The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Regulation of Myosin Phosphatase by a Specific Interaction with cGMP- Dependent Protein Kinase Iα
Abstract
Contraction and relaxation of smooth muscle are regulated by myosin light-chain kinase and myosin phosphatase through phosphorylation and dephosphorylation of myosin light chains. Cyclic guanosine monophosphate (cGMP)–dependent protein kinase Iα (cGKIα) mediates physiologic relaxation of vascular smooth muscle in response to nitric oxide and cGMP. It is shown here that cGKIα is targeted to the smooth muscle cell contractile apparatus by a leucine zipper interaction with the myosin-binding subunit (MBS) of myosin phosphatase. Uncoupling of the cGKIα-MBS interaction prevents cGMP-dependent dephosphorylation of myosin light chain, demonstrating that this interaction is essential to the regulation of vascular smooth muscle cell tone.
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Cited by
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Nitric oxide signalling in cardiovascular health and disease
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Metadata
- Authors
- Surks, H. K., Mochizuki, N., Kasai, Y., Georgescu, S. P., Tang, K. M., Ito, M., Lincoln, T. M., & Mendelsohn, M. E.
- Venue
- Science
- Published
- 1999-11-19
- Volume
- 286
- Issue
- 5444
- Pages
- 1583-1587
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2085220858
- Cited by
- 527
- References
- 48
- FWCI
- 7.83
- Type
- journal article
- Language
- en
- Open access
- closed
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- Surks, H. K., Mochizuki, N., Kasai, Y., Georgescu, S. P., Tang, K. M., Ito, M., Lincoln, T. M., & Mendelsohn, M. E. (1999). Regulation of Myosin Phosphatase by a Specific Interaction with cGMP- Dependent Protein Kinase Iα. Science. https://doi.org/10.1126/science.286.5444.1583
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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