Table 1.
In vivo site | Increased phosphorylation | Outcome | Decreased phosphorylation | Outcome |
---|---|---|---|---|
PKC domain | PKC activators | ↓DA uptake Vmax(g,h,l,n) | PKC inhibitors | ↑DA uptake Vmax(b,l,m) |
AMPH, METH | ↑DA efflux Vmax(e,i,j) | Δ21/22 truncation | ↓PKC-induced down-regulation(f,n) | |
PP1 inhibitors | ↑PKC-induced down-regulation(f) | Palmitoylation enhancers | ↓AMPH-induced efflux(h,i,m) | |
Palmitoylation inhibitors | ↑CFT affinity(k) | Botulinum neurotoxin C | ↓AMPH-induced down-regulation(a) | |
Ser7 | PKC activators | ↓DA uptake Vmax(l) | S7A mutation | ↑DA uptake Vmax(l) |
C580A mutation | ↓Cys580 palmitoylation(l) | ↓AMPH-induced efflux(j,n,o,p) | ||
Palmitoylation inhibitors | ↑CFT affinity(l) | ↓PKC-induced down-regulation(f) | ||
↑Cys580 palmitoylation(l) | ||||
↓CFT affinity(l) | ||||
Thr53 | PIN1 inhibitors | ↑DA efflux(d) | T53A mutation | ↓DA uptake Vmax(c,f) |
PKC activators | ↓AMPH-induced MPP+ efflux(f) | |||
AMPH, METH | ↑AMPH-induced DA efflux(c) | |||
PP1/2A inhibitors | ↓CFT affinity(c) |
Superscripts denote references for studies that link the indicated outcomes to one or more of the conditions that increase or decrease phosphorylation of specified sites:
Granas et al., 1995