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N-Myristoylation as a Novel Molecular Target for the Design of Chemotherapeutic Drugs
Published in Robert I. Glazer, Developments in Cancer Chemotherapy, 2019
Ronald L. Felsted, Colin Goddard, Constance J. Glover
Another possibility for interfering with the overall myristoylation-dependent phenomenon is to block the cytoplasmic translocation of myristoylated proteins. As previously described, shortly after synthesis on free ribosomes, the myristoylated p60src kinase forms a soluble complex with p50 and p90 (see Section III.D). Since similar complexes have been reported for oncogene kinases encoded by other retroviruses, interference with such a complex-mediated translocation could be an effective means to block or reverse oncogene kinasemediated transformations.
Guanosine Triphosphate-Binding Proteins
Published in Enrique Pimentel, Handbook of Growth Factors, 2017
G proteins can undergo different types of posttranslational modifications. The amino-terminal portion of the α subunit of some G proteins may be myristoylated, i.e., they may contain covalently amide-linked myristic acid.34 Myristate may play an important role in stabilizing interactions of G proteins with phospholipid or with plasma membrane-bound proteins. Myristoylation may be essential for some α subunits (αi and α0) to become membrane-bound as well as for high affinity interaction with the βγ complex. G protein γ subunits undergo a series of posttranslational modifications at their carboxy terminus, including isoprenylation (addition of a farnesyl or geranylgeranyl moiety). The activated insulin receptor kinase may induce phosphorylation of the α subunit of Gi and G0 proteins.35 The c-Src kinase is associated with G proteins in vivo and may be involved with the phosphorylation of the α subunit of these proteins, which could result in enhanced function of the G proteins.36 However, the precise physiological significance of G protein phosphorylation is not clear at present.
The role of N-myristoyltransferase 1 in tumour development
Published in Annals of Medicine, 2023
Hong Wang, Xin Xu, Jiayi Wang, Yongxia Qiao
Myristoylation is the irreversible covalent bonding of myristic acid (also known as tetradecanoic acid, a 14-carbon saturated fatty acid) to the N-terminal glycine of a protein with myristoyl coenzyme A as the donor [8]. Recent studies have revealed that lysines can also be myristoylated [9]. In eukaryotes, myristoylation occurs in 0.5–3% of the cellular proteome [10]. Although myristoylation affects only a minority of eukaryotic proteins, it is vital for the survival and development of organisms and has implications for various diseases such as cancer [6] and malaria [11]. Myristoylation controls protein function by targeting proteins to specific locations, promoting specific protein–protein and protein–lipid interactions, and causing ligand-induced conformational changes [12]. Familiar myristoylated proteins include the β subunit of calmodulin independent protein phosphatase, the myristoylated alanine-rich C kinase substrate, the α subunit of several G proteins, and several ARF proteins involved in ADP ribosylation [13,14].
Role of co- and post-translational modifications of SFKs in their kinase activation
Published in Journal of Drug Targeting, 2020
Mei-Lian Cai, Meng-Yan Wang, Cong-Hui Zhang, Jun-Xia Wang, Hong Liu, Hong-Wei He, Wu-Li Zhao, Gui-Ming Xia, Rong-Guang Shao
During myristoylation, a myristoyl group (derived from myristic acid) is added to the N-terminal glycine 2 (Gly2) residue of SFKs, and N-myristoyltransferase (NMT) catalyses this reaction [31]. For SFKs, myristoylation play a critical role in membrane anchor and subsequent functional performance. All SFKs are co-translationally myristoylated at Gly2 within the SH4 domain [32].