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Updated: May 30, 2026

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
Published on: December 14, 2017
Modulation of Rab GTPase function by a protein phosphocholine transferase
Shaeri Mukherjee1, Xiaoyun Liu, Kohei Arasaki
1Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, Yale University, New Haven, Connecticut, CT 06536, USA.
Legionella pneumophila modifies host cell GTPases using novel phosphocholination. This bacterial strategy alters host cell functions by targeting Rab GTPases, impacting membrane transport pathways.
Area of Science:
- Microbiology
- Cell Biology
- Biochemistry
Background:
- Intracellular pathogens like Legionella pneumophila manipulate host cell GTPases.
- Legionella proteins, such as DrrA, are known to modify GTPases like Rab1 via AMPylation.
Purpose of the Study:
- To investigate post-translational modifications to Rab1 during Legionella infection using mass spectrometry.
- To identify novel bacterial effector proteins and mechanisms involved in host cell modulation.
Main Methods:
- Mass spectrometry to analyze host cell protein modifications during infection.
- Biochemical assays to characterize protein-protein interactions and enzymatic activities.
- In vitro studies using purified proteins and substrates.
Main Results:
- Confirmed DrrA-mediated AMPylation of Rab1 during Legionella infection.
- Discovered a novel, DrrA-independent modification of Rab1 by the effector protein AnkX.
- AnkX mediates phosphocholination of Rab1 and Rab35 using CDP-choline, requiring its FIC domain.
Conclusions:
- Phosphocholination by bacterial FIC-domain proteins is a mechanism to alter host cell functions.
- AnkX's phosphocholination of Rab GTPases impacts both endocytic and exocytic pathways.
- This study reveals a new strategy employed by Legionella to control host cell transport.
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