Journal
PROGRESS IN LIPID RESEARCH
Volume 85, Issue -, Pages -Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.plipres.2021.101139
Keywords
N-terminus; Cysteine; Glycine; Lysine; Compartments; Acylation
Funding
- French National Research Agency (ANR) [ANR-2010-BLAN-1611-01, ANR-20-CE440013]
- Fondation ARC [ARCPJA32020060002137]
- French State grant (EUR SPS-GSR) by the ANR [ANR-17-EUR-0007, ANR-11-IDEX-0003-02]
- I2BC crystallization platform by FRISBI [ANR-10-INSB-0501]
- IBiSA
- Paris-Saclay University
- Region Ile-de-France [17012695]
- Fondation pour la Recherche Medicale [FDT202001010779]
- Ile de France Region
- Plan Cancer
- CNRS
Ask authors/readers for more resources
Protein myristoylation is a common modification found in all living organisms, where myristate serves as a molecular anchor for tagged proteins targeting membranes. Activation of myristate to myristoyl coenzyme A is required in eukaryotes, while bacteria use derivatives for conversion. This process allows proteins to travel across membranes and endomembrane networks efficiently.
Protein myristoylation is a C14 fatty acid modification found in all living organisms. Myristoylation tags either the N-terminal alpha groups of cysteine or glycine residues through amide bonds or lysine and cysteine side chains directly or indirectly via glycerol thioester and ester linkages. Before transfer to proteins, myristate must be activated into myristoyl coenzyme A in eukaryotes or, in bacteria, to derivatives like phosphatidylethanolamine. Myristate originates through de novo biosynthesis (e.g., plants), from external uptake (e.g., human tissues), or from mixed origins (e.g., unicellular organisms). Myristate usually serves as a molecular anchor, allowing tagged proteins to be targeted to membranes and travel across endomembrane networks in eukaryotes. In this review, we describe and discuss the metabolic origins of protein-bound myristate. We review strategies for in vivo protein labeling that take advantage of click-chemistry with reactive analogs, and we discuss new approaches to the proteome-wide discovery of myristate-containing proteins. The machineries of myristoylation are described, along with how protein targets can be generated directly from translating precursors or from processed proteins. Few myristoylation catalysts are currently described, with only N-myristoyltransferase described to date in eukaryotes. Finally, we describe how viruses and bacteria hijack and exploit myristoylation for their pathogenicity.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available