1 Rac 1 Rescues Neurite Retraction Caused by G 2019 S Leucine - Rich Repeat Kinase 2 ( Lrrk 2 )

Promoting Self - association and Cellular Leucine - rich Repeat Kinase 2 ( LRRK 2 ) , Phosphorylation and 14 - 3 - 3 Binding of Arsenite Stress Down - regulates

Human leucine-rich repeat kinase 1 and 2: intersecting or unrelated functions?

Mutations in LRRK2 (leucine-rich repeat kinase 2) are associated with both familial and sporadic PD (Parkinson's disease). LRRK1 (leucine-rich repeat kinase 1) shares a similar domain structure with LRRK2, but it is not linked to PD. LRRK proteins belong to a gene family known as ROCO, which codes for large proteins with several domains. All ROCO proteins have a ROC (Ras of complex proteins) GT...

Lrrk regulates the dynamic profile of dendritic Golgi outposts through the golgin Lava lamp

Constructing the dendritic arbor of neurons requires dynamic movements of Golgi outposts (GOPs), the prominent component in the dendritic secretory pathway. GOPs move toward dendritic ends (anterograde) or cell bodies (retrograde), whereas most of them remain stationary. Here, we show that Leucine-rich repeat kinase (Lrrk), the Drosophila melanogaster homologue of Parkinson's disease-associated...

Multiplying Messages LRRK beneath Parkinson Disease

Parkinson Disease (PD) is a progressive neurodegenerative disorder with limited therapeutic options. In this issue of Cell, Martin et al. link PD protein leucine-rich repeat kinase 2 (LRRK2) to abnormalities of translational control, a pathogenic mechanism implicated in an increasing number of CNS neurodegenerative diseases, as well as in normal aging.

A QUICK Screen for Lrrk2 Interaction Partners – Leucine-rich Repeat Kinase 2 is Involved in Actin Cytoskeleton Dynamics*□S

Mutations in human leucine-rich repeat kinase 2 (Lrrk2), a protein of yet unknown function, are linked to Parkinson’s disease caused by degeneration of midbrain dopaminergic neurons. The protein comprises several domains including a GTPase and a kinase domain both affected by several pathogenic mutations. To elucidate the molecular interaction network of endogenous Lrrk2 under stoichiometric co...