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Actin maturation requires the ACTMAP/C19orf54 protease.

Peter Haahr1,2, Ricardo A Galli3, Lisa G van den Hengel1,4

  • 1Division of Biochemistry, Netherlands Cancer Institute, 1066CX Amsterdam, Netherlands.

Science (New York, N.Y.)
|September 29, 2022
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Summary

Researchers identified ACTMAP as the enzyme that matures actin by removing methionine post-translation. Its absence leads to immature actin, shorter muscle filaments, and myopathy hallmarks in mice.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein synthesis typically initiates with methionine, which is usually removed during translation.
  • Cytoplasmic actin undergoes a unique post-translational modification involving the removal of acetylated methionine by an unknown enzyme.

Purpose of the Study:

  • To identify the enzyme responsible for the noncanonical post-translational modification of actin.
  • To investigate the in vivo function of this enzyme in actin maturation and its role in muscle physiology.

Main Methods:

  • Enzyme identification through genetic screening and biochemical assays.
  • Generation and analysis of knockout mice lacking the identified enzyme.
  • Assessment of cytoskeletal structure, actin filament length, muscle function, and histological features in mutant mice.

Main Results:

  • C19orf54, designated ACTMAP (actin maturation protease), was identified as the enzyme responsible for removing acetylated methionine from actin.
  • Ablation of ACTMAP resulted in mice with immature actin across all tissues.
  • Skeletal muscles of ACTMAP-deficient mice exhibited shorter sarcomeric actin filaments, reduced muscle function, and progressive accumulation of centralized nuclei, indicative of myopathy.

Conclusions:

  • ACTMAP is the crucial enzyme for producing mature cytoplasmic actin.
  • ACTMAP plays a vital role in maintaining normal actin filament length and muscle function.
  • Deficiency in ACTMAP leads to actin-related myopathies.