ApoL6 associates with lipid droplets and disrupts Perilipin1-HSL interaction to inhibit lipolysis

Yuhui Wang, Hai P. Nguyen, Pengya Xue, Ying Xie, Danielle Yi, Frances Lin, Jennie Dinh, Jose A. Viscarra, Nnejiuwa U. Ibe, Robin E. Duncan and Hei S. Sul ()
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Yuhui Wang: University of California, Berkeley
Hai P. Nguyen: University of California, Berkeley
Pengya Xue: University of California, Berkeley
Ying Xie: University of California, Berkeley
Danielle Yi: University of California, Berkeley
Frances Lin: University of California, Berkeley
Jennie Dinh: University of California, Berkeley
Jose A. Viscarra: University of California, Berkeley
Nnejiuwa U. Ibe: University of California, Berkeley
Robin E. Duncan: University of California, Berkeley
Hei S. Sul: University of California, Berkeley

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract Adipose tissue stores triacylglycerol (TAG) in lipid droplets (LD) and release fatty acids upon lipolysis during energy shortage. We identify ApoL6 as a LD-associated protein mainly found in adipose tissue, specifically in adipocytes. ApoL6 expression is low during fasting but induced upon feeding. ApoL6 knockdown results in smaller LD with lower TAG content in adipocytes, while ApoL6 overexpression causes larger LD with higher TAG content. We show that the ApoL6 affects adipocytes through inhibition of lipolysis. While ApoL6, Perilipin 1 (Plin1), and HSL can form a complex on LD, C-terminal ApoL6 directly interacts with N-terminal Plin1 to prevent Plin1 binding to HSL, to inhibit lipolysis. Thus, ApoL6 ablation decreases white adipose tissue mass, protecting mice from diet-induced obesity, while ApoL6 overexpression in adipose brings obesity and insulin resistance, making ApoL6 a potential future target against obesity and diabetes.

Date: 2024
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DOI: 10.1038/s41467-023-44559-3

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