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

Output Details

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

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