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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Related Experiment Video

Updated: Feb 14, 2026

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

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LRRK2 mediated Rab8a phosphorylation promotes lipid storage.

Miao Yu1, Muhammad Arshad2, Wenmin Wang1

  • 1MOE Key Laboratory of Bioinformatics and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, 100084, China.

Lipids in Health and Disease
|February 28, 2018
PubMed
Summary

Mutant LRRK2 phosphorylates Rab8a, promoting larger lipid droplets and potentially linking Parkinson's disease to altered lipid metabolism. This phosphorylation impacts Rab8a's interaction with Optineurin.

Keywords:
LRRK2Lipid dropletsLipid storageParkinson’s diseaseRab8a

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Assaying the Kinase Activity of LRRK2 in vitro
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Assaying the Kinase Activity of LRRK2 in vitro

Published on: January 18, 2012

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroscience

Background:

  • Mutations in leucine-rich repeat kinase 2 (LRRK2) are linked to Parkinson's disease (PD) pathogenesis.
  • Increased LRRK2 kinase activity is significantly associated with PD.
  • Rab GTPases, like Rab8, are LRRK2 substrates phosphorylated in their switch II domain.

Purpose of the Study:

  • To investigate the effects of Rab8 phosphorylation and its mutants on lipid metabolism.
  • To determine the impact of Rab8 phosphorylation on lipid droplet growth.

Main Methods:

  • Phosphorylation status of Rab8a assessed using phos-tag gel.
  • Point mutant constructs of Rab8a generated for functional analysis.
  • 3T3L1 cells transfected, lipid droplets stained with Bodipy, and sizes analyzed via fluorescent microscopy.

Main Results:

  • Mutated LRRK2 with high kinase activity phosphorylates Rab8a.
  • Phosphorylation of Rab8a at T72 residue enhances lipid droplet formation and size (average diameter increased from 2.10 μm to 2.46 μm).
  • Phosphorylation of Rab8a reduces its interaction with Optineurin.

Conclusions:

  • Y1699C mutated LRRK2 phosphorylates Rab8a, with T72 phosphorylation crucial for lipid droplet fusion and enlargement.
  • The study suggests an indirect link between increased lipid storage and Parkinson's disease pathogenesis.