P. Lis

Tagless LysoIP method for molecular profiling of lysosomal content in clinical samples

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.

Interaction with C21ORF2 controls the cellular functions of the NEK1 kinase

This study identifies C21ORF2 as a regulatory subunit of NEK1, showing that their interaction is critical for NEK1 function and that mutations disrupt this interaction, linking it to disease.

Endogenous Rab38 regulates LRRK2's membrane recruitment and substrate Rab phosphorylation in melanocytes

This study identifies Rab38 as a physiological regulator of LRRK2 function in melanocytes, showing it enhances LRRK2 membrane recruitment and substrate phosphorylation.

A Feed-forward Pathway Drives LRRK2 kinase Membrane Recruitment and Activation

This study identifies two distinct binding sites on LRRK2 that mediate its membrane recruitment and activation through Rab GTPase interactions, revealing a feed-forward pathway for kinase activity regulation.

Structural basis for the specificity of PPM1H phosphatase for Rab GTPases

This paper identifies the structural basis for PPM1H phosphatase specificity for Rab GTPases, showing that a flap domain enables recognition of phosphorylated substrates.

Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms

This study identifies distinct Rab proteins phosphorylated by LRRK1 and LRRK2, showing they are regulated by different mechanisms and respond differently to inhibitors.

PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins

This study identifies PPM1H as a phosphatase that counteracts LRRK2 signaling by dephosphorylating Rab proteins, suggesting it as a potential therapeutic target for Parkinson's disease.