ArticleJournal of muscle research and cell motility2005
Fesselin binds to actin and myosin and inhibits actin-activated ATPase activity.
Article in Journal of muscle research and cell motility, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Caldesmon ablation in mice causes umbilical herniation and alters contractility of fetal urinary bladder smooth muscle.The Journal of general physiology · 2021Article
- Various Themes of Myosin Regulation.Journal of molecular biology · 2016Review
- UNC-87 isoforms, Caenorhabditis elegans calponin-related proteins, interact with both actin and myosin and regulate actomyosin contractility.Molecular biology of the cell · 2015Article
- Avian synaptopodin 2 (fesselin) stabilizes myosin filaments and actomyosin in the presence of ATP.Biochemistry · 2013Article
- Synaptopodin family of natively unfolded, actin binding proteins: physical properties and potential biological functions.Biophysical reviews · 2010Review
- Phosphorylation of caldesmon at sites between residues 627 and 642 attenuates inhibitory activity and contributes to a reduction in Ca2+-calmodulin affinity.Biophysical journal · 2010Article
- Localization of the actin-binding protein fesselin in chicken smooth muscle.Histochemistry and cell biology · 2009Article
- In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2.Bioscience reports · 2008Article
- The actin binding protein, fesselin, is a member of the synaptopodin family.Biochemical and biophysical research communications · 2008Article
- Smooth muscle alpha-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization.Journal of muscle research and cell motility · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Fesselin is an actin binding protein that bundles actin filaments and accelerates nucleation of actin polymerization. The effect of fesselin on actin polymerization is regulated by Ca(++)-calmodulin. Because actin filaments serve both structural and contractile functions we also examined the effect of fesselin on activation of myosin S1 ATPase activity. Fesselin inhibited the activation of S1-catalyzed ATP hydrolysis in a similar manner in both the presence and absence of tropomyosin. This inhibition was unaffected by Ca(++)-calmodulin. Fesselin inhibited the binding of myosin-S1 to actin during steady-state ATP hydrolysis. Fesselin also displaced caldesmon from actin. S1 displaced fesselin from actin in the absence of nucleotide when the affinity of S1 for actin was much greater than the affinity of fesselin for actin. It is likely that fesselin and S1 share common binding sites on F-actin. We also observed that fesselin could bind to smooth muscle myosin with muM affinity. Fesselin shares some similarities to caldesmon in binding to several other proteins and having multiple potential functions.
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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.