Phosphorylation and dephosphorylation of human myristoyltransferase type 1.
N-Myristoyltransferase (NMT) is an essential eukaryotic enzyme that catalyzes the co-translational and (or) post-translational transfer of myristate to the amino terminal glycine residue of a number of important proteins, especially the non-receptor tyrosine kinases whose activity is important for tumorigenesis. Human NMT was found to be phosphorylated by non-receptor tyrosine kinase family members of Lyn, Fyn, and Lck and dephosphorylated by the Ca2+/calmodulin-dependent protein phosphatase, calcineurin. In this review, we discuss the cross-talk that exists between NMT and their N-myristoylated protein substrates. The cross-talk among NMT, tyrosine kinases, and phosphatases may be determined by their subcellular localization and by the physiological state of the cell.
Selvakumar
Ponniah
P
Department of Pathology, College of Medicine and Cancer Research Unit, Health Research Division, SK Cancer Agency, University of Saskatchewan, 20 Campus Drive, Saskatoon, SK S7N 4H4, Canada.
Sharma
Rajendra K
RK
D000217:Acyltransferases / Q000378:metabolism*; D019703:Calcineurin / Q000378:metabolism*; D006801:Humans; D019814:Myristic Acid / Q000378:metabolism; D009369:Neoplasms / Q000201:enzymology / Q000378:metabolism / Q000473:pathology; D010766:Phosphorylation; D011485:Protein Binding; D013379:Substrate Specificity; D019061:src-Family Kinases / Q000378:metabolism*
D019814:Myristic Acid; D000217:Acyltransferases; C050480:glycylpeptide N-tetradecanoyltransferase; C060902:lyn protein-tyrosine kinase; D019061:src-Family Kinases; D019703:Calcineurin