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Subunit composition of the human cytoplasmic dynein-2 complex
David Asante1, Nicola L Stevenson1, David J Stephens2
1Cell Biology Laboratories, School of Biochemistry, Medical Sciences Building, University of Bristol, Bristol BS8 1TD, UK.
Journal of Cell Science
|September 11, 2014
Summary
Researchers defined the human cytoplasmic dynein-2 complex, revealing WDR34 and WDR60 as essential intermediate chains and TCTEX1D2 as a unique light chain crucial for cilia function and skeletal ciliopathies.
Area of Science:
- Cell Biology
- Molecular Motors
- Genetics
Background:
- Cytoplasmic dynein-2 motors retrograde intraflagellar transport (IFT).
- Mutations in dynein-2 are linked to skeletal ciliopathies.
- The precise composition of human cytoplasmic dynein-2 remains undefined.
Purpose of the Study:
- To elucidate the protein composition of the human cytoplasmic dynein-2 complex.
- To identify novel subunits and regulators of dynein-2.
- To understand the molecular basis of dynein-2-related ciliopathies.
Main Methods:
- Co-immunoprecipitation assays to identify protein interactions.
- Mass spectrometry to determine complex composition.
- Genetic analysis of ciliopathy genes WDR34, WDR60, and TCTEX1D2.
Main Results:
- WDR34 and WDR60 are identified as dynein-2 intermediate chains essential for its function.
- TCTEX1D2 is characterized as a unique dynein-2 light chain required for cilia function.
- Several common subunits with dynein-1 were identified, but key dynein-1 regulators (dynactin, LIS1, BICD2) do not associate with dynein-2.
Conclusions:
- The study defines the human cytoplasmic dynein-2 complex composition.
- WDR34 and WDR60 mutations explain disease in skeletal ciliopathies.
- TCTEX1D2 is identified as a novel candidate gene for ciliopathies.
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