Paweł Lis

The paper identifies a splice variant-dependent localization of PMCA2 to lysosomes and links it to neurodegenerative diseases.

This study identifies NRBP1 as an upstream activator of the WNK pathway by forming a multi-subunit complex with WNK1, SPAK, and TSC22D4 in response to osmotic stress.

This study shows LRRK2 and PINK1 function in parallel neuroprotective pathways affecting ciliogenesis in Parkinson's disease, suggesting shared therapeutic targets.

The paper develops a tagless LysoIP method to isolate lysosomes from clinical samples and human cell lines, revealing glycerophosphodiesters as potential biomarkers for lysosomal storage disorders.

This study shows that the VPS35[D620N] mutation causes lysosomal dysfunction, activates LRRK2, and promotes the lysosomal association of RILPL1 and TMEM55B through phosphorylation of Rab proteins.

The paper develops and validates a multiplexed mass spectrometry assay to quantify LRRK2-phosphorylated Rab proteins and biomarker sites, showing VPS35[D620N] enhances Rab1 phosphorylation in Parkinson's disease.

This study shows that Rab29 does not regulate basal or nigericin/monensin-induced LRRK2 pathway activity in mice.