Deform the membrane, cAPTure the lipid

Jennifer Greaves

doi:10.1038/s41589-021-00754-1

Deform the membrane, cAPTure the lipid

Research output: Contribution to journal › Article › peer-review

Abstract

Acyl protein thioesterases are critical regulators of S-acylation, removing acyl chains from dynamically S-acylated proteins. A cytosolic deacylase, APT2, is S-acylated by zDHHC3 and zDHHC7 and is predicted to deform the lipid bilayer to extract acyl chains, capturing them within a hydrophobic pocket.

Original language	English
Pages (from-to)	371-372
Number of pages	2
Journal	Nature Chemical Biology
Volume	17
Early online date	11 Mar 2021
DOIs	https://doi.org/10.1038/s41589-021-00754-1
Publication status	Published - Apr 2021

Keywords

Membrane Lipids

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10.1038/s41589-021-00754-1

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title = "Deform the membrane, cAPTure the lipid",

abstract = "Acyl protein thioesterases are critical regulators of S-acylation, removing acyl chains from dynamically S-acylated proteins. A cytosolic deacylase, APT2, is S-acylated by zDHHC3 and zDHHC7 and is predicted to deform the lipid bilayer to extract acyl chains, capturing them within a hydrophobic pocket.",

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author = "Jennifer Greaves",

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AB - Acyl protein thioesterases are critical regulators of S-acylation, removing acyl chains from dynamically S-acylated proteins. A cytosolic deacylase, APT2, is S-acylated by zDHHC3 and zDHHC7 and is predicted to deform the lipid bilayer to extract acyl chains, capturing them within a hydrophobic pocket.

KW - Membrane Lipids

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EP - 372

JO - Nature Chemical Biology

JF - Nature Chemical Biology

ER -

Deform the membrane, cAPTure the lipid

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