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. 2024 Oct 11;22:488. doi: 10.1186/s12964-024-01873-7

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by-nc-nd/4.0/.

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Fig. 6 — SYTL4 contributes to BMP-2 ubiquitination and degradation. (A, C) Silencing SYTL4 abolished the effects of nesfatin-1 knockdown on the ubiquitination of BMP-2. (B, D) Silencing SYTL4 abolished the effects of nesfatin-1 knockdown on the protein expression of BMP-2. (E) High Pi increased the interaction of nesfatin-1 with SYTL4. (F) High Pi decreased the interaction of BMP-2 with SYTL4. (G) Overexpression of SYTL4 attenuated the deposition of calcium and ALP activity induced by nesfatin-1 overexpression. (H) Downregulation of SYTL4 attenuated the effects of nesfatin-1 deficiency on calcium deposition and ALP activity in VSMCs exposed to high Pi. Differences between groups were assessed with ANOVA followed by Bonferroni post-hoc test (C-D, G-H). The P-value was calculated by unpaired two-tailed Student’s t-test (E-F). *P < 0.05, **P < 0.01, ***P < 0.001 versus the indicated group. n = 6