Regulation of N-myristoyltransferase by the calpain and caspase systems
Sharma, R.K.; Kumar, S.; Parameswaran, S.; Dimmock, J.R.
Indian Journal of Biochemistry and Biophysics 51(6): 506-511
2014
ISSN/ISBN: 0301-1208 PMID: 25823223 Document Number: 678581
N-myristoyltransferase (NMT) is an essential eukaryotic enzyme which catalyzes the transfer of the myristoyl group to the terminal glycine residue of a number of proteins including those involved in signal transduction and apoptotic pathways. In higher eukaryotes, two isoforms of NMT have been identified (NMT1 and NMT2) which share about 76% amino acid sequence identity in humans. Protein-protein interactions of NMTs reveal that m-calpain interacts with NMT1 whereas caspase-3 interacts with NMT2. These findings reveal differential interactions of both isoforms of NMT with various signaling molecules. This minireview provides an overview of the regulation of N-myristoyltransferase by calpain and caspase systems.