Binding Properties and Stability of the Ras-Association Domain of Rap1-GTP Interacting Adapter Molecule (RIAM)
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). https://doi.org/10.1371/journal.pone.0031955
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PLoS OneDate
2012Copyright
© 2012 Takala, Ylänne. This is an open-access article distributed under the terms of the Creative Commons Attribution License.
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.
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Public Library of ScienceISSN Search the Publication Forum
1932-6203
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http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0031955Publication in research information system
https://converis.jyu.fi/converis/portal/detail/Publication/21480681
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Except where otherwise noted, this item's license is described as © 2012 Takala, Ylänne. This is an open-access article distributed under the terms of the Creative Commons Attribution License.
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