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Article Dans Une Revue Trends in Biochemical Sciences Année : 2020

Myristoylation, an ancient protein modification mirroring eukaryogenesis and evolution

Résumé

N-myristoylation (MYR) is a crucial fatty acylation catalyzed by N-myristoyltransferases (NMTs) that is likely to have appeared over 2 billion years ago. Proteome-wide approaches have now delivered an exhaustive list of substrates undergoing MYR across approximately 2% of any proteome, with constituents, several unexpected, associated with different membrane compartments. A set of \textless10 proteins conserved in eukaryotes probably represents the original set of N-myristoylated targets, marking major changes occurring throughout eukaryogenesis. Recent findings have revealed unexpected mechanisms and reactivity, suggesting competition with other acylations that are likely to influence cellular homeostasis and the steady state of the modification landscape. Here, we review recent advances in NMT catalysis, substrate specificity, and MYR proteomics, and discuss concepts regarding MYR during evolution.
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Dates et versions

hal-02571405 , version 1 (16-11-2020)

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Thierry Meinnel, Cyril Dian, Carmela Giglione. Myristoylation, an ancient protein modification mirroring eukaryogenesis and evolution. Trends in Biochemical Sciences, 2020, 45 (7), pp.619-632. ⟨10.1016/j.tibs.2020.03.007⟩. ⟨hal-02571405⟩
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