RIAM, an Ena/VASP and Profilin Ligand, Interacts with Rap1-GTP and Mediates Rap1-Induced Adhesion
The small GTPase Rap1 induces integrin-mediated adhesion and changes in the actin cytoskeleton. The mechanisms that mediate these effects of Rap1 are poorly understood. We have identified RIAM as a Rap1-GTP-interacting adaptor molecule. RIAM defines a family of adaptor molecules that contain a RA-li...
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| Format: | Article |
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Elsevier
2014
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| Online Access: | http://hdl.handle.net/1721.1/83508 https://orcid.org/0000-0003-3214-4554 |
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| author | Lafuente, Esther M. Krause, Matthias Carman, Christopher V. Freeman, Gordon J. Berezovskaya, Alla Constantine, Erica Springer, Timothy A. Boussiotis, Vassiliki A. Gertler, Frank van Puijenbroek, Andre A.F.L. |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Lafuente, Esther M. Krause, Matthias Carman, Christopher V. Freeman, Gordon J. Berezovskaya, Alla Constantine, Erica Springer, Timothy A. Boussiotis, Vassiliki A. Gertler, Frank van Puijenbroek, Andre A.F.L. |
| author_sort | Lafuente, Esther M. |
| collection | MIT |
| description | The small GTPase Rap1 induces integrin-mediated adhesion and changes in the actin cytoskeleton. The mechanisms that mediate these effects of Rap1 are poorly understood. We have identified RIAM as a Rap1-GTP-interacting adaptor molecule. RIAM defines a family of adaptor molecules that contain a RA-like (Ras association) domain, a PH (pleckstrin homology) domain, and various proline-rich motifs. RIAM also interacts with Profilin and Ena/VASP proteins, molecules that regulate actin dynamics. Overexpression of RIAM induced cell spreading and lamellipodia formation, changes that require actin polymerization. In contrast, RIAM knockdown cells had reduced content of polymerized actin. RIAM overexpression also induced integrin activation and cell adhesion. RIAM knockdown displaced Rap1-GTP from the plasma membrane and abrogated Rap1-induced adhesion. Thus, RIAM links Rap1 to integrin activation and plays a role in regulating actin dynamics. |
| first_indexed | 2024-09-23T12:50:18Z |
| format | Article |
| id | mit-1721.1/83508 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T12:50:18Z |
| publishDate | 2014 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | mit-1721.1/835082022-10-01T11:24:04Z RIAM, an Ena/VASP and Profilin Ligand, Interacts with Rap1-GTP and Mediates Rap1-Induced Adhesion Lafuente, Esther M. Krause, Matthias Carman, Christopher V. Freeman, Gordon J. Berezovskaya, Alla Constantine, Erica Springer, Timothy A. Boussiotis, Vassiliki A. Gertler, Frank van Puijenbroek, Andre A.F.L. Massachusetts Institute of Technology. Department of Biology Krause, Matthias Gertler, Frank The small GTPase Rap1 induces integrin-mediated adhesion and changes in the actin cytoskeleton. The mechanisms that mediate these effects of Rap1 are poorly understood. We have identified RIAM as a Rap1-GTP-interacting adaptor molecule. RIAM defines a family of adaptor molecules that contain a RA-like (Ras association) domain, a PH (pleckstrin homology) domain, and various proline-rich motifs. RIAM also interacts with Profilin and Ena/VASP proteins, molecules that regulate actin dynamics. Overexpression of RIAM induced cell spreading and lamellipodia formation, changes that require actin polymerization. In contrast, RIAM knockdown cells had reduced content of polymerized actin. RIAM overexpression also induced integrin activation and cell adhesion. RIAM knockdown displaced Rap1-GTP from the plasma membrane and abrogated Rap1-induced adhesion. Thus, RIAM links Rap1 to integrin activation and plays a role in regulating actin dynamics. National Institutes of Health (U.S.) (Grant AI 43552) National Institutes of Health (U.S.) (Grant AI 46584) National Institutes of Health (U.S.) (Grant AI 41584) National Institutes of Health (U.S.) (Grant GM68676) 2014-01-06T18:40:38Z 2014-01-06T18:40:38Z 2004-10 2004-07 Article http://purl.org/eprint/type/JournalArticle 15345807 1878-1551 http://hdl.handle.net/1721.1/83508 Lafuente, Esther M., Andre A.F.L. van Puijenbroek, Matthias Krause, Christopher V. Carman, Gordon J. Freeman, Alla Berezovskaya, Erica Constantine, Timothy A. Springer, Frank B. Gertler, and Vassiliki A. Boussiotis. “RIAM, an Ena/VASP and Profilin Ligand, Interacts with Rap1-GTP and Mediates Rap1-Induced Adhesion.” Developmental Cell 7, no. 4 (October 2004): 585-595. Copyright © 2004 Cell Press https://orcid.org/0000-0003-3214-4554 en_US http://dx.doi.org/10.1016/j.devcel.2004.07.021 Developmental Cell Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf Elsevier Elsevier Open Archive |
| spellingShingle | Lafuente, Esther M. Krause, Matthias Carman, Christopher V. Freeman, Gordon J. Berezovskaya, Alla Constantine, Erica Springer, Timothy A. Boussiotis, Vassiliki A. Gertler, Frank van Puijenbroek, Andre A.F.L. RIAM, an Ena/VASP and Profilin Ligand, Interacts with Rap1-GTP and Mediates Rap1-Induced Adhesion |
| title | RIAM, an Ena/VASP and Profilin Ligand, Interacts with Rap1-GTP and Mediates Rap1-Induced Adhesion |
| title_full | RIAM, an Ena/VASP and Profilin Ligand, Interacts with Rap1-GTP and Mediates Rap1-Induced Adhesion |
| title_fullStr | RIAM, an Ena/VASP and Profilin Ligand, Interacts with Rap1-GTP and Mediates Rap1-Induced Adhesion |
| title_full_unstemmed | RIAM, an Ena/VASP and Profilin Ligand, Interacts with Rap1-GTP and Mediates Rap1-Induced Adhesion |
| title_short | RIAM, an Ena/VASP and Profilin Ligand, Interacts with Rap1-GTP and Mediates Rap1-Induced Adhesion |
| title_sort | riam an ena vasp and profilin ligand interacts with rap1 gtp and mediates rap1 induced adhesion |
| url | http://hdl.handle.net/1721.1/83508 https://orcid.org/0000-0003-3214-4554 |
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