Miura et al. used a mixed-mode CNX-1351 Turing pattern to explain the Doublefoot mutant mouse limb, Turing models of the development of Arabidopsis trichomes on the leaf blade were recently tested against a suite of mutants and transgenic lines. Mathematical models have also been compared with mutants to explain the multi-cellular arrangement of Arabidopsis root hair and non hair cells. PD is a neurodegenerative disease characterized by tremor, rigidity, akinesia, and postural instability that affects of the population over the age of 65. The economic impact ranges from 13 to 29 billion dollars annually in the US alone. All current treatments for PD act by suppressing disease symptoms; none slow or prevent the underlying neurodegenerative process. Incomplete understanding of the molecular mechanisms that mediate neurodegeneration in PD has limited the development of neuroprotective drugs. Mutations in a growing list of genes have been linked to the pathogenesis of PD, providing valuable clues into the pathogenic mechanisms of the disease. LRRK2 is one of these, and multiple aspects of LRRK2 biology have combined to create considerable interest in this protein. First, LRRK2 mutations are the most common genetic cause of PD. LRRK2 mutations account for approximately 5% of familial and 2% of sporadic PD. Second, most patients with LRRK2 mutations exhibit clinical and pathological features that are indistinguishable from idiopathic PD. Finally, the well-defined catalytic domains present in LRRK2 render functional assays on this molecule tractable, and suggest that it may be amenable to therapeutic targeting. LRRK2 isa complex 286 kDa protein that contains multiple wellrecognized domains, including : LRR, Ras of complex, carboxyl-terminus of ROC, kinase and WD40 domains. Multiple studies have focused on the functions of the ROC and kinase domains. LRRK2 isolated from murine brain possesses Isoliquiritigenin GTPase activity, but this activity is considerably lower when LRRK2 is isolated from other tissues. GTP binding stimulates LRRK2 kinase activity, potentially linking the ROC domain to the activity of the kinase domain.