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

Article

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

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.

Copyright information

© Springer Science+Business Media, Inc. 2006

Authors and Affiliations

  1. 1.Brody School of Medicine at East Carolina UniversityGreenvilleUSA