Destrin

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Destrin (actin binding protein)
Chr. 20 p12.1
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Destrin or DSTN (also known as actin depolymerizing factor or ADF) is a protein which in humans is encoded by the DSTN gene.[2][3][4] Destrin is a component protein in microfilaments.

The product of this gene belongs to the

cofilin family. This family of proteins is responsible for enhancing the turnover rate of actin in vivo. This gene encodes the actin depolymerizing protein that severs actin filaments (F-actin) and binds to actin monomers (G-actin). Two transcript variants encoding distinct isoforms have been identified for this gene.[2]

Structure

The tertiary structure of destrin was determined by the use of triple-resonance multidimensional nuclear magnetic resonance,

NMR.[1] The secondary and tertiary structures of destrin are similar to the gelsolin
family which is another actin-regulating protein family.

There are three ordered layers to destrin which is a globular protein. There is a central

α helix along with a shorter one and two shorter helices on the opposite side. The four helices are parallel to the β strands.[1]

Function

In a variety of

eukaryotes, destrin regulates actin in the cytoskeleton. Destrin binds actin and is thought to connect it as gelsolin segment-1 does. Furthermore, the binding of actin by destrin and cofilin is regulated negatively by phosphorylation. Destrin can also sever actin filaments.[1]

References

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.