Vimentin is a developmentally regulated intermediate filament protein (IFP) found in cells of mesenchymal origin. It is believed to be involved with the intracellular transport of proteins between the nucleus and plasma membrane. Unlike other IFP proteins, vimentin is expressed, along with desmin, during the early stages of cellular development. During the development process, vimentin is exchanged for new, tissue-specific IFPs. Vimentin has been implicated to be involved in the rate of steroid synthesis via its role as a storage network for steroidogenic cholesterol containing lipid droplets. Vimentin phosphorylation by a protein kinase causes the breakdown of intermediate filaments and activation of an ATP and myosin light chain dependent contractile event. This results in cytoskeletal changes that facilitate the interaction of the lipid droplets within mitochondria, and subsequent transport of cholesterol to the organelles leading to an increase in steroid synthesis.
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Protein Aliases: epididymis luminal protein 113; FLJ36605; RP11-124N14.1; VIME; Vimentin
Gene Aliases: CTRCT30; HEL113; VIM