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Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
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Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells

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Lysine fatty acylation promotes lysosomal targeting of TNF-α

Hong Jiang1, Xiaoyu Zhang1, Hening Lin1,2

  • 1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.

Scientific Reports
|April 16, 2016
PubMed

Tumor necrosis factor-α (TNF-α) is a proinflammation cytokine secreted by various cells. Understanding its secretive pathway is important to understand the biological functions of TNF-α and diseases associated with TNF-α. TNF-α is one of the first proteins known be modified by lysine fatty acylation (e.g. myristoylation). We previously demonstrated that SIRT6, a member of the mammalian sirtuin family of enzymes, can remove the fatty acyl modification on TNF-α and promote its secretion. However, the mechanistic details about how lysine fatty acylation regulates TNF-α secretion have been unknown. Here we present experimental data supporting that lysine fatty acylation promotes lysosomal targeting of TNF-α. The result is an important first step toward understanding the biological functions of lysine fatty acylation.

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