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 α-actinin. Binding was measured by blot overlay, affinity chromatography and sedimentation methods. Binding was moderate with an association constant of 1–4×107 M−1 assuming a 1:1 association of fesselin with α-actinin. Fesselin binds to the central spectrin domain repeat region of α-actinin but not to the CH1–CH2 domain. Fesselin accelerates the polymerization of actin. This activity of fesselin was attenuated by α-actinin. These observations support the role of fesselin in organizing the cytoskeleton.
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Acknowledgements
The authors thank Dr. Roberto Dominguez for his gift of the CH1–CH2 domain of α-actinin and Ms. Natalie Lonergan and Ms. Tamatha Baxley for technical assistance. This work was supported by grant AR35216 from the National Institutes of Health to JMC.
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Pham, M., Chalovich, J.M. Smooth muscle α-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization. J Muscle Res Cell Motil 27, 45–51 (2006). https://doi.org/10.1007/s10974-005-9053-2
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DOI: https://doi.org/10.1007/s10974-005-9053-2