Cell Reports (Feb 2024)

ABHD7-mediated depalmitoylation of lamin A promotes myoblast differentiation

  • Yuan Shen,
  • Liang-Liang Zheng,
  • Cai-Yun Fang,
  • Yao-Yao Xu,
  • Chao Wang,
  • Jin-Tao Li,
  • Ming-Zhu Lei,
  • Miao Yin,
  • Hao-Jie Lu,
  • Qun-Ying Lei,
  • Jia Qu

Journal volume & issue
Vol. 43, no. 2
p. 113720

Abstract

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Summary: LMNA gene mutation can cause muscular dystrophy, and post-translational modification plays a critical role in regulating its function. Here, we identify that lamin A is palmitoylated at cysteine 522, 588, and 591 residues, which are reversely catalyzed by palmitoyltransferase zinc finger DHHC-type palmitoyltransferase 5 (ZDHHC5) and depalmitoylase α/β hydrolase domain 7 (ABHD7). Furthermore, the metabolite lactate promotes palmitoylation of lamin A by inhibiting the interaction between it and ABHD7. Interestingly, low-level palmitoylation of lamin A promotes, whereas high-level palmitoylation of lamin A inhibits, murine myoblast differentiation. Together, these observations suggest that ABHD7-mediated depalmitoylation of lamin A controls myoblast differentiation.

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