Identification of peptides interfering with the PP2Ac And LRRK2 interaction
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.
Authors
- Pierre Tufféry (ORCID: https://orcid.org/0000-0003-1033-9895)
- Samuel Murail (ORCID: https://orcid.org/0000-0002-3842-5333)
- Angelita Rebollo (ORCID: https://orcid.org/0000-0002-1293-9686)
Institutions
- Centre National de la Recherche Scientifique (FR)
- Inserm (FR)
- Université Paris Cité (FR)
- Unit of Functional and Adaptive Biology (FR)
- Unité de Technologies Chimiques et Biologiques pour la Santé (FR)
Publication Details
- Journal
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Published
- 2026-04-15
- DOI
- https://doi.org/10.1016/j.bbapap.2026.141145
- Primary Topic
- Protein Kinase Regulation and GTPase Signaling
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Institut National de la Santé et de la Recherche Médicale