Activation of alpha-actinin's vinculin binding site by mechanical stimuli

Mohammad Jafarnejad & Samira Jamalian

Sharif University of Technology, Mechanical Engineering, Tehran, Iran

α-actinin is one of the cytoskeletal proteins which is found in cell-cell and cell-matrix contacts. α-actinin is an anti parallel dimmer. Each of its monomers consists of 2 domains: Head domain and rod domain. The binding site for several cytoskeletal proteins is known to be in the α-actinin rod domain. Vinculin is one of focal adhesion proteins, its binding site which is known as αVBS is known to be hidden in the central rod domain helical bundles of α-actinin. Previous experiments suggest that activation of Vinculin by α-actinin happens due to some structural changes, the initiation of these changes is the unraveling of αVBS from its buried location in R4 spectrin repeat. In this study mechanical stimuli is applied to activate vinculin binding site of alpha-actinin using molecular dynamics method. Our future plans is to observe vinculin activation in the presence of α-actinin. Finally dynamics of vinculin á-actinin interaction can be investigated.

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