RT Journal Article
SR Electronic
T1 The low complexity motif of cytoplasmic polyadenylation element binding protein 3 (CPEB3) is critical for the trafficking of its targets in neurons
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.05.16.100032
DO 10.1101/2020.05.16.100032
A1 Lenzie Ford
A1 Arun Asok
A1 Arielle D. Tripp
A1 Cameron Parro
A1 Michelle Fitzpatrick
A1 Christopher A. de Solis
A1 Neeva Shafiian
A1 Luana Fioriti
A1 Rajesh Kumar Soni
A1 Eric R. Kandel
YR 2020
UL http://biorxiv.org/content/early/2020/05/17/2020.05.16.100032.abstract
AB Biomolecular condensates, membraneless organelles found throughout the cell, play critical roles in many aspects of cellular function. Ribonucleoprotein granules (RNPs), a type of biomolecular condensate found in neurons that are necessary for local protein synthesis and are involved in long-term potentiation (LTP). Several RNA-binding proteins present in RNPs are necessary for the synaptic plasticity involved in LTP and long-term memory. Most of these proteins possess low complexity motifs, allowing for increased promiscuity. We explore the role the low complexity motif plays for RNA binding protein cytoplasmic polyadenylation element binding protein 3 (CPEB3), a protein necessary for long-term memory persistence. We found that RNA binding and SUMOylation are necessary for CPEB3 localization to the P body, thereby having functional implications on translation. Here, we investigate the role of the low complexity motif of CPEB3 and find that it is necessary for P body localization and downstream targeting for local protein synthesis.Competing Interest StatementThe authors have declared no competing interest.