Table 2.
Post-translational modifications to polyanionic C-terminal domains of αSyn and tubulin.
| PTM | CT residues affected |
Effect on residue charge |
Increase in residue volume |
References | Predicted effects |
|---|---|---|---|---|---|
| α-Synuclein | |||||
| Phosphorylation | 125, 129, 133, 136 | −2 | 54 Å3 | 41 | Higher translocation probability, longer dwell time at low voltages |
| Nitration | 125, 133, 136 | 0 | 53 Å3 | Molecular volume from MW and density of NO2 liquid | Minimal |
| Ubiquitination/Sumoylation | 96 / 96, 102 | 0 / −5 (does not affect CTT properties) | 11130 Å3 / 14890 Å3 | 42 | Eliminates translocation, behaves like tubulin |
| Dopamination | 125-129 | 0 | 150 Å3 | 33, 42 | Smaller capture rate, longer dwell time at low voltages |
| Tubulin | |||||
| Polyglutamylation (N residues) | varies by isotype | −(N + 1) | N × 155 Å3 | 42 | Longer dwell time, stronger dependence on voltage |
| Polyglycylation (N residues) | varies by isotype | −1 | N × 66 Å3 | 42 | Longer dwell time, same voltage dependence |