Binding Properties and Stability of the Ras-Association Domain of Rap1-GTP Interacting Adapter Molecule (RIAM)

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dc.contributor.author Takala, Heikki
dc.contributor.author Ylänne, Jari
dc.date.accessioned 2012-08-21T11:46:54Z
dc.date.available 2012-08-21T11:46:54Z
dc.date.issued 2012
dc.identifier.citation Takala H, Ylänne J (2012) Binding Properties and Stability of the Ras-Association Domain of Rap1-GTP Interacting Adapter Molecule (RIAM). PLoS ONE 7(4): e31955. doi:10.1371/journal.pone.0031955
dc.identifier.issn 1932-6203
dc.identifier.uri http://hdl.handle.net/123456789/38344
dc.description.abstract The Rap1-GTP interacting adapter protein (RIAM) is an important protein in Rap1-mediated integrin activation. By binding to both Rap1 GTPase and talin, RIAM recruits talin to the cell membrane, thus facilitating talin-dependent integrin activation. In this article, we studied the role of the RIAM Ras-association (RA) and pleckstrin-homology (PH) domains in the interaction with Rap1. We found that the RA domain was sufficient for GTP-dependent interaction with Rap1B, and the addition of the PH domain did not change the binding affinity. We also detected GTP-independent interaction of Rap1B with the N-terminus of RIAM. In addition, we found that the PH domain stabilized the RA domain both in vitro and in cells. fi
dc.language.iso eng
dc.publisher Public Library of Science
dc.relation.ispartofseries PLoS ONE
dc.rights © 2012 Takala, Ylänne. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.subject.other RIAM fi
dc.subject.other sitoutuminen fi
dc.subject.other integriinit fi
dc.subject.other interaction en
dc.subject.other integrins en
dc.title Binding Properties and Stability of the Ras-Association Domain of Rap1-GTP Interacting Adapter Molecule (RIAM)
dc.type Article en
dc.identifier.urn URN:NBN:fi:jyu-201208212213
dc.subject.kota 118
dc.contributor.laitos Bio- ja ympäristötieteiden laitos fi
dc.contributor.laitos The Department of Biological and Environmental Science en
dc.type.uri http://purl.org/eprint/type/JournalArticle
dc.identifier.doi doi:10.1371/journal.pone.0031955
dc.description.version Publisher's PDF
eprint.status http://purl.org/eprint/type/status/PeerReviewed

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