Destrin

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.

Destrin (actin binding protein)
Nuclear magnetic resonance determined configuration of the tertiary structure of Destrin.[1]
Identifiers
Symbol	DSTN
Alt. symbols	ADF
NCBI gene	11034
HGNC	15750
OMIM	609114
RefSeq	NM_006870
UniProt	P60981
Other data
Locus	Chr. 20 p12.1
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The product of this gene belongs to the actin-binding proteins ADF (Actin-Depolymerizing Factor)/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, or NMR for short.^[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 β sheet that is composed of one parallel strand and three antiparallel strands. This β sheet is between a long 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]