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Expression of multiple UNC-13 proteins in the Caenorhabditis elegans nervous system.


ABSTRACT: The Caenorhabditis elegans UNC-13 protein and its mammalian homologues are important for normal neurotransmitter release. We have identified a set of transcripts from the unc-13 locus in C. elegans resulting from alternative splicing and apparent alternative promoters. These transcripts encode proteins that are identical in their C-terminal regions but that vary in their N-terminal regions. The most abundant protein form is localized to most or all synapses. We have analyzed the sequence alterations, immunostaining patterns, and behavioral phenotypes of 31 independent unc-13 alleles. Many of these mutations are transcript-specific; their phenotypes suggest that the different UNC-13 forms have different cellular functions. We have also isolated a deletion allele that is predicted to disrupt all UNC-13 protein products; animals homozygous for this null allele are able to complete embryogenesis and hatch, but they die as paralyzed first-stage larvae. Transgenic expression of the entire gene rescues the behavior of mutants fully; transgenic overexpression of one of the transcripts can partially compensate for the genetic loss of another. This finding suggests some degree of functional overlap of the different protein products.

SUBMITTER: Kohn RE 

PROVIDER: S-EPMC15005 | biostudies-literature | 2000 Oct

REPOSITORIES: biostudies-literature

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Expression of multiple UNC-13 proteins in the Caenorhabditis elegans nervous system.

Kohn R E RE   Duerr J S JS   McManus J R JR   Duke A A   Rakow T L TL   Maruyama H H   Moulder G G   Maruyama I N IN   Barstead R J RJ   Rand J B JB  

Molecular biology of the cell 20001001 10


The Caenorhabditis elegans UNC-13 protein and its mammalian homologues are important for normal neurotransmitter release. We have identified a set of transcripts from the unc-13 locus in C. elegans resulting from alternative splicing and apparent alternative promoters. These transcripts encode proteins that are identical in their C-terminal regions but that vary in their N-terminal regions. The most abundant protein form is localized to most or all synapses. We have analyzed the sequence alterat  ...[more]

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