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Gene Review:

Abhd5 - abhydrolase domain containing 5

Mus musculus

Synonyms: 1-acylglycerol-3-phosphate O-acyltransferase ABHD5, 1300003D03Rik, 2010002J10Rik, Abhydrolase domain-containing protein 5, CDS, ...

Subramanian, V. et al., Yamaguchi, T. et al., Schweiger, M. et al., Yamaguchi, T. et al.

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High impact information on Abhd5

CGI-58, a recently identified coactivator of ATGL, stimulates TG hydrolase activity in wild-type and HSL-deficient WAT but not in ATGL-deficient WAT, suggesting that ATGL is the sole target for CGI-58-mediated activation of adipose lipolysis [1].
Thus, CGI-58 binds to perilipin A-coated lipid droplets in a manner that is dependent upon the metabolic status of the adipocyte and the activity of cAMP-dependent protein kinase [2].
Furthermore, we identified CGI-58 as a binding partner of ADRP, another PAT domain protein expressed ubiquitously, by yeast two-hybrid assay [3].
Remarkably, activation of cAMP-dependent protein kinase by the incubation of 3T3-L1 adipocytes with isoproterenol and isobutylmethylxanthine disperses CGI-58 from the surfaces of lipid droplets to a cytoplasmic distribution [2].
The localization of endogenous CGI-58 was investigated in 3T3-L1 cells stably expressing mutated forms of perilipin using microscopy [2].

Biological context of Abhd5

This interaction seems physiologically important because CGI-58 mutants carrying an amino acid substitution identical to that found in CDS lost the ability to be recruited to LDs [3].

Anatomical context of Abhd5

We have used proteomic analysis to identify CGI-58, a member of the alpha/beta-hydrolase fold family of enzymes, as a component of lipid droplets of 3T3-L1 adipocytes [2].
Endogenous CGI-58 was distributed predominantly on the surface of LDs in differentiated 3T3-L1 cells, and its expression increased during adipocyte differentiation [3].
CGI-58 mRNA is highly expressed in adipose tissue and testes, tissues that also express perilipins, and at lower levels in liver, skin, kidney, and heart [2].

Physical interactions of Abhd5

Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in 3T3-L1 adipocytes [2].

Other interactions of Abhd5

Immunoprecipitation studies confirmed these findings, but also showed co-precipitation of perilipin B and CGI-58 [2].
We identified CGI-58, a product of the causal gene of Chanarin-Dorfman syndrome (CDS), as an interactor for both perilipin and ADRP [4].

References

Adipose Triglyceride Lipase and Hormone-sensitive Lipase Are the Major Enzymes in Adipose Tissue Triacylglycerol Catabolism. Schweiger, M., Schreiber, R., Haemmerle, G., Lass, A., Fledelius, C., Jacobsen, P., Tornqvist, H., Zechner, R., Zimmermann, R. J. Biol. Chem. (2006) [Pubmed]
Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in 3T3-L1 adipocytes. Subramanian, V., Rothenberg, A., Gomez, C., Cohen, A.W., Garcia, A., Bhattacharyya, S., Shapiro, L., Dolios, G., Wang, R., Lisanti, M.P., Brasaemle, D.L. J. Biol. Chem. (2004) [Pubmed]
CGI-58 interacts with perilipin and is localized to lipid droplets. Possible involvement of CGI-58 mislocalization in Chanarin-Dorfman syndrome. Yamaguchi, T., Omatsu, N., Matsushita, S., Osumi, T. J. Biol. Chem. (2004) [Pubmed]
Analysis of interaction partners for perilipin and ADRP on lipid droplets. Yamaguchi, T., Omatsu, N., Omukae, A., Osumi, T. Mol. Cell. Biochem. (2006) [Pubmed]

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