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. 2015 Feb 3;13:7. doi: 10.1186/s12964-015-0087-9

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© Gupta et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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PI3Kα and γ isoforms associate with CNGA1 through their RA domain. The physical interaction of these domains was analyzed by reciprocal co-immunoprecipitations. The Flag-tagged RLD-CNGA1 domain and Myc-tagged PI3Kα and γ RA domains were transiently expressed in HEK-293 T cells. Expressed proteins were subjected to immunoprecipitation with either anti-Flag or anti-Myc antibodies or IgG. Anti-Flag and normal IgG IPs were subjected to immunoblot analysis with anti-Flag (A) and anti-Myc (B) antibodies along with Flag- and Myc-expressed protein lysates, whereas anti-Myc and normal IgG IPs were subjected to immunoblot analysis with anti-Myc (D) and anti-Flag (E) antibodies along with Myc- and Flag-expressed protein lysates. The relative binding was expressed as percentage of the RA-PI3K and RLD-CNGA1 and vice versa in each case (C, F). Data are mean ± SD, n = 3, *p < 0.001.