St. Jude, Loyola and Kyoto University report that the system that controls the folding of newly made proteins also triggers the production of new membranes used to package and ship proteins
Part of a cellular mechanism that regulates the folding of new proteins into their proper shapes also includes a genetic response that enlarges the factory where both protein folding and packaging of proteins occurs. This finding, from researchers at St. Jude Childrens Research Hospital, Loyola University (Chicago) and Kyoto University (Kyoto, Japan), are published in the Oct. 15 issue of the Journal of Cell Biology. The link between protein folding and factory construction ensures that the two processes are coordinated when the cell is called upon to quickly make, fold and secrete large amounts of specific proteins.
The investigators discovered that the cell makes a molecule called XBP1 in response to an increased demand on the protein-folding machinery. This increased demand for folded proteins triggers the so-called unfolded protein response (UPR), as well as the expansion of the factory where proteins are folded and packaged so they can be secreted from the cell. The UPR also prompts the cell to make molecules called chaperones, which do the actual task of protein folding.
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