Protein knase C-mediated phosphorylation of Kvβ2 in adult rat brain

Xintao Wang, Jie Zhang, Stan M. Berkowski, Heather Knowleg, A. B. Chandramouly, Martha Downens, Michael B. Prystowsky

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


The phosphorylation of Kvβ2 was investigated by different protein kinases. Protein kinase A catalytic subunit (PKA-CS) yielded the greatest phosphorylation of recombinant Kvβ2 (rKvβ2), with limited phosphorylation by protein kinase C catalytic subunit (PKC-CS) and no detectable phosphorylation by casein kinase II (CKII). Protein kinase(s) from adult rat brain lysate phosphorylated both rKvβ2 and endogenous Kvβ. The PKA inhibitor, PKI 6-22, fully inhibited PKA-mediated phophorylation of rKvβ2 yet showed minimal inhibition of kinase activity present in rat brain. The inhibitor Gö 6983, that blocks PKCα, PKCβ, PKCγ, PKCδ and PKCζ activities, inhibited rKvβ2 phosphorylation by rat brain kinases, with no inhibition by Gö 6976 which blocks PKCα and PKCβI activities. Dose-response analysis of Gö 6983 inhibitory activity indicates that at least two PKC isozymes account for the kinase activity present in rat brain. hus, while PKA was the most active protein kinase to phosphorylate rKvβ2 in vitro, Kvβ2 phosphorylation in the rat brain is mainly mediated by PKC isozymes.

Original languageEnglish (US)
Pages (from-to)1879-1886
Number of pages8
JournalNeurochemical Research
Issue number10
StatePublished - Oct 2004


  • KVβ
  • protein kinase inhibitor
  • protein kinase(s)
  • voltage-gated potassium (Kv)channel

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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