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Modulation of Rab GTPase function by a protein phosphocholine transferase

Author

Listed:
  • Shaeri Mukherjee

    (Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, Yale University, 295 Congress Avenue, New Haven, Connecticut, CT-06536, USA)

  • Xiaoyun Liu

    (Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, Yale University, 295 Congress Avenue, New Haven, Connecticut, CT-06536, USA)

  • Kohei Arasaki

    (Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, Yale University, 295 Congress Avenue, New Haven, Connecticut, CT-06536, USA)

  • Justin McDonough

    (Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, Yale University, 295 Congress Avenue, New Haven, Connecticut, CT-06536, USA)

  • Jorge E. Galán

    (Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, Yale University, 295 Congress Avenue, New Haven, Connecticut, CT-06536, USA)

  • Craig R. Roy

    (Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, Yale University, 295 Congress Avenue, New Haven, Connecticut, CT-06536, USA)

Abstract

Novel role for phosphocholination The pathogen that causes legionnaires' disease, Legionella pneumophila, secretes proteins into host cells that target Rab GTPases involved in vesicular trafficking, thereby enhancing intracellular replication. It is now shown that the L. pneumophila effector protein AnkX modifies Rab1 through a novel protein modification — phosphocholination.

Suggested Citation

  • Shaeri Mukherjee & Xiaoyun Liu & Kohei Arasaki & Justin McDonough & Jorge E. Galán & Craig R. Roy, 2011. "Modulation of Rab GTPase function by a protein phosphocholine transferase," Nature, Nature, vol. 477(7362), pages 103-106, September.
    • Handle: RePEc:nat:nature:v:477:y:2011:i:7362:d:10.1038_nature10335
    DOI: 10.1038/nature10335
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    Cited by:

    1. Dandan Wang & Lingfang Zhu & Xiangkai Zhen & Daoyan Yang & Changfu Li & Yating Chen & Huannan Wang & Yichen Qu & Xiaozhen Liu & Yanling Yin & Huawei Gu & Lei Xu & Chuanxing Wan & Yao Wang & Songying O, 2022. "A secreted effector with a dual role as a toxin and as a transcriptional factor," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Jinli Ge & Ying Wang & Xueyu Li & Qian Lu & Hangqian Yu & Hongtao Liu & Kelong Ma & Xuming Deng & Zhao-Qing Luo & Xiaoyun Liu & Jiazhang Qiu, 2024. "Phosphorylation of caspases by a bacterial kinase inhibits host programmed cell death," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Marietta S. Kaspers & Vivian Pogenberg & Christian Pett & Stefan Ernst & Felix Ecker & Philipp Ochtrop & Michael Groll & Christian Hedberg & Aymelt Itzen, 2023. "Dephosphocholination by Legionella effector Lem3 functions through remodelling of the switch II region of Rab1b," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    4. Tobias Sahr & Pedro Escoll & Christophe Rusniok & Sheryl Bui & Gérard Pehau-Arnaudet & Gregory Lavieu & Carmen Buchrieser, 2022. "Translocated Legionella pneumophila small RNAs mimic eukaryotic microRNAs targeting the host immune response," Nature Communications, Nature, vol. 13(1), pages 1-18, December.

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