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Updated: Aug 13, 2026

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
Published on: June 3, 2021
Smooth muscle alpha-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization
Minh Pham1, Joseph M Chalovich
1Brody School of Medicine at East Carolina University, 600 Moye Blvd., Greenville, NC 27834, USA.
Abstract:
Fesselin is an actin binding protein from smooth muscle that nucleates actin polymerization in a Ca(++)-calmodulin dependent manner, bundles actin and inhibits the actin-activated ATPase activity of myosin S1. We now report that fesselin binds to smooth muscle alpha-actinin. Binding was measured by blot overlay, affinity chromatography and sedimentation methods. Binding was moderate with an association constant of 1-4 x 10(7) M(-1) assuming a 1:1 association of fesselin with alpha-actinin. Fesselin binds to the central spectrin domain repeat region of alpha-actinin but not to the CH1-CH2 domain. Fesselin accelerates the polymerization of actin. This activity of fesselin was attenuated by alpha-actinin. These observations support the role of fesselin in organizing the cytoskeleton.
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