The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Aβ-Mediated NMDA Receptor Endocytosis in Alzheimer's Disease Involves Ubiquitination of the Tyrosine Phosphatase STEP61
Open accessAbstract
Amyloid β (Aβ) is involved in the etiology of Alzheimer's disease (AD) and may contribute to cognitive deficits by increasing internalization of ionotropic glutamate receptors. Striatal-enriched protein tyrosine phosphatase 61 (STEP 61), which is targeted in part to the postsynaptic terminal, has been implicated in this process. Here we show that STEP 61 levels are progressively increased in the cortex of Tg2576 mice over the first year, as well as in prefrontal cortex of human AD brains. The increased STEP 61 was associated with greater STEP activity, dephosphorylation of phospho-tyr 1472 of the NR2B subunit, and decreased NR1 and NR2B subunits on neuronal membranes. Treatment with Aβ-enriched medium also increased STEP 61 levels and decreased NR1/NR2B abundance in mouse cortical cultures as determined by biotinylation experiments. In STEP knock-out cultures, Aβ treatment failed to induce NMDA receptor internalization. The mechanism for the increase in STEP 61 levels appears to involve the ubiquitin proteasome system. Blocking the proteasome resulted in elevated levels of STEP 61. Moreover, STEP 61–ubiquitin conjugates were increased in wild-type cortical slices upon Aβ treatment as well as in 12 month Tg2576 cortex. These findings reveal a novel mechanism by which Aβ-mediated accumulation of STEP 61 results in increased internalization of NR1/NR2B receptor that may contribute to the cognitive deficits in AD.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · cited 9×
“Increased STEP protein levels are also found in human AD cor- tex. Results from our previous work found that the A -mediated reduced surface expression of NMDA receptor subunits is caused by increased endocytosis (Snyder et al., 2005).”
InfluentialSelf-citationLacor, P. N., Buniel, M. C., Furlow, P. W., Sanz Clemente, A., Velasco, P. T., Wood, M., Viola, K. L., & Klein, W. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3501-06.2007 · Cited by 1,188
NMDA receptor trafficking in synaptic plasticity and neuropsychiatric disorders
Lau, C. G., & Zukin, R. S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2153 · Cited by 1,159 · cited 1×
“The UPS system is disrupted in several other CNS disorders including Parkinson’s disease, schizophrenia, and Huntington’s disease (Altar et al., 2005; Lim and Tan, 2007; Dunah et al., 2000; Lau and Zukin, 2007).”
BackgroundKuchibhotla, K. V., Goldman, S. T., Lattarulo, C. R., Wu, H.-Y., Hyman, B. T., & Bacskai, B. J. (2008) · Neuron · doi:10.1016/j.neuron.2008.06.008 · Cited by 614
Choi, J., Levey, A. I., Weintraub, S. T., Rees, H. D., Gearing, M., Chin, L.-S., & Li, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314124200 · Cited by 568
Cited by
Aβ induces astrocytic glutamate release, extrasynaptic NMDA receptor activation, and synaptic loss
Talantova, M., Sanz-Blasco, S., Zhang, X., Xia, P., Akhtar, M. W., Okamoto, S.-I., Dziewczapolski, G., Nakamura, T., Cao, G., Pratt, A. E., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306832110 · Cited by 600
β-amyloid disrupts human NREM slow waves and related hippocampus-dependent memory consolidation
Mander, B. A., Marks, S. M., Vogel, J. W., Rao, V., Lu, B., Saletin, J. M., Ancoli-Israel, S., Jagust, W. J., & Walker, M. P. (2015) · Nature Neuroscience · doi:10.1038/nn.4035 · Cited by 569
The Role of NMDA Receptors in Alzheimer’s Disease
Liu, J., Chang, L., Song, Y., Li, H., & Wu, Y. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00043 · Cited by 535
Wang, M., Yang, Y., Wang, C.-J., Gamo, N. J., Jin, L. E., Mazer, J. A., Morrison, J. H., Wang, X.-J., & Arnsten, A. F. T. (2013) · Neuron · doi:10.1016/j.neuron.2012.12.032 · Cited by 489
Reversing EphB2 depletion rescues cognitive functions in Alzheimer model
Cissé, M., Halabisky, B., Harris, J., Devidze, N., Dubal, D. B., Sun, B., Orr, A., Lotz, G., Kim, D. H., Hamto, P., et al. (2011) · Nature · doi:10.1038/nature09635 · Cited by 433
Metadata
- Authors
- Kurup, P., Zhang, Y., Xu, J., Venkitaramani, D. V., Haroutunian, V., Greengard, P., Nairn, A. C., & Lombroso, P. J.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2010-04-28
- Volume
- 30
- Issue
- 17
- Pages
- 5948-5957
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W2016323146
- Cited by
- 224
- References
- 16
- FWCI
- 13.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Aβ-Mediated NMDA Receptor Endocytosis in Alzheimer's Disease Involves Ubiquitination of the Tyrosine Phosphatase STEP61. https://app.cochat.ai/papers/10.1523/jneurosci.0157-10.2010
- The paper
- Kurup, P., Zhang, Y., Xu, J., Venkitaramani, D. V., Haroutunian, V., Greengard, P., Nairn, A. C., & Lombroso, P. J. (2010). Aβ-Mediated NMDA Receptor Endocytosis in Alzheimer's Disease Involves Ubiquitination of the Tyrosine Phosphatase STEP61. The Journal of Neuroscience. https://doi.org/10.1523/jneurosci.0157-10.2010
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
