Data From: Astrocytic LRRK2 Controls Synaptic Connectivity via Regulation of ERM phosphorylation

Tabular raw data corresponding to figure sets used in the study. Phospho-ERM Antibody Validation: We confirmed the specificity of the phospho-ERM antibody by treating brain sections from both mice and human samples with lambda protein phosphatase (λ-PPase), which dephosphorylates proteins. In both cases, the phospho-ERM signal was eliminated after λ-PPase treatment, confirming the specificity of phospho-ERM antibodies in mouse and human samples. Cell-type specificity of pERM staining in mouse and human brains: We assessed ERM hyperphosphorylation for cell-type-specific by co-staining phospho-ERM with cellular markers. In LRRK2 G2019Ski/ki mice, phospho-ERM was significantly increased in ACC and MOp L1 and L2/3, colocalizing with S100β (astrocytes) and MAP2 (neurons) but not Iba1 (microglia), with predominant astrocytic localization. PD patients with the LRRK2 G2019S mutation showed elevated phospho-ERM colocalized with S100β and MAP2 in the frontal cortices.