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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
Published on: October 20, 2014
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CCDC32 stabilizes clathrin-coated pits and drives their invagination
Ziyan Yang1, Changsong Yang2, Zheng Huang1
1NHC 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.
Elife
|January 5, 2026
Summary
CCDC32 is a novel protein crucial for clathrin-mediated endocytosis (CME) in mammalian cells. It stabilizes clathrin-coated pits (CCPs) and aids their invagination, essential for cellular homeostasis.
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- Clathrin-mediated endocytosis (CME) is vital for cellular homeostasis.
- Over 50 accessory proteins are known, but CCP invagination mechanisms are unclear.
Purpose of the Study:
- Investigate the role of CCDC32 in CME.
- Elucidate the mechanism of clathrin-coated pit (CCP) invagination.
Main Methods:
- Quantitative live cell imaging.
- siRNA-mediated knockdown of CCDC32.
- In vitro and cellular AP2 binding assays.
- Analysis of CCDC32 mutations.
Main Results:
- CCDC32 knockdown causes unstable, flat clathrin assemblies.
- CCDC32 interacts with AP2.
- A specific region (aa78-98) of CCDC32 is essential for AP2 binding and CME function.
- CCDC32 mutations causing CFNDS lack this critical region.
Conclusions:
- CCDC32 is a novel accessory protein regulating CCP stabilization and invagination.
- CCDC32's interaction with AP2 is critical for early CME stages.
- CCDC32 dysfunction is linked to cardio-facio-neuro-developmental syndrome (CFNDS).
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