The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
A tripartite motif protein TRIM11 binds and destabilizes Humanin, a neuroprotective peptide against Alzheimer's disease‐relevant insults
Abstract
Humanin (HN) is a newly identified neuroprotective peptide that specifically suppresses Alzheimer's disease (AD)‐related neurotoxicity. HN peptide has been detected in the human AD brain as well as in mouse testis and colon by immunoblot and immunohistochemical analyses. By means of yeast two‐hybrid screening, we identified TRIM11 as a novel HN‐interacting protein. TRIM11, which is a member of protein family containing a tripartite motif (TRIM), is composed of a RING finger domain, which is a putative E3 ubiquitin ligase, a B‐box domain, a coiled‐coil domain and a B30.2 domain. Deletion of the B30.2 domain in TRIM11 abolished the interaction with HN, whereas the B30.2 domain alone did not interact with HN. For their interaction, at least the coiled‐coil domain was indispensable together with the B30.2 domain. The intracellular level of glutathione S‐transferase‐fused or EGFP‐fused HN peptides or plain HN was drastically reduced by the coexpression of TRIM11. Disruption of the RING finger domain by deleting the first consensus cysteine or proteasome inhibitor treatment significantly diminished the effect of TRIM11 on the intracellular level of HN. These results suggest that TRIM11 plays a role in the regulation of intracellular HN level through ubiquitin‐mediated protein degradation pathways.
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“Although there are no reports relating TRIM22 with AD, TRIM11, another member of this family, was shown to bind to and destabilize humanin, a neuroprotective peptide that suppresses AD-related neurotoxicity.49”
From APOE*E2 allele delays age of onset in PSEN1 E280A Alzheimer’s disease (2016) · cites this paper as [49]
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Mechanisms Underlying Ubiquitination
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The tripartite motif family identifies cell compartments
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RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
Lorick, K. L., Jensen, J. P., Fang, S., Ong, A. M., Hatakeyama, S., & Weissman, A. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11364 · Cited by 1,151
The Tyrosine Kinase Negative Regulator c-Cbl as a RING-Type, E2-Dependent Ubiquitin-Protein Ligase
Joazeiro, C. A. P., Wing, S. S., Huang, H.-K., Leverson, J. D., Hunter, T. R., & Liu, Y. (1999) · Science · doi:10.1126/science.286.5438.309 · Cited by 1,036
Impaired Proteasome Function in Alzheimer's Disease
Keller, J. N., Hanni, K. B., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750436.x · Cited by 848
Does this have a familiar RING?
Saurin, A. J., Borden, K. L. B., Boddy, M. N., & Freemont, P. S. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)80017-x · Cited by 635
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Self-citationUBIQUITIN AND THE CONTROL OF PROTEIN FATE IN THE SECRETORY AND ENDOCYTIC PATHWAYS
Bonifacino, J. S., & Weissman, A. M. (1998) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.14.1.19 · Cited by 613
Cited by
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TRIM family proteins and their emerging roles in innate immunity
Ozato, K., Shin, D., Chang, T.-H., & Morse, H. C. (2008) · Nature reviews. Immunology · doi:10.1038/nri2413 · Cited by 1,131
TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases
Meroni, G., & Diez‐Roux, G. (2005) · BioEssays · doi:10.1002/bies.20304 · Cited by 744
Targeting Proteins for Destruction by the Ubiquitin System: Implications for Human Pathobiology
Schwartz, A. L., & Ciechanover, A. J. (2008) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.051208.165340 · Cited by 498
Stremlau, M. H., Perron, M. J., Welikala, S., & Sodroski, J. (2005) · Journal of Virology · doi:10.1128/jvi.79.5.3139-3145.2005 · Cited by 372
Obulesu, M., & Lakshmi, M. J. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1454-4 · Cited by 295
Metadata
- Authors
- Niikura, T., Hashimoto, Y., Tajima, H., Ishizaka, M., Yamagishi, Y., Kawasumi, M., Nawa, M., Terashita, K., Aiso, S., & Nishimoto, I.
- Affiliations
- Keio University (JP)
- Corresponding author
- Niikura, Takako
- Venue
- European Journal of Neuroscience
- Publisher
- Wiley
- Published
- 2003-03
- Volume
- 17
- Issue
- 6
- Pages
- 1150-1158
- ISSN
- 0953-816X (ISSN-L)
- 1460-9568
- OpenAlex
- W2076514957
- Cited by
- 115
- References
- 38
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 5 · 2022: 4 · 2021: 5 · 2020: 7 · 2019: 4 · 2018: 3 · 2017: 6 · 2016: 6 · 2015: 2 · 2014: 6 · 2013: 4 · 2012: 4
- FWCI
- 4.59
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- European Journal of Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- TRIM11, humanin, Alzheimer's disease, neuroprotection, protein-protein interaction, B30.2 domain, coiled-coil domain, RING E3 ubiquitin ligase, ubiquitin-mediated proteolysis, neurotoxicity, protein stability
- MeSH terms
- Alzheimer Disease, Animals, Carrier Proteins, Membrane Proteins, Proteins, Yeasts, Immunoblotting, Polymerase Chain Reaction, Neuroprotective Agents, Two-Hybrid System Techniques, Ubiquitin, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Mice
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