TY - JOUR
T1 - Phosphorylation of Rho-associated kinase (Rho-kinase/ROCK/ROK) substrates by protein kinases A and C
AU - Kang, Jeong Hun
AU - Jiang, Yuhua
AU - Toita, Riki
AU - Oishi, Jun
AU - Kawamura, Kenji
AU - Han, Aishan
AU - Mori, Takeshi
AU - Niidome, Takuro
AU - Ishida, Masami
AU - Tatematsu, Kenji
AU - Tanizawa, Katsuyuki
AU - Katayama, Yoshiki
N1 - Funding Information:
This work was supported by CREST, Japan Science and Technology Corporation, a grant-in-aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture in Japan, and a grant-in-aid for Scientific Research from the Ministry of Health, Labour and Welfare.
PY - 2007/1
Y1 - 2007/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.biochi.2006.08.003
DO - 10.1016/j.biochi.2006.08.003
M3 - Article
C2 - 16996192
AN - SCOPUS:33845647984
SN - 0300-9084
VL - 89
SP - 39
EP - 47
JO - Biochimie
JF - Biochimie
IS - 1
ER -