Evidence map›Paper›PMID 38062209›Full record

ArticleNature structural & molecular biology2024

Structural organization of the retriever-CCC endosomal recycling complex.

Daniel J Boesch, Amika Singla, Yan Han, Daniel A Kramer, Qi Liu, Kohei Suzuki, Puneet Juneja, Xuefeng Zhao, Xin Long, Michael J Medlyn and 4 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
10.6field-weighted citation impact, top 1% 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

33 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Review
  3. Identification of the Down Syndrome Critical Region 3 Gene as a Mammalian Cell Size Regulator.Genes to cells : devoted to molecular & cellular mechanisms · 2026
    Article
  4. SNX3 exacerbates hepatic fibrosis by amplifying TGF-Acta pharmaceutica Sinica. B · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. VPS29C: Adding complexity to the Retromer complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. 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
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 1 country.

Daniel J Boesch *Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA.
Amika Singla *Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID http://orcid.org/0000-0002-9454-9111
Yan Han *Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID http://orcid.org/0000-0002-1207-7756
Daniel A KramerRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA.ORCID http://orcid.org/0000-0002-7159-9562
Qi LiuDepartment of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Kohei SuzukiDepartment of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Puneet JunejaCryo-EM Facility, Office of Biotechnology, Iowa State University, Ames, IA, USA.
Xuefeng ZhaoInformation Technology Services, Iowa State University, Ames, IA, USA.
Xin LongDepartment of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Michael J MedlynDivision of Oncology Research, College of Medicine, Mayo Clinic, Rochester, MN, USA.
Daniel D BilladeauDivision of Oncology Research, College of Medicine, Mayo Clinic, Rochester, MN, USA.
Zhe ChenDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA. zhe.chen@utsouthwestern.edu.ORCID http://orcid.org/0000-0002-1668-4051
Baoyu ChenRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA. stone@iastate.edu.ORCID http://orcid.org/0000-0002-6366-159X
Ezra BursteinDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA. ezra.burstein@utsouthwestern.edu.ORCID http://orcid.org/0000-0003-4341-6367
Iowa State University · USThe University of Texas Southwestern Medical Center · USMayo Clinic · USSouthwestern Medical Center · US

Funding

UT Southwestern NORCP30DK127984 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI Jeff G McDonald · 2022 to 2026
$7.4M
Regulation of Nutrient Homeostasis by COMMD proteinsR01DK107733 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI DANIEL D BILLADEAU, Ezra Burstein · 2016 to 2026
$4.6M
Signal Integration from Membranes to the Actin CytoskeletonR35GM128786 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI Baoyu Chen · 2018 to 2026
$3.6M
Cholesterol Regulation Through Retriever-Dependent LDL Receptor RecyclingR01HL179813 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI Ezra Burstein, Baoyu Chen · 2025 to 2026
$1.4M
NHLBI NIH HHS R01 HL179813NIDDK NIH HHS P30 DK127984NIDDK NIH HHS R01 DK107733NIGMS NIH HHS R35 GM128786
6 · The paper itself

Abstract

The recycling of membrane proteins from endosomes to the cell surface is vital for cell signaling and survival. Retriever, a trimeric complex of vacuolar protein-sorting-associated protein (VPS)35L, VPS26C and VPS29, together with the CCC complex comprising coiled-coil domain-containing (CCDC)22, CCDC93 and copper metabolism domain-containing (COMMD) proteins, plays a crucial role in this process. The precise mechanisms underlying retriever assembly and its interaction with CCC have remained elusive. Here, we present a high-resolution structure of retriever in humans determined using cryogenic electron microscopy. The structure reveals a unique assembly mechanism, distinguishing it from its remotely related paralog retromer. By combining AlphaFold predictions and biochemical, cellular and proteomic analyses, we further elucidate the structural organization of the entire retriever-CCC complex across evolution and uncover how cancer-associated mutations in humans disrupt complex formation and impair membrane protein homeostasis. These findings provide a fundamental framework for understanding the biological and pathological implications associated with retriever-CCC-mediated endosomal recycling.

Indexed as

Cryoelectron MicroscopyEndosomesCation Transport ProteinsHumansModels, MolecularMultiprotein ComplexesProtein ConformationVesicular Transport ProteinsCation Transport ProteinsMultiprotein ComplexesVesicular Transport Proteins

Identifiers

PMID38062209
PMCPMC11260360
OpenAlexW4389440027

What OpenQuestion holds

Textmetadata
LicenceTDM
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.