Regulation of Neurotransmitter Release by Protein Phosphorylation. Table 1.
Identified protein kinase substrates involved in exocytosis and the kinases that phosphorylate them
| Protein | In vitro phosphorylation sites | In vivo phosphorylation sites | Functional significance tested? |
|---|---|---|---|
| CSP | PKA: S10 | S10 | Yes |
| Munc18-1 | PKC: S306, S313 Cdk5: T574 | S313 | Yes |
| Rabphilin 3A | PKA and PKC: S234, S274 | S234, S274 | No |
| Rim 1 | PKA: S413, S1548 CaMKII: S241, S287 (indirect) | S413 | Yes |
| SNAP-25 | PKA: T138 PKC: S187 | T138 S187 | Yes |
| Synapsin | PKA and CaMKI: S9 | As for in vitro | Yes |
| CaMKII: S566, S603 | |||
| ERK1: S62 | |||
| ERK2: S67 | |||
| MAPK and Cdk5: S549 | |||
| Cdk5: S551 | |||
| Synaptotagmin I | PKC and CaMKII: T112 | T112 | No |
| Syntaxin 1A | CK2 and ROCK: S14 DAPK: S188 | S14 | Yes |
Key synaptic proteins are listed that have been shown to be phosphorylated in vitro and whose phosphorylation sites have been identified. Only those proteins that have been confirmed through genetic approaches to be required for, or to regulate neurotransmitter release, are included.