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Phosphorylation of CPI‐17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho‐kinase
Open accessAbstract
Phosphorylation of CPI‐17 by Rho‐associated kinase (Rho‐kinase) and its effect on myosin phosphatase (MP) activity were investigated. CPI‐17 was phosphorylated by Rho‐kinase to 0.92 mol of P/mol of CPI‐17 in vitro. The inhibitory phosphorylation site was Thr 38 (as reported previously) and was identified using a point mutant of CPI‐17 and a phosphorylation state‐specific antibody. Phosphorylation by Rho‐kinase dramatically increased the inhibitory effect of CPI‐17 on MP activity. Thus, CPI‐17 as a substrate of Rho‐kinase could be involved in the Ca 2+ sensitization of smooth muscle contraction as a downstream effector of Rho‐kinase.
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Citations
Cited by
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Coleman, M. L., Sahai, E. A., Yeo, M., Bosch, M., Dewar, A., & Olson, M. F. (2001) · Nature Cell Biology · doi:10.1038/35070009 · Cited by 1,311
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Amano, M., Nakayama, M., & Kaibuchi, K. (2010) · Cytoskeleton · doi:10.1002/cm.20472 · Cited by 994
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Cohen, P. T. W. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.2.241 · Cited by 912
The Function of Rho-Associated Kinases ROCK1 and ROCK2 in the Pathogenesis of Cardiovascular Disease
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Metadata
- Authors
- Koyama, M., Ito, M., Feng, J., Seko, T., Shiraki, K., Takase, K., Hartshorne, D. J., & Nakano, T.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2000-06-21
- Volume
- 475
- Issue
- 3
- Pages
- 197-200
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2061229883
- Cited by
- 220
- References
- 0
- FWCI
- 6.31
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Koyama, M., Ito, M., Feng, J., Seko, T., Shiraki, K., Takase, K., Hartshorne, D. J., & Nakano, T. (2000). Phosphorylation of CPI‐17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho‐kinase. FEBS Letters. https://doi.org/10.1016/s0014-5793(00)01654-9
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