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. 2023 Jun 6;11:goad032. doi: 10.1093/gastro/goad032

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© The Author(s) 2023. Published by Oxford University Press and Sixth Affiliated Hospital of Sun Yat-sen University

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 9. — SIRT1 deacetylates CPT1A at the Lys675 site. (A) shNC or shSIRT1 HEK293T cells were transfected with either HA-CPT1A-WT or different mutant plasmids including K195R, K292R, K580R, and K675R. Cell lysates were immunoprecipitated with an anti-HA antibody and blotted with an anti-acetyl-lysine antibody. (B) Quantitative analysis of CPT1A acetylation levels in HEK293T cells transfected with either HA-CPT1A-WT or different mutant plasmids as indicated. (C) CPT1A protein stability time course in HEK293T cells transfected with HA-CPT1A-WT and HA-CPT1A-K675R mutants following treatment with 100 μg/μL of CHX. (D) HEK293T cells transfected with HA-CPT1A-WT or HA-CPT1A-K675R mutant plasmids; cell lysates were immunoprecipitated with anti-HA antibody and blotted with anti-acetyl-lysine and anti-ubiquitin antibodies. All results are representative of three independent experiments. Values are provided as means ± SD; *P < 0.05 (compared with the control group). NC, normal control; sh, short hairpin; HEK, human embryonic kidney; CHX, cycloheximide; Ac, acetylation; Ub, ubiquitin.