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Cited by 315

The DOI matches its Crossref record; 72 of the 72 references it cites were found in a registry or an index.

Invited Review: Regulation of myosin phosphorylation in smooth muscle

Pfitzer, Gabriele·2001·Journal of Applied Physiology

Abstract

Phosphorylation of the regulatory light chains of myosin II (rMLC) by the Ca 2+/calmodulin-dependent myosin light-chain kinase (MLCK) and dephosphorylation by a type 1 phosphatase (MLCP), which is targeted to myosin by a regulatory subunit (MYPT1), are the predominant mechanisms of regulation of smooth muscle tone. The activities of both enzymes are modulated by several protein kinases. MLCK is inhibited by the Ca 2+/calmodulin-dependent protein kinase II, whereas the activity of MLCP is increased by cGMP and perhaps also cAMP-dependent protein kinases. In either case, this results in a decrease in the Ca 2+sensitivity of rMLC phosphorylation and force production. The activity of MLCP is inhibited by Rho-associated kinase, one of the effectors of the monomeric GTPase Rho, and protein kinase C, leading to an increase in Ca 2+sensitivity. Hence, smooth muscle tone appears to be regulated by a network of activating and inactivating intracellular signaling cascades.

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Crossref · 10.1152/jappl.2001.91.1.497

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Metadata

Authors
Pfitzer, G.
Venue
Journal of Applied Physiology
Published
2001-07-01
Volume
91
Issue
1
Pages
497-503
ISSN
  • 0161-7567 (ISSN-L)
  • 8750-7587
  • 1522-1601
OpenAlex
W1831347542
Cited by
315
References
72
FWCI
7.06
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Invited Review: Regulation of myosin phosphorylation in smooth muscle. https://app.cochat.ai/papers/10.1152/jappl.2001.91.1.497
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Pfitzer, G. (2001). Invited Review: Regulation of myosin phosphorylation in smooth muscle. Journal of Applied Physiology. https://doi.org/10.1152/jappl.2001.91.1.497

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.