Evidence map›Paper›PMID 41489497›Full record

ArticleeLife2026

CCDC32 stabilizes clathrin-coated pits and drives their invagination.

Ziyan Yang, Changsong Yang, Zheng Huang, Peiliu Xu, Yueping Li, Lu Han, Linyuan Peng, Xiangying Wei, John E Pak, Tatyana Svitkina and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in eLife, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. VAMP8 function reveals tight linkage between endocytic recycling and endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Dynamic early recruitment of GAK-Hsc70 regulates coated pit maturation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Ziyan YangNHC Key Laboratory of Birth Defect Research and Prevention, MOE Key Laboratory of Rare Pediatric Diseases, Institute of Cytology and Genetics of School of Basic Medical Sciences & Department of Clinical Laboratory of The First Affiliated Hospital, Hengyang Medical School, University of South China, Hengyang, China.
Changsong YangDepartment of Biology, University of Pennsylvania, Philadelphia, United States.
Zheng HuangNHC Key Laboratory of Birth Defect Research and Prevention, MOE Key Laboratory of Rare Pediatric Diseases, Institute of Cytology and Genetics of School of Basic Medical Sciences & Department of Clinical Laboratory of The First Affiliated Hospital, Hengyang Medical School, University of South China, Hengyang, China.
Peiliu XuNHC Key Laboratory of Birth Defect Research and Prevention, MOE Key Laboratory of Rare Pediatric Diseases, Institute of Cytology and Genetics of School of Basic Medical Sciences & Department of Clinical Laboratory of The First Affiliated Hospital, Hengyang Medical School, University of South China, Hengyang, China.
Yueping LiNHC Key Laboratory of Birth Defect Research and Prevention, MOE Key Laboratory of Rare Pediatric Diseases, Institute of Cytology and Genetics of School of Basic Medical Sciences & Department of Clinical Laboratory of The First Affiliated Hospital, Hengyang Medical School, University of South China, Hengyang, China.
Lu HanNHC Key Laboratory of Birth Defect Research and Prevention, MOE Key Laboratory of Rare Pediatric Diseases, Institute of Cytology and Genetics of School of Basic Medical Sciences & Department of Clinical Laboratory of The First Affiliated Hospital, Hengyang Medical School, University of South China, Hengyang, China.
Linyuan PengNHC Key Laboratory of Birth Defect Research and Prevention, MOE Key Laboratory of Rare Pediatric Diseases, Institute of Cytology and Genetics of School of Basic Medical Sciences & Department of Clinical Laboratory of The First Affiliated Hospital, Hengyang Medical School, University of South China, Hengyang, China.
Xiangying WeiFuzhou Institute of Oceanography, College of Geography and Oceanography, Minjiang University, Fuzhou, China.
John E PakChan Zuckerberg Biohub, San Francisco, United States.
Tatyana SvitkinaDepartment of Biology, University of Pennsylvania, Philadelphia, United States.
Sandra L SchmidChan Zuckerberg Biohub, San Francisco, United States.ORCID https://orcid.org/0000-0002-1690-7024
Zhiming ChenNHC Key Laboratory of Birth Defect Research and Prevention, MOE Key Laboratory of Rare Pediatric Diseases, Institute of Cytology and Genetics of School of Basic Medical Sciences & Department of Clinical Laboratory of The First Affiliated Hospital, Hengyang Medical School, University of South China, Hengyang, China.ORCID https://orcid.org/0000-0002-2423-101X

Funding

Request for administrative supplement to Parent R01 GM073165 entitled "Mechanisms regulating clathrin-mediated endocytosis"R01GM073165 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI METTLEN, MARCEL BERNARD · 2006 to 2022
$6.8M
Structure and functions of the actin cytoskeletonR35GM140832 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Tatyana Svitkina · 2021 to 2026
$2.8M
National Natural Science Foundation of China 32200564Natural Science Foundation of Hunan Province 2024JJ2045NIGMS NIH HHS R01 GM073165NIGMS NIH HHS R35 GM140832NIH HHS GM73165NIH HHS R35 GM140832
6 · The paper itself

Abstract

Clathrin-mediated endocytosis (CME) is essential for maintaining homeostasis in mammalian cells. Previous studies have reported more than 50 CME accessory proteins; however, the mechanism driving the invagination of clathrin-coated pits (CCPs) remains elusive. We show by quantitative live cell imaging that siRNA-mediated knockdown of CCDC32, a poorly characterized endocytic accessory protein, leads to the accumulation of unstable flat clathrin assemblies. CCDC32 interacts with the α-appendage domain (AD) of AP2 in vitro and with full-length AP2 complexes in cells. Deletion of aa78-98 in CCDC32, corresponding to a predicted α-helix, abrogates AP2 binding and CCDC32's early function in CME. Furthermore, clinically observed nonsense mutations in CCDC32, which result in C-terminal truncations that lack aa78-98, are linked to the development of cardio-facio-neuro-developmental syndrome (CFNDS). Overall, our data demonstrate the function of a novel endocytic accessory protein, CCDC32, in regulating CCP stabilization and invagination, critical early stages of CME.

Indexed as

ClathrinCoated Pits, Cell-MembraneEndocytosisAdaptor Protein Complex 2AnimalsHumansProtein BindingAdaptor Protein Complex 2ClathrinCCDC32cell biologyCFNDSclathrin-coated pitsclathrin-mediated endocytosisE. coliflat clathrin assembliesin vitro

Identifiers

PMID41489497
PMCPMC12768407

What OpenQuestion holds

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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.