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Global profiling of protein lipidation using chemical proteomic technologies.

Tate EW, Kalesh KA, Lanyon-Hogg T, Storck EM, Thinon E - Curr Opin Chem Biol (2014)

Bottom Line: Protein lipidation is unique amongst post-translational modifications (PTMs) in enabling direct interaction with cell membranes, and is found in every form of life.Lipidation is important in normal function and in disease, but its intricate interplay with disease context presents a challenging for drug development.This chemical proteomic technology has opened up the first quantitative whole-proteome studies of the known major classes of protein lipidation, and the first insights into their full scope in vivo.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK. Electronic address: e.tate@imperial.ac.uk.

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Structures and known scope of the major forms of protein lipidation. Each type of lipidation is involved in important disease pathways in addition to basal cellular function and development, and all types can be profiled in cells using the common technology platform outlined in Figure 1, for the discovery and elucidation of substrate scope and function.
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fig0010: Structures and known scope of the major forms of protein lipidation. Each type of lipidation is involved in important disease pathways in addition to basal cellular function and development, and all types can be profiled in cells using the common technology platform outlined in Figure 1, for the discovery and elucidation of substrate scope and function.

Mentions: The context of human infection recently provided the first example of reversal of N-terminal N-myristoylation; in this study, enzymatic treatment of YnMyr-tagged cell lysates revealed that the N-myristoylglycine moiety can be hydrolyzed by a secreted bacterial effector protein with cysteine protease activity, the Shigella virulence factor IpaJ [14•]. This process is itself irreversible since the N-terminal glycine is also cleaved from the protein, and allows Shigella to exploit host trafficking pathways during bacterial infection. In the future, IpaJ may also prove a useful and complementary tool for analysis of N-acylation, although its substrate scope has yet to be determined in cells (Figure 2).


Global profiling of protein lipidation using chemical proteomic technologies.

Tate EW, Kalesh KA, Lanyon-Hogg T, Storck EM, Thinon E - Curr Opin Chem Biol (2014)

Structures and known scope of the major forms of protein lipidation. Each type of lipidation is involved in important disease pathways in addition to basal cellular function and development, and all types can be profiled in cells using the common technology platform outlined in Figure 1, for the discovery and elucidation of substrate scope and function.
© Copyright Policy - CC BY
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4319709&req=5

fig0010: Structures and known scope of the major forms of protein lipidation. Each type of lipidation is involved in important disease pathways in addition to basal cellular function and development, and all types can be profiled in cells using the common technology platform outlined in Figure 1, for the discovery and elucidation of substrate scope and function.
Mentions: The context of human infection recently provided the first example of reversal of N-terminal N-myristoylation; in this study, enzymatic treatment of YnMyr-tagged cell lysates revealed that the N-myristoylglycine moiety can be hydrolyzed by a secreted bacterial effector protein with cysteine protease activity, the Shigella virulence factor IpaJ [14•]. This process is itself irreversible since the N-terminal glycine is also cleaved from the protein, and allows Shigella to exploit host trafficking pathways during bacterial infection. In the future, IpaJ may also prove a useful and complementary tool for analysis of N-acylation, although its substrate scope has yet to be determined in cells (Figure 2).

Bottom Line: Protein lipidation is unique amongst post-translational modifications (PTMs) in enabling direct interaction with cell membranes, and is found in every form of life.Lipidation is important in normal function and in disease, but its intricate interplay with disease context presents a challenging for drug development.This chemical proteomic technology has opened up the first quantitative whole-proteome studies of the known major classes of protein lipidation, and the first insights into their full scope in vivo.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK. Electronic address: e.tate@imperial.ac.uk.

Show MeSH