ArticleThe Journal of biological chemistry2008
Smooth muscle myosin phosphorylated at single head shows sustained mechanical activity.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Effects of EMD57033, an activator of actomyosin ATPase activity, on the relaxation process of cell membrane-permeabilized carotid artery and taenia cecum from guinea pigs.Journal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi · 2025Article
- Role of local angiotensin II signaling in bladder function.American journal of physiology. Renal physiology · 2024Review
- Molecular-level evidence of force maintenance by smooth muscle myosin during LC20 dephosphorylation.The Journal of general physiology · 2022Article
- Bioenergetics underlying single-cell migration on aligned nanofiber scaffolds.American journal of physiology. Cell physiology · 2020Article
- Mechanisms of Vascular Smooth Muscle Contraction and the Basis for Pharmacologic Treatment of Smooth Muscle Disorders.Pharmacological reviews · 2016Review
- The role of actin filament dynamics in the myogenic response of cerebral resistance arteries.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2013Review
- Modeling smooth muscle myosin's two heads: long-lived enzymatic roles and phosphorylation-dependent equilibria.Biophysical journal · 2010Article
- Mechanism of catch force: tethering of thick and thin filaments by twitchin.Journal of biomedicine & biotechnology · 2010Article
- Smooth muscle heavy meromyosin phosphorylated on one of its two heads supports force and motion.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Smooth muscle contraction is regulated by the phosphorylation of myosin. It is well known that tonic smooth muscles can maintain force with low energy consumption (latch state); however, the molecular mechanism underlying this phenomenon is unresolved. Here we show that single-head phosphorylated smooth myosin (SHPMII) exhibits fast ( approximately 24 s(-1)) and slow prolonged ( approximately 1 s(-1)) actin interactions, whereas double-head phosphorylated myosin (DHPMII) predominantly exhibits the fast ( approximately 29 s(-1)) interaction, suggesting that the phosphorylated head of SHPMII is mechanically as active as that of DHPMII. Both the fast and the slow actin interactions of SHPMII support the positive net mechanical displacement of actin. The actin translocating velocity of SHPMII was much slower than that of DHPMII, which is consistent with the slow actin interaction of SHPMII. We propose that the "latch state" can be explained by the motor characteristics of SHPMII that is present during the sustained phase of contraction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.