Structural highlights
Function
[HATA_DICDI] May act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments.
Publication Abstract from PubMed
The fast reaction of the actin-based cytoskeleton in motile cells after stimulation with a chemoattractant requires a signal-transduction chain that creates a very specific environment at distinct regions beneath the plasma membrane. Dictyostelium hisactophilin, a unique actin-binding protein, is a submembranous pH sensor that signals slight changes of the H+ concentration to actin by inducing actin polymerization and binding to microfilaments only at pH values below seven. It has a relative molecular mass of 13.5K and its most unusual feature is the presence of 31 histidine residues among its total of 118 amino acids. The transduction of an external signal from the plasma membrane to the cytoskeleton is poorly understood. Here we report the protein's structure in solution determined by nuclear magnetic resonance spectroscopy. The nuclear Overhauser effect intensities of the three-dimensional nuclear Overhauser spectra were used directly in the calculations. The overall folding of histactophilin is similar to that of interleukin-1 beta and fibroblast growth factor, but the primary amino-acid sequence of hisactophilin is unrelated to these two proteins.
Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor.,Habazettl J, Gondol D, Wiltscheck R, Otlewski J, Schleicher M, Holak TA Nature. 1992 Oct 29;359(6398):855-8. PMID:1436061[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Habazettl J, Gondol D, Wiltscheck R, Otlewski J, Schleicher M, Holak TA. Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor. Nature. 1992 Oct 29;359(6398):855-8. PMID:1436061 doi:http://dx.doi.org/10.1038/359855a0
