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- W1552489964 abstract "Characteristic features of mammalian small heat shock proteins are their rapid phosphorylation in response to stress and mitogenic signals and their ability to form multimeric particles of 200-700 kDa and large aggregates up to 5000 kDa. Recently, a chaperoning function and an actin polymerization-inhibiting activity were demonstrated for the recombinant murine and turkey small heat shock protein, respectively. In this paper, we demonstrate that the actin polymerization-inhibiting activity of the murine small heat shock protein HSP25 is dependent on the degree of its phosphorylation and structural organization. Non-phosphorylated and phosphorylated HSP25 monomers, as well as non-phosphorylated multimeric HSP25 particles, were isolated from Ehrlich ascites tumor cells by ammonium sulfate precipitation, column chromatography, and ultracentrifugation and tested for their actin polymerization-inhibiting activity. Fluorescence spectroscopy and electron microscopy were used to monitor actin polymerization. Non-phosphorylated HSP25 monomers were active in inhibiting actin polymerization with about 90% inhibition at a 1:1 ratio of actin to HSP25, while phosphorylated HSP25 monomers and non-phosphorylated multimeric HSP25 particles were inactive. Furthermore, we present electron microscopic data on the structure of HSP25 particles." @default.
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- W1552489964 date "1994-08-01" @default.
- W1552489964 modified "2023-10-16" @default.
- W1552489964 title "Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity." @default.
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- W1552489964 doi "https://doi.org/10.1016/s0021-9258(17)32060-4" @default.
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