ArticleCirculation research2013
Inhibitor κB kinase 2 is a myosin light chain kinase in vascular smooth muscle.
Article in Circulation research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
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- Elevated uric acid induces erectile dysfunction in rats by interacting with MLCK and inhibiting its ubiquitin-mediated degradation.Communications biology · 2025Article
- p90RSK2, a new MLCK mediates contractility in myosin light chain kinase null smooth muscle.Frontiers in physiology · 2023Article
- Multiscale imaging of basal cell dynamics in the functionally mature mammary gland.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The pathophysiological basis of vascular disease.Laboratory investigation; a journal of technical methods and pathology · 2019Article
- RSK2 contributes to myogenic vasoconstriction of resistance arteries by activating smooth muscle myosin and the NaScience signaling · 2018Article
- Involvement of inhibitor kappa B kinase 2 (IKK2) in the regulation of vascular tone.Laboratory investigation; a journal of technical methods and pathology · 2018Article
- Angiotensin II Signal Transduction: An Update on Mechanisms of Physiology and Pathophysiology.Physiological reviews · 2018Review
- From the Cover: Lung-Specific Overexpression of Constitutively Active IKK2 Induces Pulmonary and Systemic Inflammations but Not Hypothalamic Inflammation and Glucose Intolerance.Toxicological sciences : an official journal of the Society of Toxicology · 2017Article
- Programming of mouse obesity by maternal exposure to concentrated ambient fine particles.Particle and fibre toxicology · 2017Article
- Unique gene program of rat small resistance mesenteric arteries as revealed by deep RNA sequencing.Physiological reports · 2015Article
- Dual regulation of tumor necrosis factor-α on myosin light chain phosphorylation in vascular smooth muscle.American journal of physiology. Heart and circulatory physiology · 2015Article
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9 authors at 1 institution in 1 country.
Funding
Abstract
rationaleMyosin light chain (MLC) phosphorylation determines vascular contractile status. In addition to the classic Ca²⁺-dependent MLC kinase (MLCK), another unidentified kinase(s) also contributes to MLC phosphorylation in living cells. Inhibitor κB kinase 2 (IKK2)-deficient mouse embryonic fibroblasts demonstrate abnormal morphology and migration, suggesting that IKK2 may be involved in MLC phosphorylation.
objectiveTherefore, we tested whether IKK2 is an MLCK in living cells and the role of IKK2 in mediating vasoconstriction and blood pressure regulation. METHODS AND
resultsIn the present study, we showed that recombinant IKK2-phosphorylated MLC and intact myosin in vitro, and the kinetic parameters were comparable with those of the classic MLCK. Overexpression of IKK2 increased cellular MLC phosphorylation level, and pharmacological inhibition of IKK2 markedly decreased vascular smooth muscle cell MLC phosphorylation, suggesting that IKK2 is an MLCK in living cells. IKK2 inhibitors dose- and time-dependently attenuated vasoconstriction elicited by diverse agonists, suggesting the physiological importance of IKK2 as an MLCK. Vascular smooth muscle cell-specific IKK2-deficient mice had decreased aortic contractile responses, and reduced hypertensive responses to several vasoconstrictors, compared with wild-type mice, confirming the physiological importance of IKK2 as an MLCK.
conclusionsOur data provide a novel mechanism whereby IKK2 regulates MLC phosphorylation as an MLCK and, thus, vascular function and blood pressure.
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