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First published online 3 August 2006
doi: 10.1242/dev.02494

Development 133, 3317-3328 (2006)
Published by The Company of Biologists 2006
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An unusual Zn-finger/FH2 domain protein controls a left/right asymmetric neuronal fate decision in C. elegans

Robert J. Johnston, Jr1, John W. Copeland2, Marc Fasnacht1,3, John F. Etchberger1, Jun Liu4, Barry Honig1,3 and Oliver Hobert1,*

1 Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University Medical Center, 701 W. 168th Street, New York, NY 10032, USA.
2 Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada.
3 Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Center for Computational Biology and Bioinformatics, Columbia University Medical Center, 1130 St Nicholas Avenue, Room 815, New York, NY 10032, USA.
4 Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.

* Author for correspondence (e-mail: or38{at}columbia.edu)

Accepted 13 June 2006

Gene regulatory networks that control the terminally differentiated state of a cell are, by and large, only superficially understood. In a mutant screen aimed at identifying regulators of gene batteries that define the differentiated state of two left/right asymmetric C. elegans gustatory neurons, ASEL and ASER, we have isolated a mutant, fozi-1, with a novel mixed-fate phenotype, characterized by de-repression of ASEL fate in ASER. fozi-1 codes for a protein that functions in the nucleus of ASER to inhibit the expression of the LIM homeobox gene lim-6, neuropeptide-encoding genes and putative chemoreceptors of the GCY gene family. The FOZI-1 protein displays a highly unusual domain architecture, that combines two functionally essential C2H2 zinc-finger domains, which are probably involved in transcriptional regulation, with a formin homology 2 (FH2) domain, normally found only in cytosolic regulators of the actin cytoskeleton. We demonstrate that the FH2 domain of FOZI-1 has lost its actin polymerization function but maintains its phylogenetically ancient ability to homodimerize. fozi-1 genetically interacts with several transcription factors and micro RNAs in the context of specific regulatory network motifs. These network motifs endow the system with properties that provide insights into how cells adopt their stable terminally differentiated states.

Key words: Caenorhabditis elegans, Left/right asymmetry, Neuronal cell fate, Zn-finger transcription factor, FH2 domain




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