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. 2019 Oct 25;9:15283. doi: 10.1038/s41598-019-51689-6

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© The Author(s) 2019

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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Integrin α11 cytoplasmic tail contributes to FAK and ERK activation. (A) Serum-starved _Huα11-WT and _Huα11-1171 cells were plated on collagen I in serum-free conditions and cells were lysed at different time points (T0, T30, T45 and T60). Total and phosphorylated levels of FAK^Y397, ERK, p38, JNK were detected by Western blotting and the protein bands were quantified by densitometry analysis (full size immunoblots are shown in supplementary). (B) Human gingival fibroblasts (hGFs) were transfected with control (ctrl) siRNA or α11 siRNA (SMARTpool) and 48 hours post transfection, cells were serum-starved and plated on collagen I in serum-free conditions. After 30 mins, cells were lysed, and the lysates were analyzed by western blotting. Protein bands were quantified by densitometry analysis. Statistical significance was assessed by two tailed, unpaired t-tests and P-values are expressed as ***P < 0.001; **P < 0.01 and *P < 0.05.