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Updated: Jan 13, 2026
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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
Published on: August 13, 2012
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PDCD5 promotes substrate release from the TRiC complex in cilia and flagella
Huafang Wei1, Qianqian Song2, Liying Wang1
1Guangzhou Women and Children's Medical Center, Sino-French Hoffmann Institute, Guangzhou Medical University, Guangzhou 510623, China.
Molecular Cell
|January 8, 2026
Summary
Programmed cell death 5 (PDCD5) is essential for flagellum and cilium formation. PDCD5 regulates the TRiC/CCT complex, ensuring proper protein release for these structures.
Area of Science:
- Cell Biology
- Structural Biology
- Molecular Chaperones
Background:
- The TRiC/CCT complex, a crucial molecular chaperone in eukaryotes, folds approximately 10% of cellular proteins.
- Interaction between TRiC/CCT and programmed cell death 5 (PDCD5) has been observed, but its physiological significance is unclear.
Purpose of the Study:
- To elucidate the physiological role of the PDCD5-TRiC/CCT interaction.
- To determine the structural basis of PDCD5 binding to the open state of TRiC/CCT.
- To understand how PDCD5 influences protein folding and release by TRiC/CCT.
Main Methods:
- Near-atomic resolution cryo-electron microscopy (cryo-EM) to determine PDCD5-TRiC/CCT complex structures.
- Biochemical assays to investigate the competition between PDCD5 and PhLP2A for TRiC/CCT binding.
- Depletion studies in mouse models to assess the impact on flagellum and cilium formation.
Main Results:
- PDCD5 is indispensable for flagellum biogenesis and ciliogenesis.
- Structural analysis revealed PDCD5 binding to the open state of TRiC/CCT.
- PDCD5 facilitates substrate release from TRiC/CCT by outcompeting PhLP2A.
- PDCD5 depletion leads to malformed flagella and cilia due to trapped proteins.
Conclusions:
- PDCD5 acts as a regulator of the TRiC/CCT complex, promoting the release of specific substrates.
- The interaction of PDCD5 with TRiC/CCT, particularly via its C-terminus, is critical for flagellum and cilium development.
- These findings highlight a novel function of PDCD5 in protein homeostasis and cellular structure formation.
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