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Publication

SIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation.

Xiaoyu Zhang | Nicole A Spiegelman | Ornella D Nelson | Hui Jing | Hening Lin

eLife | 2017

The Ras family of GTPases are important in cell signaling and frequently mutated in human tumors. Understanding their regulation is thus important for studying biology and human diseases. Here, we report that a novel posttranslational mechanism, reversible lysine fatty acylation, regulates R-Ras2, a member of the Ras family. SIRT6, a sirtuin with established tumor suppressor function, regulates the lysine fatty acylation of R-Ras2. In mouse embryonic fibroblasts (MEFs), Sirt6 knockout (KO) increased R-Ras2 lysine fatty acylation. Lysine fatty acylation promotes the plasma membrane localization of R-Ras2 and its interaction with phosphatidylinositol 3-kinase PI3K, leading to activated Akt and increased cell proliferation. Our study establishes lysine fatty acylation as a previously unknown mechanism that regulates the Ras family of GTPases and provides an important mechanism by which SIRT6 functions as a tumor suppressor.

Pubmed ID: 28406396 RIS Download

Research resources used in this publication

HEK293T (RRID:CVCL_0063) (cell line)

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Associated grants

Agency: NIDDK NIH HHS, United States
Id: R01 DK107868
Agency: NIGMS NIH HHS, United States
Id: R01 GM098596
Agency: NIH HHS, United States
Id: S10 OD018516
Agency: NIGMS NIH HHS, United States
Id: T32 GM008500
Agency: Howard Hughes Medical Institute, United States

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ATCC (tool)

RRID:SCR_001672

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QIAGEN (tool)

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A commercial organization which provides assay technologies to isolate DNA, RNA, and proteins from any biological sample. Assay technologies are then used to make specific target biomolecules, such as the DNA of a specific virus, visible for subsequent analysis.

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