Tandem Mass Tag (TMT) label-based mass spectrometry analysis of RILPL1 interactors

By Raja Sekhar Nirujogi, PhD and Prosenjit Pal, PhD
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Output Details

Description
Primary mass spectrometry data associated with Fig.5 in the manuscript "Parkinson’s VPS35[D620N] mutation induces LRRK2 mediated lysosomal association of RILPL1 and TMEM55B" (Association of RILPL1 with a lysosomal membrane integral protein, TMEM55B mediated by LRRK2 activity). Curtain link for the dataset: https://curtain.proteo.info/#/4f15d6c8-9192-4bb2-a2ff-da7aa542025c
Tags
  • LRRK2 pathway
  • Mass spectrometry
Team
Team Alessi
Program
Collaborative Research Network
Theme
PD Functional Genomics

Meet the Authors

  • Raja Sekhar Nirujogi, PhD

    Key Personnel: Team Alessi, 

    University of Dundee

  • Prosenjit Pal, PhD

    Key Personnel: Team Alessi, 

    University of Dundee

Related Research

Parkinson’s VPS35[D620N] mutation induces LRRK2-mediated lysosomal association of RILPL1 and TMEM55B

This study uncovers a pathway through which dysfunctional lysosomes resulting from the VPS35[D620N] mutation recruit and activate LRRK2 on the lysosomal surface, driving assembly of the RILPL1-TMEM55B complex.

View Article

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"

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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.

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