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PMID: 9165118 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The Groucho-like transcription factor UNC-37 functions with the neural specificity gene unc-4 to govern motor neuron identity in C. elegans.

Development (Cambridge, England) ·Vol. 124 ·No. 9 ·1997-05-00 ·Pages 1699-709

Pflugrad A, Meir JY, Barnes TM, Miller DM

Abstract

Groucho and Tup1 are members of a conserved family of WD repeat proteins that interact with specific transcription factors to repress target genes. Here we show that mutations in WD domains of the Groucho-like protein, UNC-37, affect a motor neuron trait that also depends on UNC-4, a homeodomain protein that controls neuronal specificity in Caenorhabditis elegans. In unc-4 mutants, VA motor neurons assume the pattern of synaptic input normally reserved for their lineal sister cells, the VB motor neurons; the loss of normal input to the VAs produces a distinctive backward movement defect. Substitution of a conserved residue (H to Y) in the fifth WD repeat in unc-37(e262) phenocopies the Unc-4 movement defect. Conversely, an amino acid change (E to K) in the sixth WD repeat of UNC-37 is a strong suppressor of unc-37(e262) and of specific unc-4 missense mutations. We have previously shown that UNC-4 expression in the VA motor neurons specifies the wild-type pattern of presynaptic input. Here we demonstrate that UNC-37 is also expressed in the VAs and that unc-37 activity in these neurons is sufficient to restore normal movement to unc-37(e262) animals. We propose that UNC-37 and UNC-4 function together to prevent expression of genes that define the VB pattern of synaptic inputs and thereby generate connections specific to the VA motor neurons. In addition, we show that the WD repeat domains of UNC-37 and of the human homolog, TLE1, are functionally interchangeable in VA motor neurons which suggests that this highly conserved protein domain may also specify motor neuron identity and synaptic choice in more complex nervous systems.

MeSH Terms
Alleles Amino Acid Sequence Animals Animals, Genetically Modified Base Sequence Caenorhabditis elegans/genetics,physiology Caenorhabditis elegans Proteins Co-Repressor Proteins Conserved Sequence Genes, Helminth Helminth Proteins/biosynthesis,chemistry,physiology Homeodomain Proteins Humans Interneurons/cytology,physiology Molecular Sequence Data Motor Neurons/cytology,physiology Movement Muscle Proteins/biosynthesis,chemistry,physiology Mutagenesis, Site-Directed Nervous System Physiological Phenomena Nuclear Proteins/chemistry Protein Structure, Secondary Recombinant Fusion Proteins/biosynthesis,chemistry Repressor Proteins Sequence Homology, Amino Acid Synapses/physiology Transcription Factors/biosynthesis,chemistry,physiology
Chemicals
Caenorhabditis elegans Proteins Co-Repressor Proteins Helminth Proteins Homeodomain Proteins Muscle Proteins Nuclear Proteins Recombinant Fusion Proteins Repressor Proteins TLE1 protein, human Transcription Factors unc-37 protein, C elegans unc-4 protein, C elegans
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Pflugrad A
Department of Cell Biology, Vanderbilt University Medical Center, Nashville, TN 37232-2175, USA.
Meir J Y
Barnes T M
Miller D M
Article Info
Journal
Development (Cambridge, England)
Abbr.
Development
ISSN
0950-1991
Published
1997-05-00
Pages
1699-709
Language
English
Region
England
NLM ID
8701744
Subset
IM
Grants
NINDS NIH HHS · R01NS26115 · United States
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