Cited by 235Tuberous Sclerosis Complex ResearchPI3K/AKT/mTOR signaling in cancerTGF-β signaling in diseases

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

TSC1 Stabilizes TSC2 by Inhibiting the Interaction between TSC2 and the HERC1 Ubiquitin Ligase

Open access
Chong-Kopera, Huira, Inoki, Ken, Li, Yong, Zhu, Tianqing, Garcia-Gonzalo, Francesc R., Rosa, Jose Luis, Guan, Kun-Liang·2006·Journal of Biological Chemistry

Abstract

Tuberous sclerosis complex (TSC) is an autosomal dominant disease characterized by hamartoma formation in various organs. Two genes responsible for the disease, TSC1 and TSC2, have been identified. The TSC1 and TSC2 proteins, also called hamartin and tuberin, respectively, have been shown to regulate cell growth through inhibition of the mammalian target of rapamycin pathway. TSC1 is known to stabilize TSC2 by forming a complex with TSC2, which is a GTPase-activating protein for the Rheb small GTPase. We have identified HERC1 as a TSC2-interacting protein. HERC1 is a 532-kDa protein with an E3 ubiquitin ligase homology to E6AP carboxyl terminus (HECT) domain. We observed that the interaction of TSC1 with TSC2 appears to exclude TSC2 from interacting with HERC1. Disease mutations in TSC2, which result in its destabilization, allow binding to HERC1 in the presence of TSC1. Our study reveals a potential molecular mechanism of how TSC1 stabilizes TSC2 by excluding the HERC1 ubiquitin ligase from the TSC2 complex. Furthermore, these data reveal a possible biochemical basis of how certain disease mutations inactivate TSC2.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1074/jbc.c500451200

Cites

30 of 30 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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

Show all 30 references

Research works printed but not linked: 1

  1. Zhang, 2003, J. Clin. Invest., 112, 1223, 10.1172/JCI200317222 · DOI

Cited by

Sorted by citations

Metadata

Authors
Chong-Kopera, H., Inoki, K., Li, Y., Zhu, T., Garcia-Gonzalo, F. R., Rosa, J. L., & Guan, K.-L.
Affiliations
University of Michigan (US)
Corresponding author
Guan, Kun-Liang
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2006-03
Volume
281
Issue
13
Pages
8313-8316
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1984412362
Cited by
234
References
30
Citations by year
2026: 9 · 2025: 9 · 2024: 4 · 2023: 6 · 2022: 10 · 2021: 13 · 2020: 11 · 2019: 6 · 2018: 11 · 2017: 14 · 2016: 18 · 2015: 7 · 2014: 11 · 2013: 12 · 2012: 21
FWCI
10.19
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Dipòsit Digital de la Universitat de Barcelona (Universitat de Barcelona) (submittedVersion, public-domain)
Funders
  • National Institute on Aging (T32-AG00114-18, T32AG000114)
  • National Institute of Diabetes and Digestive and Kidney Diseases (R01DK124709)
Topics
  • Health Sciences › Medicine › Genetics (clinical) › Tuberous Sclerosis Complex Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Keywords
tuberous sclerosis complex, TSC1, TSC2, hamartin, tuberin, HERC1, E3 ubiquitin ligase, protein-protein interaction, protein stabilization, HECT domain, pathogenic variants, mTOR signaling, hamartoma
MeSH terms
Tuberous Sclerosis Complex 1 Protein, Tuberous Sclerosis Complex 2 Protein, Amino Acid Sequence, Animals, Brain Chemistry, Cell Extracts, Cell Line, Cycloheximide, Humans, Ligases, Precipitin Tests, Protein Synthesis Inhibitors, Blotting, Western, Silver Staining, Gene Deletion, Protein Structure, Tertiary, Guanine Nucleotide Exchange Factors, Protein Subunits, Tumor Suppressor Proteins, Ubiquitin, Ubiquitin-Protein Ligases, Mice

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