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. 2018 May 2;11:24. doi: 10.1186/s13041-018-0368-5

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© The Author(s). 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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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Fig. 2 — Effect of Cav3.1-GFP and Cav3.2-GFP C-terminal deletions on SPTAN1 and SPTBN2 binding in tsA-201 cells. (a) Cav3.1-GFP ∆CT (1851–1875) and wild type channel immunoprecipitates probed with anti-Spectrin αII (SPTAN1) polyclonal antibody. Densitometry analysis of SPTAN1 bound to Cav3.1-GFP immunoprecipitates is shown. (P = 0.0051, n = 3). (b) Cav3.2-GFP ∆CT (1860–1884) and wild type channel immunoprecipitates probed with anti-Spectrin αII (SPTAN1) polyclonal antibody. Densitometry analysis of SPTAN1 bound to Cav3.2-GFP immunoprecipitates is shown (P = 0.0005, n = 3). (c) Cav3.1-GFP ∆CT (1851–1875) and wild type channel immunoprecipitates probed with anti-Spectrin βII (SPTBN2) polyclonal antibody. Densitometry analysis of SPTBN2 bound to Cav3.1-GFP immunoprecipitates is shown (P = 0.0085, n = 3). (d) Cav3.2-GFP ∆CT (1860–1884) and wild type channel immunoprecipitates probed with anti-Spectrin βII (SPTBN2) polyclonal antibody. Densitometry analysis of SPTBN2 bound to Cav3.2-GFP immunoprecipitates is shown. (P = 0.0047, n = 3)