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Only the ABD of βI-spectrin affected dendritic spines.
Protein 4.1 promotes the association of the ABD of spectrin with F-actin [67], [68].
The ABD of βI-spectrin also affected the stability of actin filaments within the spine.
Expression of the ABD of other members of spectrin superfamily tagged with DsRed gave different results.
We found that the ABD of cortexillin interacts with the GRD domain of GAPA (Figure 6C).
We therefore tested the role of rac proteins in the morphological changes induced by the ABD of βI-spectrin.
We conclude that stabilization of actin filaments by the ABD of βI-spectrin attenuates the structural dynamics of dendritic spines.
We next asked if there were functional correlates of the morphological changes induced by the ABD of spectrin.
The ABD of α-actinin-2 (cloned78.1) was cloned into the DsRed2-c1 vector similarly, with the primers.
Even more unique to the ABD of βI-spectrin was its ability to enlarge the spine head.
This effect was also specific, as the ABD of α-actinin-2 did not stabilize actin-GFP in spines.
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