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CPEB is the stabilizing component of the synaptic mark.We have found that CPEB may serve as a stabilizer because it has prion-like properties.
We found that CPEB3-mediated protein synthesis is required for maintenance, but not for memory acquisition.
We also found that CPEB3 loses its ability to maintain long-term synaptic plasticity and long-term memory if its prion-like N-terminus domain is deleted.
Explicit Memory Storage in Mammals also requires a Prion-like Protein Is a functional prion also important for the persistence of memory in mammals?
In mouse and in human there are four distinct CPEB genes; in yeast and found that it displayed the two essential features of a prion-like protein: 1) it forms amyloidogenic aggregates and 2) aggregates are heritable across cell division.
The general finding that long-term plasticity and long-term memory recruit transcription in the nucleus, an organelle shared by all synapses of a neuron, has raised a question that we have begun to explore in and mice: Are long-term changes cell-wide, or can induced gene products be spatially compartmentalized so that they selectively alter the function of some synapses and not others?
In mice, we have also explored the molecular mechanisms whereby attention modifies and stabilizes internal representation of space.Does a prion-like conversion of CPEB3 also occur in the brain?We found that in the basal state CPEB3 binds to and represses the translation of its target m RNAs in the brain such as the AMPA receptor subunits Glu A1 and Glu A2.Prion proteins have the unusual ability to fold into functionally distinct conformations, one of which is self-perpetuating.When prion proteins convert to the self-perpetuating state, they can cause disease (in mammals) or a nonfunctioning protein (in yeast).For licensing motion picture film footage it is advised to apply directly to the copyright holders.For access to motion picture film stills please contact the Film Study Center.The propensity of CPEB3 to form aggregates derive from its N-terminus domain which comprises two regions rich in glutamine and a low complexity sequence which is predicted to be poorly structured and to form aggregates.To determine the role of CPEB3 in the persistence of synaptic plasticity and memory we generated a conditional knockout strain of CPEB3.Full-length CPEB undergoes similar changes in yeast but, surprisingly, the dominant, self-perpetuating prion-like form has the greatest capacity to stimulate translation of CPEB-regulated m RNA.Our preliminary studies suggest that conversion of CPEB to a prion-like state in stimulated synapses helps to maintain long-term synaptic changes associated with memory storage.