Differential splicing and glycosylation of Apoer2 alters synaptic plasticity and fear learning
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Glycosylation of the apolipoprotein E receptor Apoer2 is important for regulating synaptic function and cognition.
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Mild increases in ApoER2 levels in response to exon 16 deletion led to enhanced LTP.
“Interestingly, while mild increases in ApoER2 levels in response to exon 16 deletion led to enhanced LTP (Wasser et al., 2014), we showed constitutive high level of ApoER2 expression in IDOL-deficient mice severely impaired LTP.”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Wasser et al., 2014
The Results report that exon 16 deletion increased Apoer2 abundance and enhanced LTP in hippocampal slices when exon 19 was present. But deletion of exon 16 did not enhance LTP when exon 19 was also absent, so the claim omits a necessary condition. The Results describe a twofold Apoer2 increase in the mice with enhanced LTP, rather than characterizing it as mild. (LLM, conf=0.87)
Experimental — accuracy not yet measuredLrp8 lacking exon 16 increases the stability of ApoER2 in neurons and is associated with higher spine density.
“Lrp8 lacking exon 16, which encodes the O-linked sugar (OLS) domain, increased the stability of ApoER2 in neurons and was associated with higher spine density (Wasser et al., 2014).”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Wasser et al., 2014
The Results section on hippocampal spine density reports increased Apoer2 abundance in exon-16-lacking mice and higher spine density, though the increase in average spine density was significant only in mice also lacking exon 19 (page unavailable). The Discussion says reduced cleavage might make Apoer2 more stable, but also reports increased Apoer2 mRNA; it does not establish increased protein stability in neurons as a measured finding. (LLM, conf=0.85)
Experimental — accuracy not yet measuredSpine density is decreased in ApoER2 KO mice and increased with ApoER2 overexpression.
“Our observation that IDOL bidirectionally regulate spine density through ApoER2 is consistent with previous studies showing that spine density is decreased in ApoER2 KO mice and increased in the setting of ApoER2 overexpression (Dumanis et al., 2011; Wasser et al., 2014).”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Wasser et al., 2014
IDOL bidirectionally regulates spine density through ApoER2.
“Our observation that IDOL bidirectionally regulate spine density through ApoER2 is consistent with previous studies showing that spine density is decreased in ApoER2 KO mice and increased in the setting of ApoER2 overexpression (Dumanis et al., 2011; Wasser et al., 2014).”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Wasser et al., 2014
Exclusion of the OLS domain imparts strong resistance to cleavage of ApoER2 and prevents release of both the extracellular and intracellular fragments.
“In addition to increased abundance of the receptor, exclusion of the OLS domain, which contains the extracellular cleavage site, imparts a strong resistance to the cleavage of ApoER2 and thus prevents the release of both the extracellular and the intracellular fragments of ApoER2 (34).”
From Reelin: Neurodevelopmental Architect and Homeostatic Regulator of Excitatory Synapses (2017) · cites this paper as [34]
Loss of ApoER2 cleavage leads to increased ApoER2 expression and a concomitant enhancement of dendritic spine density.
“Loss of ApoER2 cleavage leads to increased ApoER2 expression and a concomitant enhancement of dendritic spine density (34), which is consistent with the published results of ApoER2 overexpression in wild-type neuron cultures (16).”
From Reelin: Neurodevelopmental Architect and Homeostatic Regulator of Excitatory Synapses (2017) · cites this paper as [34]
The OLS domain regulates the abundance of ApoER2 by protecting it from proteolytic processing in a glycosylation-dependent manner.
“This juxtamembranous O-linked sugar (OLS) domain regulates the abundance of the receptor by protecting it from proteolytic processing in a glycosylation-dependent manner (34,35).”
From Reelin: Neurodevelopmental Architect and Homeostatic Regulator of Excitatory Synapses (2017) · cites this paper as [34]
Mice lacking exon 16 either with or without exon 19 acquire contextual fear memory as well as wild-type mice; mice lacking both exons appear hypersensitive to cued fear memory, whereas inclusion of exon 19 completely blocked acquisition of cued fear memory.
“Mice lacking exon 16 either with or without exon 19 (ApoER2[⌬16ϩ19] or ApoER2[⌬16⌬19], respectively) acquire contextual fear memory as well as wild-type mice; however, mice lacking both exons appear hypersensitive to cued fear memory, whereas the inclusion of exon 19 completely blocked the acquisition of cued fear memory (34).”
From Reelin: Neurodevelopmental Architect and Homeostatic Regulator of Excitatory Synapses (2017) · cites this paper as [34]
Alternative splicing of ApoER2 can differentially modulate the acquisition of fear memory.
“Alternative splicing of the Reelin receptor, ApoER2, can differentially modulate the acquisition of fear memory (30,34).”
From Reelin: Neurodevelopmental Architect and Homeostatic Regulator of Excitatory Synapses (2017) · cites this paper as [34]
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- Authors
- Wasser, C. R., Masiulis, I., Durakoglugil, M. S., Lane-Donovan, C., Xian, X., Beffert, U., Agarwala, A., Hammer, R. E., & Herz, J.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Center for Translational Neurodegeneration Research, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
- Corresponding author
- Wasser, Catherine R.
- Masiulis, Irene
- Herz, Joachim
- ORCID
- Venue
- Science Signaling
- Published
- 2014-11-25
- Volume
- 7
- Issue
- 353
- Pages
- ra113-ra113
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- PMC
- PMC4355955
- OpenAlex
- W2157735201
- Cited by
- 48
- References
- 61
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 3 · 2023: 6 · 2022: 7 · 2021: 3 · 2020: 3 · 2019: 2 · 2018: 4 · 2017: 6 · 2016: 7 · 2015: 2 · 2014: 1
- FWCI
- 2.44
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science Signaling (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL063762, R37HL063762)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Keywords
- ApoER2, apolipoprotein E receptor, differential splicing, receptor glycosylation, synaptic plasticity, fear conditioning, long-term potentiation, hippocampus, glutamate receptors, gamma-secretase cleavage, spatial learning, memory
- MeSH terms
- Animals, Avoidance Learning, Conditioning, Classical, Cues, Dendrites, Exons, Fear, Female, Glycosylation, Male, Mice, Inbred C57BL, Nerve Tissue Proteins, Synaptic Transmission, Protein Processing, Post-Translational, Reflex, Startle, Structure-Activity Relationship, Alternative Splicing, Protein Structure, Tertiary, Long-Term Potentiation, Maze Learning, LDL-Receptor Related Proteins, Mice, Amyloid Precursor Protein Secretases, CA1 Region, Hippocampal, Mice, 129 Strain
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