Evidence map›Paper›PMID 37333304›Full record

ArticlebioRxiv : the preprint server for biology2023

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 readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed, 8 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 3 institutions in 1 country.

Daniel J BoeschRoy J. Carver Department of Biochemistry, Biophysics & Molecular Biology, Iowa State University, 2437 Pammel Drive, Ames, IA 50011, USA.
Amika SinglaDepartment of Internal Medicine, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
Yan HanDepartment of Biophysics, University of Texas Southwestern Medical Center, 6001 Forest Park Road, Dallas, TX 75390, USA.
Daniel A KramerRoy J. Carver Department of Biochemistry, Biophysics & Molecular Biology, Iowa State University, 2437 Pammel Drive, Ames, IA 50011, USA.
Qi LiuDepartment of Internal Medicine, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
Kohei SuzukiDepartment of Internal Medicine, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
Puneet JunejaCryo-EM facility, Office of Biotechnology, Iowa State University, 2437 Pammel Drive, Ames, IA 50011, USA.
Xuefeng ZhaoResearch IT, College of Liberal Arts and Sciences, Iowa State University, 2415 Osborn Dr, Ames, IA 50011, USA.
Xin LongDepartment of Internal Medicine, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
Michael J MedlynDivision of Oncology Research, College of Medicine, Mayo Clinic, Rochester MN, 55905, USA.
Daniel D BilladeauDivision of Oncology Research, College of Medicine, Mayo Clinic, Rochester MN, 55905, USA.
Zhe ChenDepartment of Biophysics, University of Texas Southwestern Medical Center, 6001 Forest Park Road, Dallas, TX 75390, USA.
Baoyu ChenRoy J. Carver Department of Biochemistry, Biophysics & Molecular Biology, Iowa State University, 2437 Pammel Drive, Ames, IA 50011, USA.
Ezra BursteinDepartment of Molecular Biology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
The University of Texas Southwestern Medical Center · USIowa State University · USMayo Clinic · US

Funding

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
NIDDK 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 VPS35L, VPS26C and VPS29, together with the CCC complex comprising CCDC22, CCDC93, and 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 the first high-resolution structure of Retriever 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 and uncover how cancer-associated mutations 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

CCC complexCCDC22CCDC93CommanderCOMMDEndosome recyclingRetrieverRetromerVPS26CVPS29VPS35L

Identifiers

PMID37333304
PMCPMC10274727
OpenAlexW4379797696

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.