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.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s10974-005-9009-6 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Direct effects of Ca/calmodulin on actin filament formation.
Biochem Biophys Res Commun
November 2018
Institute of Biochemistry I, Jena University Hospital, Friedrich Schiller University Jena, 07743, Jena, Germany. Electronic address:
Actin filament formation plays a pivotal role in the development, regeneration and modulation of the morphologies and physiological functions of subcellular compartments and entire cells. All of these processes require tight temporal and spatial control of F-actin assembly. Recent work has shed new light on the control of actin filament formation by Ca as very fast, transient messenger allowing for defined responses to signal intensities spanning several orders of magnitude.
View Article and Find Full Text PDFAvian synaptopodin 2 (fesselin) stabilizes myosin filaments and actomyosin in the presence of ATP.
Biochemistry
October 2013
Department of Biochemistry and Molecular Biology, Brody School of Medicine at East Carolina University, 600 Moye Boulevard, Greenville, North Carolina 27834-4300, United States.
Smooth muscle cells maintain filaments of actin and myosin in the presence of ATP, although dephosphorylated myosin filaments and actin-myosin interactions are unstable under those conditions in vitro. Several proteins that stabilize myosin filaments and that stabilize actin-myosin interactions have been identified. Fesselin or synaptopodin 2 appears to be another such protein.
View Article and Find Full Text PDFOrganization of F-actin by Fesselin (avian smooth muscle synaptopodin 2).
Biochemistry
July 2013
Institute of Vegetative Physiology, University of Cologne, Robert Koch Strasse 39, D-50931 Cologne, Germany.
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.
View Article and Find Full Text PDFLocalization of the actin-binding protein fesselin in chicken smooth muscle.
Histochem Cell Biol
February 2009
Department of Anatomy and Cell Biology, Brody School of Medicine at East Carolina University, Greenville, NC, USA.
This report compares cellular localization of fesselin in chicken smooth, skeletal and cardiac muscle tissues using affinity purified polyclonal fesselin antibodies. Western blot analyses revealed large amounts of fesselin in gizzard smooth muscle with lower amounts in skeletal and cardiac muscle. In gizzard, fesselin was detected by immunofluorescence as discrete cytoplasmic structures.
View Article and Find Full Text PDFIn vitro characterization of native mammalian smooth-muscle protein synaptopodin 2.
Biosci Rep
August 2008
Department of Biochemistry and Molecular Biology, Brody School of Medicine at East Carolina University, Greenville, NC 27834, USA.
An analysis of the primary structure of the actin-binding protein fesselin revealed it to be the avian homologue of mammalian synaptopodin 2 [Schroeter, Beall, Heid, and Chalovich (2008) Biochem. Biophys. Res.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!