» Articles » PMID: 29794032

Sequence Analysis and Structure Prediction of ABHD16A and the Roles of the ABHD Family Members in Human Disease

Overview
Journal Open Biol
Date 2018 May 26
PMID 29794032
Citations 16
Authors
Affiliations
Soon will be listed here.
Abstract

Abhydrolase domain containing 16A (ABHD16A) is a member of the α/β hydrolase domain-containing (ABHD) protein family and is expressed in a variety of animal cells. Studies have shown that ABHD16A has acylglycerol lipase and phosphatidylserine lipase activities. Its gene location in the main histocompatibility complex (MHC) III gene cluster suggests that this protein may participate in the immunomodulation of the body. The results of studies investigating nearly 20 species of ABHDs reveal that the ABHD proteins are key factors in metabolic regulation and disease occurrence and development. In this paper, we summarize the related progress regarding the function of ABHD16A and other ABHD proteins. A prediction of the active sites and structural domains of ABHD16A and an analysis of the amino acid sites are included. Moreover, we analysed the amino acid sequences of the ABHD16A molecules in different species and provide an overview of the related functions and diseases associated with these proteins. The functions and diseases related to ABHD are systematically summarized and highlighted. Future research directions for studies investigating the functions and mechanisms of these proteins are also suggested. Further studies investigating the function of ABHD proteins may further confirm their positions as important determinants of lipid metabolism and related diseases.

Citing Articles

An S-acylated N-terminus and a conserved loop regulate the activity of the ABHD17 deacylase.

Holme S, Sapia J, Davey M, Vanni S, Conibear E J Cell Biol. 2025; 224(4).

PMID: 39951021 PMC: 11827582. DOI: 10.1083/jcb.202405042.


Pooled PPIseq: Screening the SARS-CoV-2 and human interface with a scalable multiplexed protein-protein interaction assay platform.

Miller D, Dziulko A, Levy S PLoS One. 2025; 20(1):e0299440.

PMID: 39823405 PMC: 11741623. DOI: 10.1371/journal.pone.0299440.


Swine RNF5 positively regulates the antiviral activity of IFITM1 by mediating the degradation of ABHD16A.

Shi X, Shen L, Chen S, Liu M, Wang J, Wen X J Virol. 2024; 99(1):e0127724.

PMID: 39601593 PMC: 11784460. DOI: 10.1128/jvi.01277-24.


ABHD5 as a friend or an enemy in cancer biology?.

Cai J, Cheng H, Xu S Front Oncol. 2024; 14:1447509.

PMID: 39328203 PMC: 11424376. DOI: 10.3389/fonc.2024.1447509.


Mechanisms and functions of protein S-acylation.

S Mesquita F, Abrami L, Linder M, Bamji S, Dickinson B, van der Goot F Nat Rev Mol Cell Biol. 2024; 25(6):488-509.

PMID: 38355760 DOI: 10.1038/s41580-024-00700-8.


References
1.
Thomas G, Brown A, Brown J . In vivo metabolite profiling as a means to identify uncharacterized lipase function: recent success stories within the alpha beta hydrolase domain (ABHD) enzyme family. Biochim Biophys Acta. 2014; 1841(8):1097-101. PMC: 4069229. DOI: 10.1016/j.bbalip.2014.01.004. View

2.
Clifford R, Zhang J, Meerzaman D, Lyu M, Hu Y, Cultraro C . Genetic variations at loci involved in the immune response are risk factors for hepatocellular carcinoma. Hepatology. 2010; 52(6):2034-43. PMC: 8259333. DOI: 10.1002/hep.23943. View

3.
Lass A, Zimmermann R, Haemmerle G, Riederer M, Schoiswohl G, Schweiger M . Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome. Cell Metab. 2006; 3(5):309-19. DOI: 10.1016/j.cmet.2006.03.005. View

4.
Kohman R, Rodriguez-Zas S, Southey B, Kelley K, Dantzer R, Rhodes J . Voluntary wheel running reverses age-induced changes in hippocampal gene expression. PLoS One. 2011; 6(8):e22654. PMC: 3152565. DOI: 10.1371/journal.pone.0022654. View

5.
Tomczyk N, Nettleship J, Baxter R, Crichton H, Webster S, Campopiano D . Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway. FEBS Lett. 2002; 513(2-3):299-304. DOI: 10.1016/s0014-5793(02)02342-6. View