TY - JOUR
T1 - mTOR referees memory and disease through mRNA repression and competition
AU - Raab-Graham, Kimberly F.
AU - Niere, Farr
PY - 2017/6/1
Y1 - 2017/6/1
N2 - Mammalian target of rapamycin (mTOR) activity is required for memory and is dysregulated in disease. Activation of mTOR promotes protein synthesis; however, new studies are demonstrating that mTOR activity also represses the translation of mRNAs. Almost three decades ago, Kandel and colleagues hypothesised that memory was due to the induction of positive regulators and removal of negative constraints. Are these negative constraints repressed mRNAs that code for proteins that block memory formation? Herein, we will discuss the mRNAs coded by putative memory suppressors, how activation/inactivation of mTOR repress protein expression at the synapse, how mTOR activity regulates RNA binding proteins, mRNA stability, and translation, and what the possible implications of mRNA repression are to memory and neurodegenerative disorders.
AB - Mammalian target of rapamycin (mTOR) activity is required for memory and is dysregulated in disease. Activation of mTOR promotes protein synthesis; however, new studies are demonstrating that mTOR activity also represses the translation of mRNAs. Almost three decades ago, Kandel and colleagues hypothesised that memory was due to the induction of positive regulators and removal of negative constraints. Are these negative constraints repressed mRNAs that code for proteins that block memory formation? Herein, we will discuss the mRNAs coded by putative memory suppressors, how activation/inactivation of mTOR repress protein expression at the synapse, how mTOR activity regulates RNA binding proteins, mRNA stability, and translation, and what the possible implications of mRNA repression are to memory and neurodegenerative disorders.
KW - local translation
KW - mammalian target of rapamycin
KW - mRNA
UR - https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85019855760&origin=inward
UR - https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85019855760&origin=inward
U2 - 10.1002/1873-3468.12675
DO - 10.1002/1873-3468.12675
M3 - Review article
C2 - 28493559
SN - 0014-5793
VL - 591
SP - 1540
EP - 1554
JO - FEBS Letters
JF - FEBS Letters
IS - 11
ER -