کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2037148 | 1072301 | 2010 | 15 صفحه PDF | دانلود رایگان |
SummaryPrions are proteins that can assume at least two distinct conformational states, one of which is dominant and self-perpetuating. Previously we found that a translation regulator CPEB from Aplysia, ApCPEB, that stabilizes activity-dependent changes in synaptic efficacy can display prion-like properties in yeast. Here we find that, when exogenously expressed in sensory neurons, ApCPEB can form an amyloidogenic self-sustaining multimer, consistent with it being a prion-like protein. In addition, we find that conversion of both the exogenous and the endogenous ApCPEB to the multimeric state is enhanced by the neurotransmitter serotonin and that an antibody that recognizes preferentially the multimeric ApCPEB blocks persistence of synaptic facilitation. These results are consistent with the idea that ApCPEB can act as a self-sustaining prion-like protein in the nervous system and thereby might allow the activity-dependent change in synaptic efficacy to persist for long periods of time.PaperClip To listen to this audio, enable JavaScript on your browser. However, you can download and play the audio by clicking on the icon belowHelp with MP3 filesOptionsDownload audio (2854 K)
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► The Aplysia translational regulator ApCPEB has prion-like properties in neurons
► Exogenously expressed ApCPEB forms self-sustaining amyloidogenic multimers
► Serotonin enhances formation of exogenous ApCPEB multimers
► Inhibition of ApCPEB multimers blocks persistence of long-term facilitation
Journal: - Volume 140, Issue 3, 5 February 2010, Pages 421–435