Smooth muscle α-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization

Minh Pham; Joseph M. Chalovich

doi:10.1007/s10974-005-9053-2

Journal of Muscle Research & Cell Motility

February 2006, 27:45

Smooth muscle α-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization

Authors
Authors and affiliations

Minh Pham
Joseph M. ChalovichEmail author

Article

First Online:: 01 February 2006

Received:: 04 August 2005
Accepted:: 09 December 2005

DOI: 10.1007/s10974-005-9053-2

Cite this article as:: Pham, M. & Chalovich, J.M. J Muscle Res Cell Motil (2006) 27: 45. doi:10.1007/s10974-005-9053-2

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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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Minh Pham
- 1
Joseph M. Chalovich
- 1
Email author

1.Brody School of Medicine at East Carolina UniversityGreenvilleUSA

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Smooth muscle α-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization

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