Evidence map›Paper›PMID 27827364›Full record

ArticleNature communications2016

Structural and mechanistic insights into regulation of the retromer coat by TBC1d5.

Da Jia, Jin-San Zhang, Fang Li, Jing Wang, Zhihui Deng, Mark A White, Douglas G Osborne, Christine Phillips-Krawczak, Timothy S Gomez, Haiying Li and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

73 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. VPS29C: Adding complexity to the Retromer complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Identification of a VPS29 isoform with restricted association to Retriever and Retromer accessory proteins through autoinhibition.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Structural basis for coupling of the WASH subunit FAM21 with the endosomal SNX27-Retromer complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

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

14 authors at 8 institutions in 2 countries.

Da JiaKey Laboratory of Birth Defects and Related Diseases of Women and Children (Ministry of Education), Department of Paediatrics, West China Second University Hospital and State Key Laboratory of Biotherapy, Sichuan University, Chengdu 610041, China.
Jin-San ZhangDepartments of Immunology, Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Mayo Clinic, Rochester, Minnesota 55905, USA.
Fang LiKey Laboratory of Birth Defects and Related Diseases of Women and Children (Ministry of Education), Department of Paediatrics, West China Second University Hospital and State Key Laboratory of Biotherapy, Sichuan University, Chengdu 610041, China.
Jing WangKey Laboratory of Birth Defects and Related Diseases of Women and Children (Ministry of Education), Department of Paediatrics, West China Second University Hospital and State Key Laboratory of Biotherapy, Sichuan University, Chengdu 610041, China.
Zhihui DengDepartments of Immunology, Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Mayo Clinic, Rochester, Minnesota 55905, USA.
Mark A WhiteSealy Center for Structural Biology, University of Texas Medical Branch, Galveston, Texas 77555, USA.
Douglas G OsborneDepartments of Immunology, Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Mayo Clinic, Rochester, Minnesota 55905, USA.
Christine Phillips-KrawczakDepartments of Immunology, Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Mayo Clinic, Rochester, Minnesota 55905, USA.
Timothy S GomezDepartments of Immunology, Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Mayo Clinic, Rochester, Minnesota 55905, USA.
Haiying LiDepartment of Internal Medicine, UT Southwestern Medical Center, Dallas, Texas 75390, USA.
Amika SinglaDepartment of Internal Medicine, UT Southwestern Medical Center, Dallas, Texas 75390, USA.
Ezra BursteinDepartment of Internal Medicine, UT Southwestern Medical Center, Dallas, Texas 75390, USA.
Daniel D BilladeauDepartments of Immunology, Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Mayo Clinic, Rochester, Minnesota 55905, USA.
Michael K RosenDepartment of Biophysics, UT Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390, USA.
Mayo Clinic · USState Key Laboratory of BiotherapyThe University of Texas Southwestern Medical Center · USHoward Hughes Medical Institute · USSichuan University · CNSouthwestern Medical CenterThe University of Texas Medical Branch at Galveston · USWenzhou Medical University · CN

Funding

Women's Cancer ProgramP30CA015083 · NCI · MAYO CLINIC ROCHESTER · PI Felicity Enders · 1985 to 2026
$151.3M
STRUCTURAL STUDY OF RHO-GTPASE REGULATORS AND EFFECTORSR01GM056322 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ROSEN, MICHAEL K · 1997 to 2019
$5.7M
Regulation of Nutrient Homeostasis by COMMD proteinsR01DK107733 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI DANIEL D BILLADEAU, Ezra Burstein · 2016 to 2026
$4.6M
Role of the CCC complex in immune functionR01DK073639 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI BURSTEIN, EZRA · 2007 to 2020
$3.7M
Regulation of Actin Dynamics During T Cell ActivationR01AI065474 · NIAID · MAYO CLINIC ROCHESTER · PI BILLADEAU, DANIEL D · 2005 to 2014
$3.1M
NCI NIH HHS P30 CA015083NIAID NIH HHS R01 AI065474NIDDK NIH HHS R01 DK073639NIDDK NIH HHS R01 DK107733NIGMS NIH HHS R01 GM056322
6 · The paper itself

Abstract

Retromer is a membrane coat complex that is recruited to endosomes by the small GTPase Rab7 and sorting nexin 3. The timing of this interaction and consequent endosomal dynamics are thought to be regulated by the guanine nucleotide cycle of Rab7. Here we demonstrate that TBC1d5, a GTPase-activating protein (GAP) for Rab7, is a high-affinity ligand of the retromer cargo selective complex VPS26/VPS29/VPS35. The crystal structure of the TBC1d5 GAP domain bound to VPS29 and complementary biochemical and cellular data show that a loop from TBC1d5 binds to a conserved hydrophobic pocket on VPS29 opposite the VPS29-VPS35 interface. Additional data suggest that a distinct loop of the GAP domain may contact VPS35. Loss of TBC1d5 causes defective retromer-dependent trafficking of receptors. Our findings illustrate how retromer recruits a GAP, which is likely to be involved in the timing of Rab7 inactivation leading to membrane uncoating, with important consequences for receptor trafficking.

Indexed as

Crystallography, X-RayEndosomesGTPase-Activating ProteinsHEK293 CellsHeLa CellsHumansProtein BindingProtein Transportrab GTP-Binding ProteinsVesicular Transport ProteinsGTPase-Activating Proteinsrab GTP-Binding ProteinsTBC1D5 protein, humanVesicular Transport Proteins

Identifiers

PMID27827364
PMCPMC5105194
OpenAlexW2550537208

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.