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  1. Article ; Online: SIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation.

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

    eLife

    2017  Volume 6

    Abstract: ... 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), ...

    Abstract 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),
    MeSH term(s) Acylation ; Animals ; Fibroblasts/metabolism ; Lysine/metabolism ; Mice ; Mice, Knockout ; Protein Processing, Post-Translational ; Sirtuins/metabolism ; ras Proteins/metabolism
    Chemical Substances Sirt6 protein, mouse (EC 2.4.2.31) ; Sirtuins (EC 3.5.1.-) ; Rras protein, mouse (EC 3.6.1.-) ; ras Proteins (EC 3.6.5.2) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2017-04-13
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.25158
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: SIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation

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

    eLife, Vol

    2017  Volume 6

    Abstract: ... acylation of R-Ras2. In mouse embryonic fibroblasts (MEFs), Sirt6 knockout (KO) increased R-Ras2 lysine ... that a novel posttranslational mechanism, reversible lysine fatty acylation, regulates R-Ras2, a member ... fatty acylation. Lysine fatty acylation promotes the plasma membrane localization of R-Ras2 and ...

    Abstract 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.
    Keywords Ras ; acylation ; sirtuin ; defatty-acylation ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2017-04-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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