Fig. 7: Unique phosphorylation sites in brain tissue.

A Bar plot indicating all sites (black) that were detected per tissue, highlighting the sites that are unique in each tissue (blue). B Number of outliers per tissue based on z-score analysis with an absolute z-score cut-off of 2. C Ranked mitochondrial phosphorylation sites in brain based on z-score, highlighting the OPA1 top site. D Protein domain representation of mouse OPA1, including mitochondrial transition signal (MTS), transmembrane domain (TM), GTPase, PH, and GED domain. Red triangles represent sites of proteolytic cleavage generating the long and short proteo-forms of OPA1. Note, that all identified phosphosites are common to all OPA1 isoforms. Below, details of GTPase and PH domain with indicated phosphorylation sites (pS/Y) found in brain tissue (See Supplementary Fig. 8C for presence of OPA1 phosphorylation sites in other tissues). E Sequence alignment of first GTP-binding site/P-loop among mouse OPA1 isoforms and homologs in human and yeast, as well as related dynamin family members, DNM1L, MFN1, and MFN2, in mouse. Conserved residues are marked with *, including serine 298 in mouse OPA1. F Structure modeling of human OPA1 GTPase domain [263-580] based on RCSB PDB structure 6JTG⁷⁴. Left, Modeling of the entire domain with highlighted GTP-binding domains (G1-5) in blue and bound GDP (yellow). Right, Detail (i.) of the G1/P-loop domain containing the discussed S298 (magenta) and the nucleotide-binding G300 (red). K+ (yellow) stabilizes the vicinity of the nucleotide. Source Data are provided as a Source Data file.