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. 2015 Jun 17;9(4):186–195. doi: 10.1080/19336950.2015.1058454

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© 2015 The Author(s). Published with license by Taylor & Francis Group, LLC

© Jinhong Wie, Byung Joo Kim, Jongyun Myeong, Kotdaji Ha, Seung Joo Jeong, Dongki Yang, Euiyong Kim, Ju-Hong Jeon, and Insuk So

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 3. — Gα_i and TRPC4β interact with Rasd1. Rasd1-CFP and Gα_i1 was co-transfected in HEK293 cells. Immunoprecipitation was performed with Gα_i1followed by immunoblotting with GFP antibody. Total proteins of Rasd1-CFP and Gα_i1 were detected using GFP and Gα_i1 antibody. (B) FRET efficiency was measured in HEK293 cells Rasd1-CFP, Gα_i2 WT-YFP, Gα_i2 QL-YFP, Gq WT-YFP, Gq QL-YFP, YFP-mTRPC4β, mTRPC4β-CFP, YFP-mTRPC5, YFP-GβGγ, and GβYFP-Gγ. Among these proteins, Rasd1 bound Gα_i2 WT, Gα_i2 QL, and Gq WT. QL: Constitutively active form Q205L to impair GTPase activity of Gα_i2.