ArticleBiochemistry2013
Organization of F-actin by Fesselin (avian smooth muscle synaptopodin 2).
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
The trial behind it
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Comprehensive Transcriptome Sequencing Analysis ofFrontiers in physiology · 2022Article
- Actin polymerization is stimulated by actin cross-linking protein palladin.The Biochemical journal · 2016Article
- Article
- Identification of cardiac myofilament protein isoforms using multiple mass spectrometry based approaches.Proteomics. Clinical applications · 2014Article
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
Fesselin or avian synaptopodin 2 is a member of the synaptopodin family of actin binding proteins. Fesselin promotes G-actin polymerization and the formation of large actin complexes that can be collected by low-speed centrifugation. Because of the potential role of fesselin in some cancers and its effects on actin, we further investigated the effect of fesselin on actin. Fesselin initiated actin polymerization under a variety of conditions, including the virtual absence of salt. Actin filaments formed at low salt concentrations in the presence of fesselin were similar to filaments polymerized in the presence of 100 mM KCl. In both cases, the filaments were long and straight with a common orientation. Highly ordered actin bundles formed with increasing times of incubation. Blockers of actin growth at the barbed end (cytochalasin D and CapZ) did not prevent fesselin from polymerizing actin. Low concentrations of fesselin increased the critical concentration of actin. Both observations are consistent with preferential growth at the pointed end of actin filaments. These results indicate a role of fesselin in organizing cellular actin. These and other results indicate that fesselin is part of a cellular actin organizing center.
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Registered trials
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