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. 2019 Dec 28;18:232. doi: 10.1186/s12944-019-1181-6

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© The Author(s). 2019

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 1 — ABHD5 protein structure and function. Schematic representation of ABHD5 protein (a). The ABHD5 protein is characterized by two functional domains: a LD-binding site (hydrophobic domain) and an α/βhydrolase domain that includes two amino acid residues involved in ATGL and perilipin interaction (Q130 and E260). ABHD5 as coactivator of PNPLA1 and ATGL (b). During the formation of the skin barrier (keratinocytes), ABHD5 activates PNPLA1 determining the production of ὠ–O-acylceramide. In liver, muscle and many other tissues (including skin), ABHD5 acts as ATGL coactivator, inducing TAG hydrolysis