Disease relevance of DSTN

• Human ADF expressed in Escherichia coli behaves like native ADF from porcine brain [1].
• New information about the biochemical activities of the Salmonella protein SipA suggests that this protein might inhibit host cell actin dynamics by competing with ADF/cofilin and gelsolin, two key proteins that promote the turnover of actin filaments [2].
• Recent evidence suggests these actin surface membrane alterations induced by ischemia are secondary to activation and relocation of the actin-associated protein, actin depolymerizing factor/cofilin, to the apical membrane domain [3].
• Once activated, the diffuse cytoplasmic distribution of the actin depolymerizing factor/cofilin protein relocalizes to the luminal membrane blebs [3].
• Tissues from normal human skin and various skin diseases were studied with the immunoperoxidase technique using an antibody to adult T-cell leukemia-derived factor (ADF), a homologue of human thioredoxin [4].

Psychiatry related information on DSTN

• The Advisory Committee on the Training of Dental Practitioners of the EU (ACTDP) in order to ensure a comparably demanding standard in dental education, recommended in 1986 a self-assessment system, and visitations to dental training establishments [5].

High impact information on DSTN

• Destrin is an isoprotein of cofilin that regulates actin cytoskeleton in various eukaryotes [6].
• In spite of there being no significant amino acid sequence homology, we found that the folding of destrin was strikingly similar to that of repeated segments in the gelsolin family, which resulted in a new protein fold group [6].
• Ubiquitous among eukaryotes, the ADF/cofilins are essential proteins responsible for the high turnover rates of actin filaments in vivo [7].
• Although vertebrate ADF/cofilins contain a nuclear localization sequence, they are usually concentrated in regions containing dynamic actin pools, such as the leading edge of migrating cells and neuronal growth cones [7].
• ADF/cofilins are essential for cytokinesis, phagocytosis, fluid phase endocytosis, and other cellular processes dependent upon actin dynamics [7].

Biological context of DSTN

• ADF uses ATP hydrolysis in actin assembly to enhance filament dynamics [8].
• The clone contains an open reading frame of 139 amino acid residues which shows greater than 40% sequence identity in a 91 amino acid overlap to animal actin-depolymerizing factors (ADF), cofilin and destrin [9].
• Control of actin dynamics in cell motility. Role of ADF/cofilin [10].
• As a test to determine whether such signal-responsive pathways existed in plants, this study addressed the ability of maize ADF to be phosphorylated and the likely effects of such phosphorylation on its capacity to modulate actin dynamics [11].
• In the absence of any crystal structures of ADF or cofilin in complex with actin, these studies provide further information about the binding sites on F-actin for these important actin regulatory proteins [12].

Anatomical context of DSTN

• HeLa cells, transfected with either chick wild-type ADF cDNA or a cDNA mutated to code for Ala in place of Ser24 or Thr25, express and phosphorylate the exogenous ADF [13].
• Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments [1].
• Further analysis revealed that these proteins were the phosphorylated forms of the actin cytoskeleton modulators cofilin-1 and destrin [14].
• Immunostaining of neurites indicates that these rods also contain the majority of the actin filament dynamizing proteins, actin-depolymerizing factor (ADF) and cofilin (AC) [15].
• Colocalization of ADF and cofilin in intranuclear actin rods of cultured muscle cells [16].

Associations of DSTN with chemical compounds

• Cofilin/ADF, beryllium fluoride complex (BeFx), and phalloidin have opposing effects on actin filament structure and dynamics [17].
• Immunofluorescence microscopy revealed that two actin-binding proteins of low molecular weight with different functional activity, ADF and cofilin, are transported into nuclei of cultured myogenic cells to form rod structures there together with actin, when the cells were incubated in medium containing dimethylsulfoxide [16].
• Inorganic phosphate (Pi) and cofilin/actin depolymerizing factor proteins have opposite effects on actin filament structure and dynamics [18].
• Rather, reduced ROCKII expression and attenuated phosphorylation of ADF/cofilin on serine 3 occurred [19].
• When existing information about tropomyosin, myosin, actin-depolymerizing factor, and nebulin is considered, these results suggest that many actin-binding proteins may have multiple binding sites on F-actin [20].

Physical interactions of DSTN

• These results are consistent with a model in which pH-dependent motion of subdomain 1 relative to subdomain 2 (through region 75-105) of actin reveals a second cofilin binding site on actin (centered around region 112-125) that allows ADF/cofilin association with the actin filament [21].

Enzymatic interactions of DSTN

• Cofilin was indeed dephosphorylated and could thus be activated and operate as an actin-depolymerizing factor [22].

Other interactions of DSTN

• Although 72% identical in sequence, ADF has a much higher depolymerizing activity than cofilin at pH 8 [23].
• The functional interactions of actin with capping proteins, formin, actin-depolymerizing factor/cofilin, and the VCA-Arp2/3 filament branching machinery were profoundly altered by TMR labeling [24].
• One target site was chosen because we previously showed that the villin head piece competes with ADF for binding to F-actin [25].
• Brain-derived neurotrophic factor regulation of retinal growth cone filopodial dynamics is mediated through actin depolymerizing factor/cofilin [26].
• In addition to mRNA expression studies, up-regulation of GDI2, destrin and stathmin were confirmed with immunohistochemical analysis [27].

Analytical, diagnostic and therapeutic context of DSTN

• Molecular cloning and characterization of anther-preferential cDNA encoding a putative actin-depolymerizing factor [9].
• Southern blot analysis showed that there are one or a few copies of the putative ADF genes in B. napus and Arabidopsis thaliana [9].
• Cryoelectron microscopy showed that UNC-60B changed the twist of F-actin to a similar extent to vertebrate ADF/cofilins [28].
• In this study, we constructed a new cofilin expression plasmid, which had high expression frequency, and the structures of destrin and cofilin were analyzed by limited proteolysis and circular dichroism (CD) [29].
• However, we found that recombination had occurred in DSN cells, partially reconstituting a provirus-like structure that was capable of being spread, although inefficiently, through an infected cell culture [30].

References