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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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CPAP is a cell-cycle regulated protein that controls centriole length
Chieh-Ju C Tang1, Ru-Huei Fu, Kuo-Sheng Wu
1Institute of Biomedical Sciences, Taipei, Taiwan.
Nature Cell Biology
|June 9, 2009
Summary
Centrosome duplication relies on centriole elongation. This study reveals centrosomal P4.1-associated protein (CPAP) regulates centriole length, with its tubulin-binding activity essential for progeny centriole growth.
Area of Science:
- Cell Biology
- Molecular Biology
- Structural Biology
Background:
- Centriole duplication is fundamental for cell division and ciliogenesis.
- The molecular mechanisms governing procentriole elongation are not fully understood.
- Centrosomal P4.1-associated protein (CPAP) is a key component of the centriole.
Purpose of the Study:
- To investigate the role of CPAP in regulating procentriole elongation.
- To elucidate the molecular mechanisms underlying CPAP-mediated centriole length control.
Main Methods:
- Cell cycle analysis of CPAP expression and localization.
- Depletion and overexpression studies of CPAP in human cells.
- Ultrastructural analysis of centrioles and procentriole-like structures (PLSs).
- Biochemical assays to assess CPAP's interaction with tubulin.
Main Results:
- CPAP expression is cell cycle-regulated and degraded during mitosis.
- CPAP depletion inhibits centrosome duplication.
- CPAP overexpression induces the formation of elongated PLSs containing stable microtubules.
- A CPAP mutant unable to bind tubulin impairs PLS formation.
Conclusions:
- CPAP is a novel regulator of centriole length.
- CPAP's intrinsic tubulin-dimer binding activity is crucial for procentriole elongation.
- CPAP plays a critical role in controlling the length of newly forming centrioles.
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