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Charcot-Marie-Tooth disease is one of the most common hereditary peripheral neuromuscular diseases, affecting one in every 2500 people.
Existing research shows that.
SIRT2 belongs to the third group of histone deacetylases, which control the acetylation status of several proteins, including α-tubulin.
Although SIRT2 can deacetylate α-tubulin in vitro, knocking out SIRT2 in mice does not change the acetylation level of α-tubulin in vivo, indicating that SIRT2 may deacetylate α-tubulin under special conditions.
Recently, researchers reported that wild-type GARS binds to the NAD+-dependent deacetylase SIRT2 and inhibits its deacetylation activity, resulting in acetylation of α-tubulin, which is the main substrate of SIRT2.
The catalytic domain of GARS closely interacts with SIRT2, which is also the location of the CMT2D mutation.
SIRT2 knockdown can save CMT-related phenotypes and lifespan of Drosophila.
SIRT2 knockdown can save CMT-related phenotypes and lifespan of Drosophila.
CMT2D mutant GARS cannot inhibit SIRT2 deacetylation, resulting in a decrease in acetylated α-tubulin.
Original source:
Original source:Yingying Zhaoet al.
Yingying Zhao et al.
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