ABHD7-mediated depalmitoylation of lamin A promotes myoblast differentiation

Cell Rep. 2024 Feb 27;43(2):113720. doi: 10.1016/j.celrep.2024.113720. Epub 2024 Feb 2.

Abstract

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.

Keywords: ABHD7; CP: Molecular biology; CP: Stem cell research; ZDHHC5; lactate; lamin A; myoblast differentiation; palmitoylation.

MeSH terms

  • Animals
  • Cell Differentiation
  • Lamin Type A* / metabolism
  • Mice
  • Muscular Dystrophies* / genetics
  • Myoblasts / metabolism
  • Protein Processing, Post-Translational

Substances

  • Lamin Type A
  • Lmna protein, mouse