Anyone who's tried to neatly gather a fitted sheet can tell you: folding is hard.
Anyone who's tried to neatly gather a fitted sheet can tell you: folding is hard. Get it wrong with your laundry and the result can be a crumpled, wrinkled mess of fabric, but when folding fails among the approximately 7,000 proteins with an origami-like complexity that regulate essential cellular functions, the result can lead to one of a multitude of serious diseases ranging from emphysema and cystic fibrosis to Alzheimer's disease.
"But there's something else at work," says lead-author Rob Williams, a postdoctoral fellow with a joint appointment in both Hebert's and Gierasch's labs."There's an exclusive club of proteins called 'selenoproteins,' which contain the rare element selenium. Out of approximately 20,000 different proteins in our bodies, only 25 of them are selenoproteins. The UGGT partner Sep15 is a selenoprotein. Sep15 is always associated with UGGT.
So what, exactly, is Sep15 doing?"There are two possibilities, both of which we're following up on," says Hebert."Either Sep15 is giving the misfolded protein a chance at correcting its shape, or it is marking that protein for destruction." This research was supported by the National Institutes of General Medical Sciences and facilitated by the availability of instrumentation in the UMass Amherst Institute for Applied Life Sciences.
Cystic Fibrosis Genes Medical Topics Molecular Biology Cell Biology Biochemistry Research Biotechnology
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