Abstract：
:Lipids are indispensable cellular building blocks, and their post-translational attachment to proteins makes them important regulators of many biological processes. Dysfunction of protein lipidation is also implicated in many pathological states, yet its systematic analysis presents significant challenges. Thanks to innovations in chemical proteomics, lipidation can now be readily studied by metabolic tagging using functionalized lipid analogs, enabling global profiling of lipidated substrates using mass spectrometry. This has spearheaded the first deconvolution of their full scope in a range of contexts, from cells to pathogens and multicellular organisms. Protein N-myristoylation, S-acylation, and S-prenylation are the most well-studied lipid post-translational modifications because of their extensive contribution to the regulation of diverse cellular processes. In this review, we focus on recent advances in the study of these post-translational modifications, with an emphasis on how novel mass spectrometry methods have elucidated their roles in fundamental biological processes.
journal_name
Curr Opin Chem Bioljournal_title
Current opinion in chemical biologyauthors
Losada de la Lastra A,Hassan S,Tate EWdoi
10.1016/j.cbpa.2020.10.002subject
Has Abstractpub_date
2020-11-19 00:00:00pages
97-112eissn
1367-5931issn
1879-0402pii
S1367-5931(20)30133-2journal_volume
60pub_type
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