazuya</creatorcontrib><creatorcontrib>Mayer, Bruce J</creatorcontrib><creatorcontrib>Koleske, Anthony J</creatorcontrib><title>Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The molecular mechanisms by which the Abelson (Abl) or Abl-related gene (Arg) kinases interface with the actin polymerization machinery to promote cell edge protrusions during cell-matrix adhesion are unclear. In this study, we show that interactions between Arg and the Arp2/3 complex regulator cortactin are essential to mediate actin-based cell edge protrusion during fibroblast adhesion to fibronectin. Arg-deficient and cortactin knockdown fibroblasts exhibit similar defects in adhesion-dependent cell edge protrusion, which can be restored via reexpression of Arg and cortactin. Arg interacts with cortactin via both binding and catalytic events. The cortactin Src homology (SH) 3 domain binds to a Pro-rich motif in the Arg C terminus. Arg mediates adhesion-dependent phosphorylation of cortactin, creating an additional binding site for the Arg SH2 domain. Mutation of residues that mediate Arg-cortactin interactions abrogate the abilities of both proteins to support protrusions, and the Nck adapter, which binds phosphocortactin, is also required. These results demonstrate that interactions between Arg, cortactin, and Nck1 are critical to promote adhesion-dependent cell edge protrusions.</description><subject>Actins</subject><subject>Actins - metabolism</subject><subject>Adaptor Proteins, Signal Transducing</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Cell adhesion</subject><subject>Cell adhesion & migration</subject><subject>Cell Adhesion - physiology</subject><subject>Cell Membrane - physiology</subject><subject>Cell Movement - physiology</subject><subject>Cells</subject><subject>Cortactin - metabolism</subject><subject>Endothelial cells</subject><subject>Fibroblasts</subject><subject>Fibroblasts - cytology</subject><subject>Fibroblasts - physiology</subject><subject>Fibrosis</subject><subject>Gene expression regulation</subject><subject>Genes, abl</subject><subject>Genes, Reporter</subject><subject>Humans</subject><subject>Kinases</subject><subject>Kinetics</subject><subject>Luminescent Proteins - genetics</subject><subject>Mutation</subject><subject>Oncogene Proteins - physiology</subject><subject>Phosphorylation</subject><subject>Polymerization</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proteins</subject><subject>Studies</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc2LFDEQxYMo7rh69Kg2Hrz1Wknnqy8Ly-IXLOxB9xzSSfVMhpnOmKQV_3vTzDB-nIri_Xi8qkfISwpXFHT3fuuGKwagoQctHpEVFRxaTTk8JisARtteMHFBnuW8BQCuePeUXNCeUy4prMj9TVo3YSqYrCu5-RnKpnExlbqFqSmxOaS4jwUb6zeYQ5xajwecPE6lcbjbNejXuEAlzYv8nDwZ7S7ji9O8JA8fP3y7_dze3X_6cntz1zoudGm5QK20663rhaXCayqdhVHL0eEgB99TCUpzOVL0DAffORB66JUatPbSs-6SXB99D_OwR-9qnmR35pDC3qZfJtpg_lWmsDHr-MMwBdD1shq8Oxmk-H3GXMw-5OUiO2Gcs5GqfhWEquDb_8BtnNNUjzOMKspk_XuF2iPkUsw54XhOQsEsPZnakzn3VPnXf8f_Q5-KqcCrI7DNJaazzkB0iqkl_pujPtpo7DqFbB6-MqAdUMk0dLr7DW-Oon8</recordid><startdate>20090504</startdate><enddate>20090504</enddate><creator>Lapetina, Stefanie</creator><creator>Mader, Christopher C</creator><creator>Machida, Kazuya</creator><creator>Mayer, Bruce J</creator><creator>Koleske, Anthony J</creator><general>The Rockefeller University Press</general><general>Rockefeller University Press</general><scope>FBQ</scope><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>20090504</creationdate><title>Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion</title><author>Lapetina, Stefanie ; Mader, Christopher C ; Machida, Kazuya ; Mayer, Bruce J ; Koleske, Anthony J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-45e878c9ac95a15d816ca0f86fceb6bd91607846f1ed2ebd3c058b977b88d6d23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Actins</topic><topic>Actins - metabolism</topic><topic>Adaptor Proteins, Signal Transducing</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Cell adhesion</topic><topic>Cell adhesion & migration</topic><topic>Cell Adhesion - physiology</topic><topic>Cell Membrane - physiology</topic><topic>Cell Movement - physiology</topic><topic>Cells</topic><topic>Cortactin - metabolism</topic><topic>Endothelial cells</topic><topic>Fibroblasts</topic><topic>Fibroblasts - cytology</topic><topic>Fibroblasts - physiology</topic><topic>Fibrosis</topic><topic>Gene expression regulation</topic><topic>Genes, abl</topic><topic>Genes, Reporter</topic><topic>Humans</topic><topic>Kinases</topic><topic>Kinetics</topic><topic>Luminescent Proteins - genetics</topic><topic>Mutation</topic><topic>Oncogene Proteins - physiology</topic><topic>Phosphorylation</topic><topic>Polymerization</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proteins</topic><topic>Studies</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lapetina, Stefanie</creatorcontrib><creatorcontrib>Mader, Christopher C</creatorcontrib><creatorcontrib>Machida, Kazuya</creatorcontrib><creatorcontrib>Mayer, Bruce J</creatorcontrib><creatorcontrib>Koleske, Anthony J</creatorcontrib><collection>AGRIS</collection><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>Lapetina, Stefanie</au><au>Mader, Christopher C</au><au>Machida, Kazuya</au><au>Mayer, Bruce J</au><au>Koleske, Anthony J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2009-05-04</date><risdate>2009</risdate><volume>185</volume><issue>3</issue><spage>503</spage><epage>519</epage><pages>503-519</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>The molecular mechanisms by which the Abelson (Abl) or Abl-related gene (Arg) kinases interface with the actin polymerization machinery to promote cell edge protrusions during cell-matrix adhesion are unclear. In this study, we show that interactions between Arg and the Arp2/3 complex regulator cortactin are essential to mediate actin-based cell edge protrusion during fibroblast adhesion to fibronectin. Arg-deficient and cortactin knockdown fibroblasts exhibit similar defects in adhesion-dependent cell edge protrusion, which can be restored via reexpression of Arg and cortactin. Arg interacts with cortactin via both binding and catalytic events. The cortactin Src homology (SH) 3 domain binds to a Pro-rich motif in the Arg C terminus. Arg mediates adhesion-dependent phosphorylation of cortactin, creating an additional binding site for the Arg SH2 domain. Mutation of residues that mediate Arg-cortactin interactions abrogate the abilities of both proteins to support protrusions, and the Nck adapter, which binds phosphocortactin, is also required. These results demonstrate that interactions between Arg, cortactin, and Nck1 are critical to promote adhesion-dependent cell edge protrusions.</abstract><cop>United States</cop><pub>The Rockefeller University Press</pub><pmid>19414610</pmid><doi>10.1083/jcb.200809085</doi><tpages>17</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Actins Actins - metabolism Adaptor Proteins, Signal Transducing Animals Binding Sites Cell adhesion Cell adhesion & migration Cell Adhesion - physiology Cell Membrane - physiology Cell Movement - physiology Cells Cortactin - metabolism Endothelial cells Fibroblasts Fibroblasts - cytology Fibroblasts - physiology Fibrosis Gene expression regulation Genes, abl Genes, Reporter Humans Kinases Kinetics Luminescent Proteins - genetics Mutation Oncogene Proteins - physiology Phosphorylation Polymerization Protein-Tyrosine Kinases - metabolism Proteins Studies |
| title | Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion |
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