p120-Catenin and p190RhoGAP Regulate Cell-Cell Adhesion by Coordinating Antagonism between Rac and Rho
Integration of receptor tyrosine kinase, integrin, and cadherin activities is crucial for normal cell growth, motility, and adhesion. Here, we describe roles for p120-catenin (p120) and p190RhoGAP that coordinate crosstalk between these systems and regulate cadherin function. Surprisingly, PDGFR-ind...
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| Veröffentlicht in: | Cell 2006-12, Vol.127 (5), p.1027-1039 |
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| container_title | Cell |
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| creator | Wildenberg, Gregg A. Dohn, Michael R. Carnahan, Robert H. Davis, Michael A. Lobdell, Nichole A. Settleman, Jeffrey Reynolds, Albert B. |
| description | Integration of receptor tyrosine kinase, integrin, and cadherin activities is crucial for normal cell growth, motility, and adhesion. Here, we describe roles for p120-catenin (p120) and p190RhoGAP that coordinate crosstalk between these systems and regulate cadherin function. Surprisingly, PDGFR-induced actin remodeling in NIH3T3 cells is blocked in the absence of p120, and the cells are partially transformed via constitutive activation of Rho. We have traced the mechanism to unexpected codependent roles for p120 and p190RhoGAP in regulating Rac-dependent antagonism of Rho. Receptor-induced Rac activity causes translocation of p190RhoGAP to adherens junctions (AJs), where it couples to the cadherin complex via interaction with p120. AJ formation is dependent on this p120-p190RhoGAP interaction and fails altogether if either of these proteins are compromised. We propose that Rac activation links diverse signaling systems to AJ assembly by controlling transient p190RhoGAP interactions with p120 and localized inhibition of Rho. |
| doi_str_mv | 10.1016/j.cell.2006.09.046 |
| format | Article |
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Here, we describe roles for p120-catenin (p120) and p190RhoGAP that coordinate crosstalk between these systems and regulate cadherin function. Surprisingly, PDGFR-induced actin remodeling in NIH3T3 cells is blocked in the absence of p120, and the cells are partially transformed via constitutive activation of Rho. We have traced the mechanism to unexpected codependent roles for p120 and p190RhoGAP in regulating Rac-dependent antagonism of Rho. Receptor-induced Rac activity causes translocation of p190RhoGAP to adherens junctions (AJs), where it couples to the cadherin complex via interaction with p120. AJ formation is dependent on this p120-p190RhoGAP interaction and fails altogether if either of these proteins are compromised. 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Here, we describe roles for p120-catenin (p120) and p190RhoGAP that coordinate crosstalk between these systems and regulate cadherin function. Surprisingly, PDGFR-induced actin remodeling in NIH3T3 cells is blocked in the absence of p120, and the cells are partially transformed via constitutive activation of Rho. We have traced the mechanism to unexpected codependent roles for p120 and p190RhoGAP in regulating Rac-dependent antagonism of Rho. Receptor-induced Rac activity causes translocation of p190RhoGAP to adherens junctions (AJs), where it couples to the cadherin complex via interaction with p120. AJ formation is dependent on this p120-p190RhoGAP interaction and fails altogether if either of these proteins are compromised. We propose that Rac activation links diverse signaling systems to AJ assembly by controlling transient p190RhoGAP interactions with p120 and localized inhibition of Rho.</description><subject>Actins - metabolism</subject><subject>Adherens Junctions - metabolism</subject><subject>Animals</subject><subject>Catenins</subject><subject>Cell Adhesion</subject><subject>Cell Adhesion Molecules - deficiency</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Line, Transformed</subject><subject>Cell Proliferation</subject><subject>Cell Surface Extensions - metabolism</subject><subject>Culture Media, Serum-Free</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fibroblasts - cytology</subject><subject>Fibronectins - metabolism</subject><subject>GTPase-Activating Proteins - metabolism</subject><subject>Integrins - metabolism</subject><subject>Mice</subject><subject>Models, Biological</subject><subject>NIH 3T3 Cells</subject><subject>Phosphoproteins - deficiency</subject><subject>Phosphoproteins - metabolism</subject><subject>rac GTP-Binding Proteins - antagonists & inhibitors</subject><subject>rac GTP-Binding Proteins - metabolism</subject><subject>Receptors, Platelet-Derived Growth Factor - metabolism</subject><subject>Repressor Proteins - metabolism</subject><subject>rho GTP-Binding Proteins - antagonists & inhibitors</subject><subject>rho GTP-Binding Proteins - metabolism</subject><subject>Stress Fibers - metabolism</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMGO0zAQhi0EYsvCC3BAPnFLmHEdO5a4VNGyIK0EquBsOfak66q1S5yC9u1JaCVuXDwH__83mo-xtwg1AqoP-9rT4VALAFWDqUGqZ2yFYHQlUYvnbAVgRNUqLW_Yq1L2ANA2TfOS3aBGYXSrVmw4oYCqcxOlmLhLgZ_QwPYx32--8S3tzof5i3fznmp5-CY8Uok58f6JdzmPISY3xbTjmzS5XU6xHHlP02-ixLfO_yXOtNfsxeAOhd5c5y378enue_e5evh6_6XbPFReKjlVodcqKOFArLFdmwF70E4YNRiUTb8WhEqGwaFooB8chAYHSV73gNqDb936lr2_cE9j_nmmMtljLIsllyifi1Uttko0cg6KS9CPuZSRBnsa49GNTxbBLnbt3i49u9i1YOxsdy69u9LP_ZHCv8pV5xz4eAnQfOOvSKMtPlLyFOJIfrIhx__x_wBcOYm_</recordid><startdate>20061201</startdate><enddate>20061201</enddate><creator>Wildenberg, Gregg A.</creator><creator>Dohn, Michael R.</creator><creator>Carnahan, Robert H.</creator><creator>Davis, Michael A.</creator><creator>Lobdell, Nichole A.</creator><creator>Settleman, Jeffrey</creator><creator>Reynolds, Albert B.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>20061201</creationdate><title>p120-Catenin and p190RhoGAP Regulate Cell-Cell Adhesion by Coordinating Antagonism between Rac and Rho</title><author>Wildenberg, Gregg A. ; Dohn, Michael R. ; Carnahan, Robert H. ; Davis, Michael A. ; Lobdell, Nichole A. ; Settleman, Jeffrey ; Reynolds, Albert B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c464t-db76d62a0231839f1b07a296f9145b32e164dfa1250bfa0d51f4ec7b017c0c8a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Actins - metabolism</topic><topic>Adherens Junctions - metabolism</topic><topic>Animals</topic><topic>Catenins</topic><topic>Cell Adhesion</topic><topic>Cell Adhesion Molecules - deficiency</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Cell Line, Transformed</topic><topic>Cell Proliferation</topic><topic>Cell Surface Extensions - metabolism</topic><topic>Culture Media, Serum-Free</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Fibroblasts - cytology</topic><topic>Fibronectins - metabolism</topic><topic>GTPase-Activating Proteins - metabolism</topic><topic>Integrins - metabolism</topic><topic>Mice</topic><topic>Models, Biological</topic><topic>NIH 3T3 Cells</topic><topic>Phosphoproteins - deficiency</topic><topic>Phosphoproteins - metabolism</topic><topic>rac GTP-Binding Proteins - antagonists & inhibitors</topic><topic>rac GTP-Binding Proteins - metabolism</topic><topic>Receptors, Platelet-Derived Growth Factor - metabolism</topic><topic>Repressor Proteins - metabolism</topic><topic>rho GTP-Binding Proteins - antagonists & inhibitors</topic><topic>rho GTP-Binding Proteins - metabolism</topic><topic>Stress Fibers - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wildenberg, Gregg A.</creatorcontrib><creatorcontrib>Dohn, Michael R.</creatorcontrib><creatorcontrib>Carnahan, Robert H.</creatorcontrib><creatorcontrib>Davis, Michael A.</creatorcontrib><creatorcontrib>Lobdell, Nichole A.</creatorcontrib><creatorcontrib>Settleman, Jeffrey</creatorcontrib><creatorcontrib>Reynolds, Albert B.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wildenberg, Gregg A.</au><au>Dohn, Michael R.</au><au>Carnahan, Robert H.</au><au>Davis, Michael A.</au><au>Lobdell, Nichole A.</au><au>Settleman, Jeffrey</au><au>Reynolds, Albert B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>p120-Catenin and p190RhoGAP Regulate Cell-Cell Adhesion by Coordinating Antagonism between Rac and Rho</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2006-12-01</date><risdate>2006</risdate><volume>127</volume><issue>5</issue><spage>1027</spage><epage>1039</epage><pages>1027-1039</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Integration of receptor tyrosine kinase, integrin, and cadherin activities is crucial for normal cell growth, motility, and adhesion. Here, we describe roles for p120-catenin (p120) and p190RhoGAP that coordinate crosstalk between these systems and regulate cadherin function. Surprisingly, PDGFR-induced actin remodeling in NIH3T3 cells is blocked in the absence of p120, and the cells are partially transformed via constitutive activation of Rho. We have traced the mechanism to unexpected codependent roles for p120 and p190RhoGAP in regulating Rac-dependent antagonism of Rho. Receptor-induced Rac activity causes translocation of p190RhoGAP to adherens junctions (AJs), where it couples to the cadherin complex via interaction with p120. AJ formation is dependent on this p120-p190RhoGAP interaction and fails altogether if either of these proteins are compromised. 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| subjects | Actins - metabolism Adherens Junctions - metabolism Animals Catenins Cell Adhesion Cell Adhesion Molecules - deficiency Cell Adhesion Molecules - metabolism Cell Line, Transformed Cell Proliferation Cell Surface Extensions - metabolism Culture Media, Serum-Free DNA-Binding Proteins - metabolism Fibroblasts - cytology Fibronectins - metabolism GTPase-Activating Proteins - metabolism Integrins - metabolism Mice Models, Biological NIH 3T3 Cells Phosphoproteins - deficiency Phosphoproteins - metabolism rac GTP-Binding Proteins - antagonists & inhibitors rac GTP-Binding Proteins - metabolism Receptors, Platelet-Derived Growth Factor - metabolism Repressor Proteins - metabolism rho GTP-Binding Proteins - antagonists & inhibitors rho GTP-Binding Proteins - metabolism Stress Fibers - metabolism |
| title | p120-Catenin and p190RhoGAP Regulate Cell-Cell Adhesion by Coordinating Antagonism between Rac and Rho |
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