Dont even think about trying to pronounce it. Although it is found in many organisms including humans, glycosylphosphatidylinositol has remained a mouthful for laymen and a puzzle for scientists. And yet GPIs, as science thankfully calls these cellular lipids, are important in numerous biological functions, including disease transmission.
Now, for the first time, cellular biologists at the University of Georgia have developed new tools to study and localize GPIs in living organisms and are discovering a new understanding of how they work in tropical parasites that cause human disease and suffering.
The research was published in the May 9 issue of The FEBS (Federation of European Biochemical Societies) Journal by Kojo Mensa-Wilmot, professor of cellular and molecular biology, and Sandesh Subramanya, a former doctoral student in the department of cellular biology at UGA.
Kim Carlyle | EurekAlert!
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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