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Structural basis for the specificity of PPM1H phosphatase for Rab GTPases

By Kerryn Berndsen, Dario Alessi, PhD, Pawel Lis
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Output Details

Description

Raw immunoblotting data; Scans of Coomassie-stained SDS-PAGE gels; Tabular data for quantifications; List of cross-links with distances; Numerical data for in vitro assays; Data files from Astra Software analysis

Identifier (DOI)
10.5281/zenodo.5045023
Tags
  • LRRK2
  • PPM1H phosphatase
  • Rab GTPases
Discovery Team
Team Alessi
Program
Collaborative Research Network
Theme
PD Functional Genomics

Meet the Authors

  • User avatar fallback logo

    Kerryn Berndsen

    External Collaborator

  • Dario Alessi, PhD

    Lead PI (Core Leadership): Team Alessi, 

    University of Dundee

  • User avatar fallback logo

    Pawel Lis

    External Collaborator

Related Research

Primary data associated with doi: 10.1042/BCJ20220161 (Impact of 100 LRRK2 variants linked to Parkinson’s Disease on kinase activity and microtubule binding)

Raw immunoblotting data; tabular data for quantifications; numerical data for in vitro assays; immunofluorescence images; Prism files for statistical analysis.

View Dataset

Binding of Rab29 to the LRRK2 Armadillo domain by Microscale Thermophoresis

Microscale thermophoresis is a powerful tool to measure the affinities of interactions between proteins. We present here our method for determining the binding of Rab29 GTPase to the LRRK2 N-terminal Armadillo domain.

View Protocol

RAB3 phosphorylation by pathogenic LRRK2 impairs trafficking of synaptic vesicle precursors

Gain-of-function mutations in LRRK2 gene lead to by increasing phosphorylation of RAB GTPases. Over-phosphorylation of RAB3A disrupts synaptic vesicle transport in human neurons, altering synaptic protein distribution and likely contributing to PD.

View Article
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Aligning Science Across Parkinson's
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