Protein self-assembly: A new frontier in cell signaling |
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| Affiliation: | 1. Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA, 94305, USA;2. Department of Developmental Biology, Stanford University School of Medicine, Stanford, CA, 94305, USA;1. Department of Biology, Duke University, Durham, NC, 27708, USA;2. Center for Engineering MechanoBiology, Washington University, St. Louis, MO, 63130, USA;3. Center for Science and Engineering Living Systems (CSELS), Washington University, St. Louis, MO, 63130, USA;1. Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA 94305, USA;2. Department of Developmental Biology, Stanford University, Stanford, CA 94305, USA;3. Ann Romney Center for Neurologic Disease, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA;4. Harvard Stem Cell Institute, Cambridge, MA 02138, USA;5. Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA;1. Department of Chemical and Systems Biology, Stanford University, Stanford, CA 94305, United States;2. Department of Developmental Biology, Stanford University, Stanford, CA 94305, United States;1. Department of Biology, Stanford University, 269 Campus Drive, Stanford, CA 94305, USA;2. Department of Chemical and Systems Biology, Stanford University, 269 Campus Drive, Stanford, CA 94305, USA;3. Department of Developmental Biology, Stanford University, 269 Campus Drive, Stanford, CA 94305, USA |
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| Abstract: | Long viewed as paradigm-shifting, but rare, prions have recently been discovered in all domains of life. Protein sequences that can drive this form of self-assembly are strikingly common in eukaryotic proteomes, where they are enriched in proteins involved in information flow and signal transduction. Although prions were thought to be a consequence of random errors in protein folding, recent studies suggest that prion formation can be a controlled process initiated by defined cellular signals. Many are present in normal biological contexts, yet are invisible to most technologies used to interrogate the proteome. Here, we review mechanisms by which protein self-assembly can create a stable record of past stimuli, altering adaptive responses, and how prion behavior is controlled by signaling processes. We touch on the diverse implications that this has for normal biological function and regulation, ranging from drug resistance in fungi to the innate immune response in humans. Finally, we discuss the potential for prion domains in transcription factors and RNA-binding proteins to orchestrate heritable gene expression changes in response to transient signals, such as during development. |
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| Keywords: | Prions Protein self-assembly Chaperones Cellular memory Adaptation Signaling Mnemons Intrinsic disorder Gene expression |
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