PPM1H protein phosphatase dephosphorylates Rab proteins modulating LRRK2 signalling.

The dynein light intermediate chain is a member of the G protein superfamily and links the motor to several intracellular cargo adaptors.

Discovery of a physiological LRRK2 substrate and a new mechanism of Rab regulation should aid Parkinson’s research and the understanding of Rab function.

A human three-helix Rab-binding domain can potentially bind to two Rab proteins simultaneously with different affinities at binding sites generated by gene duplication.

Parkinson’s disease-associated LRRK2 kinase is recruited to membranes by its Rab GTPase substrates, and LRRK2 is both retained on membranes and further activated there by cooperative interaction with the phosphorylated Rab proteins that it generates.

Analysis of multiple guanine exchange factors shows that Rab activation can occur via a number of mechanistically distinct GDP-release pathways.

Rab6A binds directly to both the C-terminus and the N-terminal motor domain of the kinesin KIF1C to regulate vesicle motility and Golgi organization.

Reconstitution of the endosomal Rab cascade reveals that Rab5 binds and activates the Mon1-Ccz1 guanine nucleotide exchange factor, which in turn recruits Rab7 to membranes to drive fusion.

Parkinson's kinase LRRK2 phosphorylates a distinct subset of Rabs, and LRRK2-dependent phosphorylation links LRKK2 to ciliogenesis.

Two GAP proteins bound to mitochondria regulate the enyzme Rab7, and thereby the expansion of the isolation membrane during mitophagy, downstream of PINK1 and Parkin, two proteins that are mutated in familial Parkinson's disease.