SAD-1 kinase controls presynaptic phase separation by relieving SYD-2/Liprin-α autoinhibition
Fig 3
SAD-1 kinase phosphoproteomics reveal direct phosphorylation of SYD-2.
(A) In vivo SAD-1 phosphoproteomics experiment to identify possible substrates. Protein names for the top 10 phosphopeptides identified are shown. See S1 Table for complete data. (B) In vitro kinase assay between SAD-1 and SYD-2’s C-terminal SAM domains. SAD-1 is activated by the LKB-1 kinase complex. (C) Alphafold 2 model of SYD-2’s SAM domains, residues 863–1139. Potential phosphosites identified from the phosphoproteomics in (A) and in vitro kinase assay in (B) are shown. Candidate phosphosites are organized into groups based on location for follow-up testing. See also S4A Fig and S1 and S2 Tables. (D) In vitro kinase assay between SAD-1 and SYD-2 phosphomutants. SAD-1 is activated by the LKB-1 kinase complex.