Levels of Drp1 phosphorylation were determined in mitochondrial fractions by immunoblotting using anti‐phosphorylated‐S616‐Drp1 or anti‐phosphorylated‐S637‐Drp1 antibodies in hSOD1‐WT‐ and hSOD1‐G93A‐expressing NSC‐34 differentiated cells under serum starvation in the presence or absence of P110 (1 μM/24 h); β‐actin was used as a loading control. Protein levels were quantified and presented as fold change of hSOD1‐WT.