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- W2025588265 abstract "Rho family GTPases play important roles in the regulation of the cell's actin cytoskeleton and mediate the repulsive and attractive effects of guidance molecules. Their interaction with single transmembrane receptors Plexins are of particular importance, since Plexin receptors are important for axon guidance, angiogenesis and also cancer. Our previous study mapped the interactions of small Rho GTPases, Rnd1 and active Rac1, with the plexin-B1 through a common region, the Rho GTPase Binding Domain (RBD)[1]. And NMR relaxation experiments on the RBD: Rac1 complex revealed that the Rac1 is less dynamic in the Plexin bound state[2]. To further address the mechanism under the specificity and different functions of different Rho GTPase involving Plexin-B1, we present here the dynamical behavior of Rac1 and Rnd1, and the changes upon their association with plexin-B1 RBD. Solution NMR as well as mass spectrometry experiments are conducted to monitor the amide hydrogen exchange process. Both Rnd1 and Rac1 become rigid in general, especially in the switch I and switch II regions. In addition, both GTPases show complimentary dynamics changes distal from the binding sites, indicating an allosteric signaling mechanism. This also suggests a more direct role of Rho GTPase upon binding to Plexin-B1, rather than simply being sequestrated by Plexin-B1. More importantly, the dynamical study revealed the binding with Plexin-B1 RBD induces different changes in the dynamics and in different regions of the two GTPases. These are in accord with previous thermodynamic measurements and implies a difference in the mechanism of action of the two Rho GTPases-Rac1 and Rnd1, upon interaction with Plexin-B1[3]. These studies together suggest the origin of the specificity of the GTPase- protein interaction and signaling in the plexin-B1 system." @default.
- W2025588265 created "2016-06-24" @default.
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- W2025588265 date "2015-01-01" @default.
- W2025588265 modified "2023-09-27" @default.
- W2025588265 title "Allosteric Communication in Rnd1 and Rac1 Association with the Plexin-B1 RhoGTPase Binding Domain Revealed by Hydrogen Exchange Mass Spectroscopy and by Solution NMR" @default.
- W2025588265 doi "https://doi.org/10.1016/j.bpj.2014.11.1022" @default.
- W2025588265 hasPublicationYear "2015" @default.
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