کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1952368 | 1057205 | 2011 | 14 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Post-translational myristoylation: Fat matters in cellular life and death Post-translational myristoylation: Fat matters in cellular life and death](/preview/png/1952368.png)
Myristoylation corresponds to the irreversible covalent linkage of the 14-carbon saturated fatty acid, myristic acid, to the N-terminal glycine of many eukaryotic and viral proteins. It is catalyzed by N-myristoyltransferase. Typically, the myristate moiety participates in protein subcellular localization by facilitating protein-membrane interactions as well as protein–protein interactions. Myristoylated proteins are crucial components of a wide variety of functions, which include many signalling pathways, oncogenesis or viral replication. Initially, myristoylation was described as a co-translational reaction that occurs after the removal of the initiator methionine residue. However, it is now well established that myristoylation can also occur post-translationally in apoptotic cells. Indeed, during apoptosis hundreds of proteins are cleaved by caspases and in many cases this cleavage exposes an N-terminal glycine within a cryptic myristoylation consensus sequence, which can be myristoylated. The principal objective of this review is to provide an overview on the implication of myristoylation in health and disease with a special emphasis on post-translational myristoylation. In addition, new advancements in the detection and identification of myristoylated proteins are also briefly reviewed.
Research highlights
► Myristoylation in health and disease.
► Post-translational myristoylation in apoptosis.
► Use of chemical biology to improve detection and identification of myristoylated proteins.
Journal: Biochimie - Volume 93, Issue 1, January 2011, Pages 18–31