Phosphorylation of Rho-associated kinase (Rho-kinase/ROCK/ROK) substrates by protein kinases A and C

Jeong Hun Kang, Yuhua Jiang, Riki Toita, Jun Oishi, Kenji Kawamura, Aishan Han, Takeshi Mori, Takuro Niidome, Masami Ishida, Kenji Tatematsu, Katsuyuki Tanizawa, Yoshiki Katayama

    Research output: Contribution to journalArticlepeer-review

    43 Citations (Scopus)


    Rho-associated kinase (Rho-kinase/ROCK/ROK) is a serine/threonine kinase and plays an important role in various cellular functions. The cAMP-dependent protein kinase (protein kinase A/PKA) and protein kinase C (PKC) are also serine/threonine kinases, and directly and/or indirectly take part in the signal transduction pathways of Rho-kinase. They have similar phosphorylation site motifs, RXXS/T and RXS/T. The purpose of this study was to identify whether sites phosphorylated by Rho-kinase could be targets for PKA and PKC and to find peptide substrates that are specific to Rho-kinase, i.e., with no phosphorylation by PKA and PKC. A total of 18 substrates for Rho-kinase were tested for phosphorylation by PKA and PKC. Twelve of these sites were easily phosphorylated. These results mean that Rho-kinase substrates can be good substrates for PKA and/or PKC. On the other hand, six Rho-kinase substrates showing no or very low phosphorylation efficiency (<20%) for PKA and PKC were identified. Kinetic parameters (Km and kcat) showed that two of these peptides could be useful as substrates specific to Rho-kinase phosphorylation.

    Original languageEnglish
    Pages (from-to)39-47
    Number of pages9
    Issue number1
    Publication statusPublished - Jan 2007

    All Science Journal Classification (ASJC) codes

    • Biochemistry


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