Extended Data Fig. 6: Proteomic comparison of SVs from WT and mocha mice.
a, Diagram of SV purification. After velocity sedimentation in glycerol, fractions 5-9 (pink) were collected, sedimented and analyzed by LC-MS/MS. b, Enrichment of SV proteins. Equal amounts of protein (0.5 µg) from the different stages of SV purification (H, homogenate; P1, tissue debris, nuclei, and large myelin fragments; P2, synaptosomes; LP1, synaptic plasma membrane and associated organelles; LS2, synaptosomal cytoplasm; LP2, synaptic vesicles) were analyzed by immunoblotting. Representative blots were from three independent experiments. c, Fractionation of synaptic vesicles (LP2) by glycerol velocity sedimentation showing the migration of VAMP7, VGLUT2 and synaptophysin. Representative blots were from three independent experiments. d, Fold enrichment of proteins in mocha SVs relative to WT. e, Quantitative western analysis of SV proteins in WT and mocha mice. Scatterplots show the fraction relative to WT. P = 4.24 × 10−5, VAMP7; 0.04, Syt1, 0.0019, VGLUT1; 8.05 × 10−6, ZnT-3; 3.24 × 10−3, ATP8A1; 0.0052, Scamp1 (n = 3 independent experiments). The data indicate mean ±  s.e.m. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001 by unpaired two-tailed t-test.
