Table 2.

Summary of Kv1.3 phosphorylation residues and physiological relevance. As shown, only two serine/threonine kinases have been reported to phosphorylate specific amino acids of the channel. Kv1.3 is phosphorylated in diverse tyrosine residues with different outcomes depending on the kinase. PKC: Protein Kinase C, ERK1/2: Extracellular signal-Related Kinases, v-Src: viral sarcoma, EGFR: Epidermal Growth Factor Receptor, PDGFR: Platelet-Derived Growth Factor Receptor, IRK: Insulin Receptor Kinase, TrkB: Tropomyosin Receptor Kinase B.

Serine/Threonine Kinases
Kinase/Trigger	Residues	Outcome
PKC [23]	Ser 342	Modulation of Kv1.3 ion conductivity
ERK1/2 [59,70]	Ser 461 Thr 495	Kv1.3-induced cell proliferation EGF-dependent Kv1.3 endocytosis
Tyrosine Kinases
Kinase/Trigger	Residues	Outcome
v-Src [66]	Tyr 111-113 Tyr 137 Tyr 449 Tyr 479	Current suppression and fast deactivation (Tyr 137, Tyr 449) Slow C-type inactivation (more than 3 Tyr)
EGFR [80]	Tyr 479	Decreased peak current independent of inactivation
PDGFR-ERK1/2 [70]	Tyr 449	Kv1.3 induced mitochondrial respiration and cell proliferation
IRK [67]	Tyr 111-113 Tyr 137 Tyr 479	Insulin-mediated current suppression
TrkB [93]	Tyr 111-113 Tyr 137 Tyr449	BDNF-induced current decrease (Tyr 111-113, Tyr 137, Tyr 449) Modulation of BDNF-dependent inactivation (Tyr 137)
Pervanadate [67]	Tyr 111-113 Tyr 449	Pervanadate-dependent current suppression