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Updated: Apr 18, 2026
Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
Published on: December 14, 2017
Identification of peptides interfering with the PP2Ac And LRRK2 interaction
Angelita Rebollo1, Samuel Murail2, Pierre Tuffery2
1Unité de Technologies Chimiques et Biologiques pour la Santé, INSERM U1267 - CNRS UMR8258, Université Paris Cité, Faculté de Pharmacie, France.
None:
Using the PEP-scan approach, we have identified the binding site of PP2Ac to LRRK2, a protein associated with Parkinson's disease. We also have identified the binding site of LRRK2 to PP2Ac, referred to as mirror peptide. All isolated fragments are predicted to be solvent-accessible and are compatible with contributing to LRRK2/PP2Ac interaction except for peptide M2. The In vitro competition experiment demonstrated that peptide P3 and M1 effectively compete PP2A/LRRK2 interaction. Both appear to have propensity to adopt helical conformation. These newly generated peptides can be tools to investigate the role of PP2A/LRRK2 interaction under both physiological and pathological conditions.
