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. 2017 Aug 24;7:9302. doi: 10.1038/s41598-017-09434-4

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Acetylation and cleavage of IQGAP1. (A) Cells were treated with nicotinamide (NAM) or phenylbutyrate (PB) at 5 mmol/l for 24 hours. Cell lysates were then analyzed by western blotting. Acetylated proteins were detected with an acetylated lysine-specific antibody. Identity of the IQGAP1 band was confirmed by subsequent co-staining with an anti-IQGAP1 antibody. Cropped gels are shown. (B) Bar graph and statistical analysis of IQGAP1 acetylation in untreated, NAM treated and PB treated cells. (C) Endogenous IQGAP1 is immunoprecipitated from lysates of NAM-treated aortic smooth muscle cells with an acetylated lysine-specific antibody, but not with a GFP antibody. A cropped gel is shown. (D) Treatment with NAM or PB results in reduced cleavage of IQGAP1 relative to full length IQGAP1. Cropped gels are shown. (E) The bar graph shows full length IQGAP1 relative to the sum of full length IQGAP1 and smaller IQGAP1 fragments (normalized to control). (*p < 0.05, **p < 0.01).