Please Take Over This Page and Apply to be Editor-In-Chief for this topic: There can be one or more than one Editor-In-Chief. You may also apply to be an Associate Editor-In-Chief of one of the subtopics below. Please mail us  to indicate your interest in serving either as an Editor-In-Chief of the entire topic or as an Associate Editor-In-Chief for a subtopic. Please be sure to attach your CV and or biographical sketch.
Myristoylation is an irreversible, post-translational protein modification found in animals, plants, fungi and viruses. In this protein modification a myristoyl group (derived from myristic acid) is covalently attached via an amide bond to the alpha-amino group of an N-terminal glycine residue of a nascent polypeptide. The modification is catalyzed by the enzyme N-myristoyltransferase, and occurs most commonly on glycine residues exposed during co-translational N-terminal methionine removal. Myristoylation also occurs post-translationally, for example when previously internal glycine residues become exposed by caspase cleavage during apoptosis.
Myristoylation plays a vital role in membrane targeting and signal transduction in plant responses to environmental stress.
- Podell S and Gribskov M. (2004) "Predicting N-terminal myristoylation sites in plant proteins", BMC Genomics, 5, 37.
- Zha J, Weiler S, Oh KJ, Wei MC, Korsmeyer SJ (2000) "Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis", Science 290, 1761-1765.