4,065
Views
30
CrossRef citations to date
0
Altmetric
Review

Long-term memory consolidation: The role of RNA-binding proteins with prion-like domains

&
Pages 568-586 | Received 08 Jun 2016, Accepted 29 Sep 2016, Published online: 14 Nov 2016

Figures & data

Figure 1. Schematic for bifurcated Sensory – Motor neuron culture system of Aplysia.

Figure 1. Schematic for bifurcated Sensory – Motor neuron culture system of Aplysia.

Table 1. Stimulation protocols and associated LTF in the Aplysia bifurcated culture system.

Figure 2. Prion mechanism of CPEB in memory (A) Mechanism of CPEB function in translational regulation: In the basal state CPEB interacts with Maskin or similar 4E-BPs which further interacts with eIF4E and prevents eIF4E interaction with eIF4G. Upon neuronal activity, CPEB gets phosphorylated and polyadenylation enables PABP association with eIF4G, which then disrupts 4E-BP-eIF4E interaction thereby permitting eIF4E-eIF4G interaction and resultant translation. (B) In the basal state both prionogenic and non-prion forms of CPEB exists mostly as monomers and can bind RNA and keep it in a translationally repressed state. Upon activity, the prionogenic form induces aggregation and the prion like nature induces self assembly and propagation of the aggregates where the RNA gets translated (C) CPEB monomers in the resting synapses and Q/N domain mediated amyloid like assemblies in active synapses.

Figure 2. Prion mechanism of CPEB in memory (A) Mechanism of CPEB function in translational regulation: In the basal state CPEB interacts with Maskin or similar 4E-BPs which further interacts with eIF4E and prevents eIF4E interaction with eIF4G. Upon neuronal activity, CPEB gets phosphorylated and polyadenylation enables PABP association with eIF4G, which then disrupts 4E-BP-eIF4E interaction thereby permitting eIF4E-eIF4G interaction and resultant translation. (B) In the basal state both prionogenic and non-prion forms of CPEB exists mostly as monomers and can bind RNA and keep it in a translationally repressed state. Upon activity, the prionogenic form induces aggregation and the prion like nature induces self assembly and propagation of the aggregates where the RNA gets translated (C) CPEB monomers in the resting synapses and Q/N domain mediated amyloid like assemblies in active synapses.

Figure 3. LC domain mediated RNP assembly in neuronal translational control (A) In the resting state, RNPs formed by interaction of individual RBPs and RNAs, sequester the RNA within RNPs in a translationally repressed state. Upon activity, the RNP disassembles leading to release of suppression resulting in translation of mRNAs with key synaptic functions (B) Models for LC mediated RNP assembly in neurons: in the resting state of synapses, individual RBPs interact by virtue of LC domains that are intrinsically disordered and form either a) transient and reversible amyloid like assemblies or b) reversible aggregates that are formed as result of weak multivalent interactions between LC domains.

Figure 3. LC domain mediated RNP assembly in neuronal translational control (A) In the resting state, RNPs formed by interaction of individual RBPs and RNAs, sequester the RNA within RNPs in a translationally repressed state. Upon activity, the RNP disassembles leading to release of suppression resulting in translation of mRNAs with key synaptic functions (B) Models for LC mediated RNP assembly in neurons: in the resting state of synapses, individual RBPs interact by virtue of LC domains that are intrinsically disordered and form either a) transient and reversible amyloid like assemblies or b) reversible aggregates that are formed as result of weak multivalent interactions between LC domains.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.