PMID- 23931994
OWN - NLM
STAT- MEDLINE
DCOM- 20131104
LR  - 20211021
IS  - 1097-4199 (Electronic)
IS  - 0896-6273 (Print)
IS  - 0896-6273 (Linking)
VI  - 79
IP  - 3
DP  - 2013 Aug 7
TI  - Leucine-rich repeat transmembrane proteins are essential for maintenance of 
      long-term potentiation.
PG  - 439-46
LID - S0896-6273(13)00498-4 [pii]
LID - 10.1016/j.neuron.2013.06.007 [doi]
AB  - Leucine-rich repeat transmembrane proteins (LRRTMs) are synaptic cell adhesion 
      molecules that trigger excitatory synapse assembly in cultured neurons and 
      influence synaptic function in vivo, but their role in synaptic plasticity is 
      unknown. shRNA-mediated knockdown (KD) of LRRTM1 and LRRTM2 in vivo in CA1 
      pyramidal neurons of newborn mice blocked long-term potentiation (LTP) in acute 
      hippocampal slices. Molecular replacement experiments revealed that the LRRTM2 
      extracellular domain is sufficient for LTP, probably because it mediates binding 
      to neurexins (Nrxs). Examination of surface expression of endogenous AMPA 
      receptors (AMPARs) in cultured neurons suggests that LRRTMs maintain newly 
      delivered AMPARs at synapses after LTP induction. LRRTMs are also required for 
      LTP of mature synapses on adult CA1 pyramidal neurons, indicating that the block 
      of LTP in neonatal synapses by LRRTM1 and LRRTM2 KD is not due to impairment of 
      synapse maturation.
CI  - Copyright (c) 2013 Elsevier Inc. All rights reserved.
FAU - Soler-Llavina, Gilberto J
AU  - Soler-Llavina GJ
AD  - Nancy Pritzker Laboratory, Department of Psychiatry and Behavioral Sciences, 
      Stanford University School of Medicine, 265 Campus Drive, Stanford, CA 94305, 
      USA.
FAU - Arstikaitis, Pamela
AU  - Arstikaitis P
FAU - Morishita, Wade
AU  - Morishita W
FAU - Ahmad, Mohiuddin
AU  - Ahmad M
FAU - Sudhof, Thomas C
AU  - Sudhof TC
FAU - Malenka, Robert C
AU  - Malenka RC
LA  - eng
GR  - R01 MH063394/MH/NIMH NIH HHS/United States
GR  - MH086403/MH/NIMH NIH HHS/United States
GR  - MH063394/MH/NIMH NIH HHS/United States
GR  - CAPMC/CIHR/Canada
GR  - P50 MH086403/MH/NIMH NIH HHS/United States
GR  - R37 MH063394/MH/NIMH NIH HHS/United States
GR  - R01 DA030379/DA/NIDA NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Neuron
JT  - Neuron
JID - 8809320
RN  - 0 (LRRTM1 protein, mouse)
RN  - 0 (LRRTM2 protein, mouse)
RN  - 0 (Membrane Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Neural Cell Adhesion Molecules)
RN  - 0 (RNA, Small Interfering)
RN  - 0 (Receptors, AMPA)
RN  - 0 (Vesicular Glutamate Transport Protein 1)
RN  - TFZ3H25BS1 (glutamate receptor ionotropic, AMPA 1)
SB  - IM
MH  - Age Factors
MH  - Animals
MH  - Animals, Newborn
MH  - Cells, Cultured
MH  - Dendrites/metabolism
MH  - Endocytosis/drug effects/genetics
MH  - Excitatory Postsynaptic Potentials/drug effects/genetics
MH  - Gene Expression Regulation/drug effects/genetics
MH  - Hippocampus/cytology/physiology
MH  - Humans
MH  - Long-Term Potentiation/*physiology
MH  - Membrane Proteins
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mutation/genetics
MH  - Nerve Tissue Proteins
MH  - Neural Cell Adhesion Molecules/genetics/*metabolism
MH  - Neurons/drug effects/physiology
MH  - Organ Culture Techniques
MH  - RNA, Small Interfering/metabolism
MH  - Receptors, AMPA/genetics/*metabolism
MH  - Synapses/*physiology
MH  - Time Factors
MH  - Transduction, Genetic
MH  - Vesicular Glutamate Transport Protein 1/metabolism
PMC - PMC3741667
MID - NIHMS491483
EDAT- 2013/08/13 06:00
MHDA- 2013/11/05 06:00
PMCR- 2014/08/07
CRDT- 2013/08/13 06:00
PHST- 2013/05/28 00:00 [accepted]
PHST- 2013/08/13 06:00 [entrez]
PHST- 2013/08/13 06:00 [pubmed]
PHST- 2013/11/05 06:00 [medline]
PHST- 2014/08/07 00:00 [pmc-release]
AID - S0896-6273(13)00498-4 [pii]
AID - 10.1016/j.neuron.2013.06.007 [doi]
PST - ppublish
SO  - Neuron. 2013 Aug 7;79(3):439-46. doi: 10.1016/j.neuron.2013.06.007.