[PDF][PDF] CDC-42 controls early cell polarity and spindle orientation in C. elegans
M Gotta, MC Abraham, J Ahringer - Current biology, 2001 - cell.com
M Gotta, MC Abraham, J Ahringer
Current biology, 2001•cell.comBackground: Generation of asymmetry in the one-cell embryo of C. elegans establishes the
anterior–posterior axis (AP), and is necessary for the proper identity of early blastomeres.
Conserved PAR proteins are asymmetrically distributed and are required for the generation
of this early asymmetry. The small G protein Cdc42 is a key regulator of polarity in other
systems, and recently it has been shown to interact with the mammalian homolog of PAR-6.
The function of Cdc42 in C. elegans had not yet been investigated, however. Results: Here …
anterior–posterior axis (AP), and is necessary for the proper identity of early blastomeres.
Conserved PAR proteins are asymmetrically distributed and are required for the generation
of this early asymmetry. The small G protein Cdc42 is a key regulator of polarity in other
systems, and recently it has been shown to interact with the mammalian homolog of PAR-6.
The function of Cdc42 in C. elegans had not yet been investigated, however. Results: Here …
Abstract
Background: Generation of asymmetry in the one-cell embryo of C. elegans establishes the anterior–posterior axis (A-P), and is necessary for the proper identity of early blastomeres. Conserved PAR proteins are asymmetrically distributed and are required for the generation of this early asymmetry. The small G protein Cdc42 is a key regulator of polarity in other systems, and recently it has been shown to interact with the mammalian homolog of PAR-6. The function of Cdc42 in C. elegans had not yet been investigated, however.
Results: Here, we show that C. elegans cdc-42 plays an essential role in the polarity of the one-cell embryo and the proper localization of PAR proteins. Inhibition of cdc-42 using RNA interference results in embryos with a phenotype that is nearly identical to par-3, par-6, and pkc-3 mutants, and asymmetric localization of these and other PAR proteins is lost. We further show that C. elegans CDC-42 physically interacts with PAR-6 in a yeast two-hybrid system, consistent with data on the interaction of human homologs.
Conclusions: Our results show that CDC-42 acts in concert with the PAR proteins to control the polarity of the C. elegans embryo, and provide evidence that the interaction of CDC-42 and the PAR-3/PAR-6/PKC-3 complex has been evolutionarily conserved as a functional unit.
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