Mass spectrometry analysis of proteome changes in VPS35-WT vs VPS35[D620N] MEFs and VPS35[D620N] MEFs vs LRRK2 inhibitor in whole cell lysates and lysosomes

By Pui Yiu (Yuko) Lam, PhD and Matthew Taylor, PhD
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Output Details

Description
Primary mass spectrometry data associated with Fig.1 and Fig.2 in the manuscript "Parkinson’s VPS35[D620N] mutation induces LRRK2 mediated lysosomal association of RILPL1 and TMEM55B" (Phospho-Rab and RILPL1 enrichment at VPS35[D620N] mutant lysosome and Lysosomal recruitment of RILPL1 is dependent on LRRK2 kinase activity). Curtain links for the datasets: https://curtain.proteo.info/#/0e673d58-d8f2-4368-996b- 0869d5513d46; https://curtain.proteo.info/#/0e673d58-d8f2-4368-996b-0869d5513d46; https://curtain.proteo.info/#/d864df78-e2a5-4a64-99fb-8c5d8b2e1ab8; https://curtain.proteo.info/#/062e0a64-1fd3-4cc1-833a-a5b007d95a3c.
Tags
  • LRRK2 pathway
  • Lysosomes
  • Mass spectrometry
  • Mouse
  • VPS35
Team
Team Alessi
Program
Collaborative Research Network
Theme
PD Functional Genomics

Meet the Authors

  • Pui Yiu (Yuko) Lam, PhD

    Key Personnel: Team Alessi, 

    University of Dundee

  • Matthew Taylor, PhD

    Key Personnel: Team Alessi, 

    University of Dundee

Related Research

Primary data associated with the manuscript “Genome wide screen reveals Rab12 GTPase as a critical activator of pathogenic LRRK2 kinase” (doi: 10.1101/2023.02.17.529028)

Primary data associated with the manuscript "Genome wide screen reveals Rab12 GTPase as a critical activator of pathogenic LRRK2 kinase"

View Dataset

Primary data associated with the manuscript “Parkinson’s VPS35[D620N] mutation induces LRRK2 mediated lysosomal association of RILPL1 and TMEM55B” (doi: 10.1101/2023.06.07.544051)

Confocal microscopy images, CellProfiler Excel files of Pearson's coefficients between TMEM55B/RILPL1 or pRab10/RILPL1 in R1441C MEF or VPS35[D620N] MEF cells as seen in doi: 10.1101/2023.06.07.544051.

View Dataset

Localization of PPM1H phosphatase tunes Parkinson’s disease-linked LRRK2 kinase-mediated Rab GTPase phosphorylation and ciliogenesis

The data support a model in which localization drives PPM1H substrate selection and centriolar PPM1H is critical for regulation of Rab GTPase-regulated ciliogenesis.

View Article
View More Outputs
Aligning Science Across Parkinson's
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