Phosphorylation of Rho-associated kinase (Rho-kinase/ROCK/ROK) substrates by protein kinases A and C.
Biochimie
; 89(1): 39-47, 2007 Jan.
Article
em En
| MEDLINE
| ID: mdl-16996192
ABSTRACT
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 (K(m) and k(cat)) showed that two of these peptides could be useful as substrates specific to Rho-kinase phosphorylation.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Proteína Quinase C
/
Proteínas Serina-Treonina Quinases
/
Proteínas Quinases Dependentes de AMP Cíclico
/
Peptídeos e Proteínas de Sinalização Intracelular
Tipo de estudo:
Risk_factors_studies
Idioma:
En
Ano de publicação:
2007
Tipo de documento:
Article