A tripartite motif protein TRIM11 binds and destabilizes Humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults.

Niikura T, Hashimoto Y, Tajima H, Ishizaka M, Yamagishi Y, Kawasumi M, Nawa M, Terashita K, Aiso S, Nishimoto I

The European journal of neuroscience1 Mar 2003Cited by 98 (Europe PMC)

PMID12670303DOI10.1046/j.1460-9568.2003.02553.xPepBankPUB-12670303

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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study5

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone5

In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Humanin.

01LabNot a test of Humanin aloneIn vitro (cells)Mechanism
A yeast two-hybrid screen identified TRIM11 as a novel humanin-interacting protein.
In plain wordsIn a lab screen, TRIM11 was found to be a protein that binds humanin.
Peptide
Humanin
Outcome
Not applicableTRIM11 as humanin-interacting protein
Study
yeastn: not reported in source
yeast two-hybrid screening
Outcome group
Receptor activity and mechanism · Nervous system and cognition
Source sentences
Summary
By means of yeast two-hybrid screening, we identified TRIM11 as a novel HN-interacting protein.
In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Humanin.
Report a problemFND-1267030301
02LabNot a test of Humanin aloneIn vitro (cells)Mechanism
Deletion of the B30.2 domain in TRIM11 abolished its interaction with humanin, while the B30.2 domain alone did not interact with humanin.
In plain wordsIn lab cells, TRIM11 needed its B30.2 domain to bind humanin, but this domain alone was not enough.
Peptide
Humanin
Outcome
Not applicableRole of TRIM11 B30.2 domain in the interaction with humanin
Study
n: not reported in source
cells coexpressing humanin and TRIM11 constructs
Outcome group
Receptor activity and mechanism · Nervous system and cognition
Source sentences
Summary
Deletion of the B30.2 domain in TRIM11 abolished the interaction with HN, whereas the B30.2 domain alone did not interact with HN.
In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Humanin.
Report a problemFND-1267030302
03LabNot a test of Humanin aloneIn vitro (cells)Mechanism
For the interaction of TRIM11 with humanin, at least the coiled-coil domain was indispensable together with the B30.2 domain.
In plain wordsIn lab cells, TRIM11 needed both its coiled-coil domain and its B30.2 domain to bind humanin.
Peptide
Humanin
Outcome
Not applicableRole of TRIM11 coiled-coil domain in the interaction with humanin
Study
n: not reported in source
cells coexpressing humanin and TRIM11 constructs
Outcome group
Receptor activity and mechanism · Nervous system and cognition
Source sentences
Summary
For their interaction, at least the coiled-coil domain was indispensable together with the B30.2 domain.
In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Humanin.
Report a problemFND-1267030303
04LabNot a test of Humanin aloneIn vitro (cells)Mechanism
In cells, coexpression of TRIM11 drastically reduced the intracellular level of glutathione S-transferase-fused, EGFP-fused and plain humanin.
In plain wordsIn lab cells, making more TRIM11 sharply lowered the level of humanin inside the cells.
Peptide
Humanin
Outcome
DecreaseIntracellular humanin level with TRIM11 coexpression
Study
n: not reported in source
cells coexpressing humanin and TRIM11 constructs
Outcome group
Receptor activity and mechanism · Nervous system and cognition
Source sentences
Summary
The intracellular level of glutathione S-transferase-fused or EGFP-fused HN peptides or plain HN was drastically reduced by the coexpression of TRIM11.
In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Humanin.
Report a problemFND-1267030304
05LabNot a test of Humanin aloneIn vitro (cells)Mechanism
In cells, deleting the first consensus cysteine of the RING finger domain or treating with a proteasome inhibitor significantly diminished the effect of TRIM11 on intracellular humanin level.
In plain wordsIn lab cells, blocking the TRIM11 RING domain or the proteasome weakened the way TRIM11 lowers humanin levels.
Peptide
Humanin
Outcome
Not applicableRole of TRIM11 RING finger domain and proteasome in humanin level
Study
n: not reported in source
cells coexpressing humanin and TRIM11 constructs
Outcome group
Receptor activity and mechanism · Nervous system and cognition
Source sentences
Summary
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.
In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Humanin.
Report a problemFND-1267030305

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Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

Version 2Current
13 Oct 2026, 21:44 UTC
Study results updated
Version 1
13 Oct 2026, 16:31 UTC
First added · source update from Europe PMC

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