The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index; 4 of the 8 sources its claims cite were checked for support.
USP16 Regulates the Stability and Function of LDL receptor by Deubiquitination
Open accessAbstract
Low-density lipoprotein (LDL) particles are known to be atherogenic agents in coronary artery diseases. They adjust to other electronegative forms and can be the subject for the enhancement of inflammatory events in vessel subendothelial spaces. The LDL uptake is related to the membrane scavenger receptors, including LDL receptor (LDLR). The LDLR expression is closely associated with LDL uptake and occurrence of diseases, such as atherosclerotic cardiovascular diseases. Our findings identified USP16 as a novel regulator of LDLR due to its ability to prevent ubiquitylation-dependent LDLR degradation, further promoting the uptake of LDL. The enhancement of USP16-mediated deubiquitination andthe suppressive degradation of the LDLR cause the presentation of a potential strategy to increase LDL cholesterol clearance.
Overview
AI snapshot
Written from the paper’s full text.
TL;DR
USP16 is identified as a deubiquitinase that stabilizes LDLR by removing ubiquitin, thereby promoting LDL uptake in Hela cells. It acts post-translationally, since USP16 manipulation did not change LDLR mRNA levels.
Key findings
- USP siRNA library screening in LDLR-Myc-overexpressing Hela cells found USP16, USP2, USP18, and USP52 had the greatest effect on LDLR protein; repeated checks confirmed USP16 and USP2 changes, while USP52 interference showed no statistical change. USP16 had the most significant effect on LDLR.
- USP16 overexpression or interference did not alter LDLR mRNA levels, indicating post-transcriptional regulation.
- Co-IP showed USP16 interacted with LDLR but not IDOL; USP16 interference significantly increased LDLR ubiquitin levels, and CHX treatment caused a remarkable decrease in LDLR protein after USP16 interference.
- LDL uptake was significantly reduced with USP16 interference, but USP16 interference had no noticeable effect on LDL uptake in LDLR-overexpressing Hela cells.
Methods
- Hela cells were cultured and used for LDLR-Myc stable line construction, siRNA knockdown of USPs, and HA-USP16/Myc-LDLR overexpression; four independent series of treatments were conducted, and experiments were repeated four times.
- Assays included Co-IP, Western blot, RT-qPCR, immunofluorescence, cycloheximide degradation, and LDL uptake with 5 μg/mL DyLight 594-labeled LDL; fluorescence was quantified with ImageJ.
- Data are presented as mean ± SD and analyzed by one-way ANOVA, with P < 0.05 considered statistically significant.
Limitations
- Stated: further research is needed to enhance USP16 expression and decrease LDL in the human body.
- Evident: all experiments were performed in Hela cervical cancer cells, with no in vivo animal or clinical validation.
- Evident: some screening data are not shown (e.g., decreased cell viability in the USP18 siRNA group), and the study does not provide additional mechanistic details beyond ubiquitination and stability.
Model-written summary. Check it against the paper before relying on it.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
4 of 8 cited sources checked · 2 supported · 0 flagged · accuracy not yet measured
- Findingcitation
USP2 significantly regulates LDLR protein.
“These results revealed that USP2 could significantly regulate LDLR protein, which was consistent with the outcomes of a previous research.13)”
Quote in the paperNot a substantial claim1 of 1 sources checked- cites [13] 13. Nelson JK, Sorrentino V, Avagliano Trezza R, et al. The deubiquitylase USP2 regulates the LDLR pathway by counteracting the E3-ubiquitin ligase IDOL. Circ Res 2016; 118: 410-9. source
- Findingown data
USP16 has the most significant effect on LDLR among the screened USPs.
“Collectively, the abovementioned data demonstrated that through siRNA library screening, USP16 has the most significant effect on LDLR.”
Quote in the paperSubstantial claim - Findingown data
USP16 interference does not noticeably affect LDL uptake in LDLR-overexpressing Hela cells.
“Conversely, there was no noticeable influence on LDL uptake even with USP16 interference in LDLR overexpressing Hela cells (Figure 5A, B).”
Quote in the paperSubstantial claim - Findingown data
USP16 interference does not down-regulate LDLR mRNA levels.
“Furthermore, we noted that the mRNA level of LDLR was not down-regulated after USP16 interference (Figure 3B).”
Quote in the paperSubstantial claim - Findingown data
USP52 interference has no remarkable influence on LDLR protein.
“There was no remarkable influence on LDLR after USP52 interference (Figure 2A-C).”
Quote in the paperNot a substantial claim
- Findingown data
In a USP siRNA library screen, USP16, USP2, USP18, and USP52 had the greatest effect on LDLR protein level.
“In the present study, through the USP siRNA library screening, it was found that the USP16, USP2, USP18, and USP52 had the greatest effect on the level of LDLR protein (Figure 2A), which was consistent with findings of a previous research, 13) and we also found that the cell viability was decreased in the group of USP18 siRNA (data not are shown).”
Quote in the paperSubstantial claim - Findingown data
USP16 interacts with LDLR.
“The results showed that LDLR, but not IDOL, was coimmunoprecipitated by USP16 (Figure 4A, B), reflecting an interaction between USP16 and LDLR.”
Quote in the paperSubstantial claim - Findingown data
Overexpression of LDLR in Hela cell lines was successfully verified at both protein and mRNA levels.
“Furthermore, the overexpression of LDLR was successfully verified in both protein and mRNA expression levels (Figure 1A, B).”
Quote in the paperSubstantial claim - Findingown data
USP16 overexpression does not influence LDLR mRNA levels.
“Compared with the control group and the overexpressed LDLR group, the results showed that the overexpressed USP16 did not influence mRNA levels of LDLR (Figure 3A).”
Quote in the paperSubstantial claim - Findingown data
USP16 interference increases the ubiquitin level of LDLR.
“The ubiquitin of LDLR was detected, and it was noted that the ubiquitin level of LDLR was significantly higher with USP16 interference (Figure 4C).”
Quote in the paperSubstantial claim - Interpretationown data
USP16 promotes LDL uptake.
“The uptake of LDL was detected by immunofluorescence staining, and the results showed that the uptake of LDL was significantly reduced with USP16 interference (Figure 5A, B).”
- Also stated in: § Discussion · boosted
“In summary, the present study identified deubiquitylase USP16 as a novel regulator of LDL uptake due to its ability to inhibit LDLR degradation.”
Quote in the paperSubstantial claim - Also stated in: § Discussion · boosted
- Interpretationown data
USP16 prevents ubiquitylation-dependent degradation of LDLR by removing ubiquitin from LDLR.
“Our findings identified USP16 as a novel regulator of LDLR due to its ability to prevent ubiquitylation-dependent LDLR degradation, further promoting the uptake of LDL.”
- Also stated in: § USP16 positively regulates LDLR via post-translational modification: · boosted
“Taken together, these results were consistent with the notion that USP16 removes ubiquitin from LDLR to prevent its degradation, and it was demonstrated that USP16 regulated the protein stability of LDLR via the deubiquiti- nation manner.”
- Also stated in: § Discussion · hedged
“Our results revealed that USP 16 could inhibit the ubiquitination LDLR degradation, promoting the uptake of LDL in human cervical tumor cell lines.”
Quote in the paperSubstantial claim- Rests on an assumption: USP16 is a deubiquitinating enzyme (DUB).
- Also stated in: § USP16 positively regulates LDLR via post-translational modification: · boosted
- Interpretationown data
USP16 is a novel positive regulator of LDLR protein levels.
“Our findings identified USP16 as a novel regulator of LDLR due to its ability to prevent ubiquitylation-dependent LDLR degradation, further promoting the uptake of LDL.”
- Also stated in: § USP16 increases the stability of LDLR: · plain
“By contrast, USP16 markedly regulated LDLR protein levels compared with USP2.”
- Also stated in: § USP16 increases the stability of LDLR: · boosted
“Collectively, the abovementioned data demonstrated that through siRNA library screening, USP16 has the most significant effect on LDLR.”
Quote in the paperSubstantial claim- Rests on an assumption: USP16 has not been reported to regulate LDLR.
- Also stated in: § USP16 increases the stability of LDLR: · plain
- Interpretationown data
USP16 interference decreases LDLR protein stability when protein synthesis is inhibited.
“Compared with the control group, when the synthesis of protein was inhibited, Western blot assay revealed that USP 16 interference resulted in a remarkable decrease of LDLR protein in Hela cells (Figure 4D), indicating that USP16 significantly increased stability of LDLR.”
Quote in the paperSubstantial claim - Interpretationown data
USP16 regulates LDL uptake through promoting deubiquitination of LDLR.
“These results indicated that USP16 regulates the uptake of LDL through promoting the deubiquitination of LDLR.”
Quote in the paperSubstantial claim- Rests on an assumption: USP16 is a deubiquitinating enzyme (DUB).
- Probably not a substantial claim. 3
- It may state two separate claims as one. 2
Probably not a substantial claim. The paper’s conclusions may not depend on it.
PremisecitationUSP2 regulates the LDLR pathway by counteracting the E3-ubiquitin ligase IDOL.
“It has been reported that USP2 can regulate the deubiquitination of LDLR.13)”
Quote in the paperNot a substantial claim2 of 3 sources checked- cites [13] 13. Nelson JK, Sorrentino V, Avagliano Trezza R, et al. The deubiquitylase USP2 regulates the LDLR pathway by counteracting the E3-ubiquitin ligase IDOL. Circ Res 2016; 118: 410-9. source
- cites [14] 14. Hobbs HH, Russell DW, Brown MS, Goldstein JL. The LDL receptor locus in familial hypercholesterolemia: mutational analysis of a membrane protein. Annu Rev Genet 1990; 24: 133-70. source
- cites [15] 15. Bjune K, Wierød L, Naderi S. Triciribine increases LDLR expression and LDL uptake through stabilization of LDLR mRNA. Sci Rep 2018; 8: 16174. source
The Introduction describes LDLR regulation through PCSK9-mediated degradation and mRNA stability, while the Discussion focuses on triciribine's effect on LDLR mRNA stability. Searches for USP2-mediated deubiquitination and IDOL found no passage addressing either mechanism, so our copy does not verify the attributed claim. Page numbers were not available in the indexed passages. (LLM, conf=0.76)
Experimental — accuracy not yet measured
Probably not a substantial claim.
PremisecitationThe ubiquitin-proteasome system regulates the LDLR pathway through ubiquitylation-dependent degradation of LDLR mediated by the E3-ubiquitin ligase IDOL.
“Recently, the ubiquitin-proteasome system has been recognized as a novel regulator in the LDLR pathway through ubiquitylation-dependent degradation of the LDLR mediated by the E3-ubiquitin ligase inducible degrader of the LDLR (IDOL).”
Quote in the paperSubstantial claim1 of 1 sources checked- cites [12] 12. Zelcer N, Hong C, Boyadjian R, Tontonoz P. LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor. Science 2009; 325: 100-4. source
The passage labeled Abstract states that IDOL is an E3 ubiquitin ligase that ubiquitinates LDLR and targets it for degradation. But the Fig. 4H passage says the proteasome blocker MG132 did not stabilize LDLR and that LDLR degradation occurs in the lysosome, so describing this as proteasome-mediated degradation is not supported. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Probably not a substantial claim. The paper’s conclusions may not depend on it.
PremisecitationLDLR is a major determinant of circulating levels of LDL.
“A number of scholars reported that LDLR is a major determinant of circulating levels of LDL.[16][17][18]”
Quote in the paperNot a substantial claim0 of 3 sources checked- cites [16] 16. Jeon H, Blacklow SC. Structure and physiologic function of the low-density lipoprotein receptor. Annu Rev Biochem 2005; 74: 535-62. source
- cites [17] 17. Li Y, Cam J, Bu G. Low-density lipoprotein receptor family: endocytosis and signal transduction. Mol Neurobiol 2001; 23: 53-67. source
- cites [18] 18. Brown MS, Goldstein JL. A receptor-mediated pathway for cholesterol homeostasis. Science 1986; 232: 34-47. source
It may state two separate claims as one.
Interpretationown dataUSP16 regulation of LDLR protein is independent of transcriptional regulation and may be post-transcriptional.
“These results demonstrated that regulation of LDLR protein by USP16 was independent of transcriptional regulation while may be associated with posttranscriptional regulation.”
- Also stated in: § Discussion · plain
“Using a siRNA screening approach, in the present research, we identified USP16 as a post-transcriptional regulator of LDLR degradation.”
Quote in the paperSubstantial claim- Also stated in: § Discussion · plain
It may state two separate claims as one.
InterpretationreasoningMaintenance of USP16 activity may cause increased LDLR abundance and enhanced LDL uptake.
“This finding can demonstrate that maintenance of USP16 activity may cause increased LDLR abundance and enhanced LDL uptake.”
Quote in the paperSubstantial claim
The paper relies on this without support.
Regulation of deubiquitylases in cholesterol metabolism has remained elusive.
“However, regulation of deubiquitylases in cholesterol metabolism has remained elusive.”
The paper relies on this without support.
Regulation of LDLR by other members of the USP family has remained obscure.
“However, the regulation of LDLR by other members of the USP family has remained obscure.”
The paper relies on this without support.
USP16 has not been reported to regulate LDLR.
“To date, remarkably, the regulation of LDLR by USP 16 has not been reported.”
The paper relies on this without support.
USP16 is a deubiquitinating enzyme (DUB).
“Since USP16 is a DUB, we attempted to indicate whether USP16 can regulate the LDLR protein level by its deubiquitinase activity.”
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Figure 4 names IDOL rather than LDLR as the deubiquitylation target
MinorThe Figure 4 title says USP16 deubiquitylates IDOL, whereas the Results say USP16 removes ubiquitin from LDLR and that IDOL was not coimmunoprecipitated with USP16. This changes the stated target of the paper's central mechanism.
“Figure 4. USP16 deubiquitylates inducible degrader of the LDLR and increases its stability.”
“Taken together, these results were consistent with the notion that USP16 removes ubiquitin from LDLR to prevent its degradation”
Figure 1 reports a different statistical test from the Methods
MinorThe Methods state that all data were evaluated by one-way ANOVA, but the Figure 1 caption reports a non-parametric t-test.
“These data were evaluated by one-way analysis of variance (ANOVA) test using GraphPad Prism software (GraphPad Software, Inc., San Diego, CA, USA).”
“The experiments were repeated for four times.Non-parametric t-test, *P < 0.05, **P < 0.01.”
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Metadata
- Authors
- Li, Y., Rao, Y., Zhu, H., Jiang, B., & Zhu, M.
- Affiliations
- Department of Cardiovascular Internal Medicine, The Fifth Hospital of Xiamen
- Central Laboratory, The Fifth Hospital of Xiamen
- Venue
- International Heart Journal
- Published
- 2020-09-29
- Volume
- 61
- Issue
- 5
- Pages
- 1034-1040
- ISSN
- 1349-2365 (ISSN-L)
- 1349-3299
- OpenAlex
- W3089593046
- Cited by
- 8
- References
- 27
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 3 · 2022: 1
- FWCI
- 0.41
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Locations
- International Heart Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Natural Science Foundation of Fujian Province (2018D0022)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Keywords
- USP16, LDL receptor, deubiquitination, protein stability, LDL uptake, LDLR degradation, atherosclerosis, atherogenic lipoproteins, coronary artery disease
- MeSH terms
- HeLa Cells, Humans, Lipoproteins, LDL, Protein Processing, Post-Translational, Receptors, LDL, Ubiquitin Thiolesterase, Ubiquitination
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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.
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