Evidence map›Paper›PMID 40448120›Full record

ArticleBMC medical genomics2025

CCDC22 mutations that impair COMMD binding cause attenuated 3C/Ritscher-Schinzel syndrome.

Amika Singla, Carolyn Rogers, Mary-Joe Touma, Yassin El-Najjar, Alison Colley, Daniel J Boesch, Daniel D Billadeau, Jozef Gecz, Baoyu Chen, Ezra Burstein

Abstract read
In one paragraph

Article in BMC medical genomics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

10 authors.

Amika SinglaDepartment of Internal Medicine, Division of Digestive and Liver Diseases, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Carolyn RogersGenetics of Learning Disability Service, Hunter Genetics, Waratah, NSW, Australia.
Mary-Joe ToumaDepartment of Internal Medicine, Division of Digestive and Liver Diseases, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Yassin El-NajjarDepartment of Internal Medicine, Division of Digestive and Liver Diseases, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Alison ColleyGenetics of Learning Disability Service, Hunter Genetics, Waratah, NSW, Australia.
Daniel J BoeschRoy J. Carver Department of Biochemistry, Biophysics & Molecular Biology, Iowa State University, Ames, IA, USA.
Daniel D BilladeauDivision of Oncology Research, Mayo Clinic College of Medicine, Rochester, MN, USA.
Jozef GeczNeurogenetics Research Program, School of Pediatrics and Reproductive Health, University of Adelaide, Adelaide, Australia.
Baoyu ChenRoy J. Carver Department of Biochemistry, Biophysics & Molecular Biology, Iowa State University, Ames, IA, USA.
Ezra BursteinDepartment of Internal Medicine, Division of Digestive and Liver Diseases, University of Texas Southwestern Medical Center, Dallas, TX, USA. ezra.burstein@utsouthwestern.edu.

Funding

UT Southwestern NORCP30DK127984 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI Jeffrey M Zigman · 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
National Science Foundation CDF 2047640NHLBI NIH HHS R01 HL179813NIDDK NIH HHS P30 DK127984NIDDK NIH HHS R01 DK107733NIGMS NIH HHS R35 GM128786NIH HHS R01 DK107733NIH HHS R35 GM128786
6 · The paper itself

Abstract

The CCC complex, composed of CCDC22, CCDC93, and ten proteins of the COMMD family, coordinates several critical steps required to recycle internalized plasma membrane proteins from endosomes to the cell surface. CCC interacts with Retriever, a trimeric cargo recognition complex comprising VPS35L, VPS26C, and VPS29, and works closely with the WASH complex, a crucial regulator of branched actin polymerization at endosomal membranes. Mutations in genes encoding subunits of these three complexes, CCDC22, VPS35L, and WASHC5, have been linked with a developmental syndrome known as 3 C (cranio-cerebello-cardiac) or Ritscher-Schinzel syndrome. Here, we report a new CCDC22 missense mutation, p.E208K, that results in attenuated 3 C syndrome, without cardiac or neuroanatomical abnormalities. We show that this mutation impairs CCC complex assembly by disrupting a conserved interaction surface required for CCDC22-COMMD4 binding. We also review previously described cases and identify that CCDC22 p.P172R has a similar attenuated phenotype and impairs complex assembly in a similar fashion as p.E208K. The characterization of these mutations adds to our understanding of the clinical and molecular spectrum of these disorders.

Indexed as

Abnormalities, MultipleAdaptor Proteins, Signal TransducingMutationMutation, MissenseFemaleHumansMaleProtein BindingAdaptor Proteins, Signal Transducing3 C syndromeCCDC22COMMD proteinRetrieverRitscher-Schinzel syndrome

Identifiers

PMID40448120
PMCPMC12125813

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.