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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, examined using membrane-based yeast two-hybrid analyses. DSY-1 yeast cells co-expressing pDHB1-CNGA1 and pAlg5-NubG as negative control, CNGA1 + Grb14 as positive control, and CNGA1 + RA-PI3Kα and γ isoforms, respectively. The membrane and cytosolic fractions of yeast were subjected to immunoblot analysis with anti-CNGA1 and anti-G6PDH antibodies (A). All other expressed proteins (either alone or co-expressed) were immunoblotted with anti-CNGA1 antibody (B). Transformants were assayed for β-galactosidase assay by colony color by filter lift assay (C) or quantitative determination of β-galactosidase activity by the solution assay (D). Data are mean ± SD, n = 6, *p < 0.001 (significance between RA-PI3Kγ compared to RA-PI3Kα).