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@article{Losada:2021:10.1016/j.cbpa.2020.10.002,
author = {Losada, de la Lastra A and Hassan, S and Tate, EW},
doi = {10.1016/j.cbpa.2020.10.002},
journal = {Current Opinion in Chemical Biology},
pages = {97--112},
title = {Deconvoluting the biology and druggability of protein lipidation using chemical proteomics},
url = {http://dx.doi.org/10.1016/j.cbpa.2020.10.002},
volume = {60},
year = {2021}
}
TY - JOUR
AB - 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.
AU - Losada,de la Lastra A
AU - Hassan,S
AU - Tate,EW
DO - 10.1016/j.cbpa.2020.10.002
EP - 112
PY - 2021///
SN - 1367-5931
SP - 97
TI - Deconvoluting the biology and druggability of protein lipidation using chemical proteomics
T2 - Current Opinion in Chemical Biology
UR - http://dx.doi.org/10.1016/j.cbpa.2020.10.002
UR - https://www.ncbi.nlm.nih.gov/pubmed/33221680
UR - http://hdl.handle.net/10044/1/87142
VL - 60
ER -
Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ
e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821