Identification of a novel target of sulforaphane: Sulforaphane binds to acyl-protein thioesterase 2 (APT2) and attenuates its palmitoylation.
Biochem Biophys Res Commun
; 726: 150244, 2024 Sep 24.
Article
in En
| MEDLINE
| ID: mdl-38905785
ABSTRACT
Sulforaphane (SFaN) is a food-derived compound with several bioactive properties, including atherosclerosis, diabetes, and obesity treatment. However, the mechanisms by which SFaN exerts its various effects are still unclear. To elucidate the mechanisms of the various effects of SFaN, we explored novel SFaN-binding proteins using SFaN beads and identified acyl protein thioesterase 2 (APT2). We also found that SFaN binds to the APT2 via C56 residue and attenuates the palmitoylation of APT2, thereby reducing plasma membrane localization of APT2. This study reveals a novel bioactivity of SFaN as a regulator of APT2 protein palmitoylation.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Sulfoxides
/
Thiolester Hydrolases
/
Isothiocyanates
/
Lipoylation
Limits:
Humans
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
2024
Type:
Article