Evidence map›Paper›PMID 26893383›Full record

ArticleThe Journal of biological chemistry2016

Structural Basis of the Interaction between Tuberous Sclerosis Complex 1 (TSC1) and Tre2-Bub2-Cdc16 Domain Family Member 7 (TBC1D7).

Jiayue Qin, Zhizhi Wang, Marianne Hoogeveen-Westerveld, Guobo Shen, Weimin Gong, Mark Nellist, Wenqing Xu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. TSC2 is a stress granule suppressor.bioRxiv : the preprint server for biology · 2026
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  10. Frontiers in molecular neuroscience · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 3 countries.

Jiayue QinFrom the Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, the Department of Biological Structure, University of Washington, Seattle, Washington 98195, the University of Chinese Academy of Sciences, Beijing 100049, China.
Zhizhi Wangthe Department of Biological Structure, University of Washington, Seattle, Washington 98195.
Marianne Hoogeveen-Westerveldthe Department of Clinical Genetics, Erasmus Medical Center, 3015CN Rotterdam, The Netherlands, and.
Guobo Shenthe Department of Biological Structure, University of Washington, Seattle, Washington 98195.
Weimin GongFrom the Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, the Hefei National Laboratory for Physical Science at Microscale, University of Science and Technology of China, Hefei 230026, China wgong@ibp.ac.cn.
Mark Nellistthe Department of Clinical Genetics, Erasmus Medical Center, 3015CN Rotterdam, The Netherlands, and m.nellist@erasmusmc.nl.
Wenqing XuFrom the Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, the Department of Biological Structure, University of Washington, Seattle, Washington 98195, wxu@uw.edu.
University of Washington · USErasmus MC · NLHefei National Center for Physical Sciences at Nanoscale · CNInstitute of Biophysics · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations in TSC1 or TSC2 cause tuberous sclerosis complex (TSC), an autosomal dominant disorder characterized by the occurrence of benign tumors in various vital organs and tissues. TSC1 and TSC2, the TSC1 and TSC2 gene products, form the TSC protein complex that senses specific cellular growth conditions to control mTORC1 signaling. TBC1D7 is the third subunit of the TSC complex, and helps to stabilize the TSC1-TSC2 complex through its direct interaction with TSC1. Homozygous inactivation of TBC1D7 causes intellectual disability and megaencephaly. Here we report the crystal structure of a TSC1-TBC1D7 complex and biochemical characterization of the TSC1-TBC1D7 interaction. TBC1D7 interacts with the C-terminal region of the predicted coiled-coil domain of TSC1. The TSC1-TBC1D7 interface is largely hydrophobic, involving the α4 helix of TBC1D7. Each TBC1D7 molecule interacts simultaneously with two parallel TSC1 helices from two TSC1 molecules, suggesting that TBC1D7 may stabilize the TSC complex by tethering the C-terminal ends of two TSC1 coiled-coils.

Indexed as

Carrier ProteinsCrystallography, X-RayHumansIntracellular Signaling Peptides and ProteinsProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryTuberous Sclerosis Complex 1 ProteinTumor Suppressor ProteinsCarrier ProteinsIntracellular Signaling Peptides and ProteinsTBC1D7 protein, humanTSC1 protein, humanTuberous Sclerosis Complex 1 ProteinTumor Suppressor Proteinscrystal structureisothermal titration calorimetry (ITC)mTOR complex (mTORC)protein complexTBC1D7TSC1tuberous sclerosis complex (TSC)

Identifiers

PMID26893383
PMCPMC4861430
OpenAlexW2284424749

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.