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[Function of protein myristoylation in cellular regulation and viral proliferation]
Abstract:
Protein myristoylation was first discovered in the catalytic subunit of adenosine 3',5'-cyclic monophosphate-dependent protein kinase. Subsequently, various cellular and viral myristoylated proteins were detected. In each case, the myristoyl moiety was found in an amide linkage with the amino terminal glycine residue of the modified proteins. The biological functions of protein myristoylation of various cellular protein, oncogene product, and viral structural proteins have been studied by many biochemists. Two of the most thoroughly studies myristoylated proteins are the transforming protein of Rous sarcoma virus, pp60v-src, and the proto-oncogene product, pp60c-src. Deletion, modification of the first 14 NH2-terminal amino acid of pp60v-src, or chemical antimyristoylation of the protein with N-myristoyl glycinal diethylacetal does not affect intrinsic tyrosine src-kinase activity, but prevents myristoylation and membrane association, and abolishes the transforming activity of the protein. Protein myristoylations of some viral structural proteins were also studied by many investigators, and X-ray crystallographic studies of poliovirus suggest that myristate moiety may play a central role in capsid assembly. Recently, human immunodeficiency virus, HIV-I, process a myristoylated p17gag protein, which is proteolytically derived from the NH2-terminus of a gag precursor protein, and its myristate moiety may be important for virus assembly. In this review, we detailed recent studies of the protein myristoylation in cellular regulation and virus proliferation.
Insights
Protein myristoylation, the attachment of fatty acids, is crucial for cellular regulation and virus proliferation. This process affects protein function, membrane association, and viral assembly, as seen in studies of src-kinases and HIV.
Area of Science:
- Biochemistry
- Molecular Biology
- Virology
Background:
- Protein myristoylation involves attaching a myristoyl group to proteins via an amide linkage to the N-terminal glycine.
- This modification is observed in various cellular, oncogenic, and viral proteins, including pp60v-src and HIV p17gag.
Purpose of the Study:
- To review recent studies on the biological functions of protein myristoylation.
- To highlight the role of myristoylation in cellular regulation and virus proliferation.
Main Methods:
- Analysis of existing biochemical and structural studies on myristoylated proteins.
- Review of experimental data on src-kinases and viral proteins like poliovirus and HIV.
Main Results:
- Myristoylation is essential for membrane association and transforming activity of pp60v-src, though not its intrinsic kinase activity.
- Myristoylation of viral proteins like poliovirus capsid and HIV p17gag appears critical for assembly and proliferation.
Conclusions:
- Protein myristoylation plays a significant role in diverse biological processes, including cell signaling and viral replication.
- Further research into myristoylation mechanisms can offer insights into disease pathogenesis and therapeutic strategies.