Abstract
We have identified homologs of a human BMP receptor-associated molecule BRAM1 in Caenorhabditis elegans. One of them, BRA-1, has been found to bind DAF-1, the type I receptor in the DAF-7 transforming growth factor-beta pathway through the conserved C-terminal region. As analyzed using a BRA-1GFP (green fluorescent protein) fusion gene product, the bra-1 gene is expressed in amphid neurons such as ASK, ASI, and ASG, where daf-1 is also expressed. A loss-of-function mutation in bra-1 exhibits robust suppression of the Daf-c phenotype caused by the DAF-7 pathway mutations. We propose that BRA-1 represents a novel class of receptor-associated molecules that negatively regulate transforming growth factor-beta pathways.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Amino Acid Sequence
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Animals
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Artificial Gene Fusion
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Base Sequence
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Binding Sites
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COS Cells
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Caenorhabditis elegans / genetics
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Caenorhabditis elegans / metabolism
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Caenorhabditis elegans / physiology
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Caenorhabditis elegans Proteins*
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Chlorocebus aethiops
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Conserved Sequence
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DNA, Helminth
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Green Fluorescent Proteins
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Helminth Proteins / genetics
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Helminth Proteins / metabolism*
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Humans
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Luminescent Proteins / genetics
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Molecular Sequence Data
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Neurons / metabolism
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / metabolism*
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Signal Transduction / physiology*
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Transforming Growth Factor beta / metabolism*
Substances
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Adaptor Proteins, Signal Transducing
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BRA-1 protein, C elegans
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Caenorhabditis elegans Proteins
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Carrier Proteins
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DAF-1 protein, C elegans
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DAF-7 protein, C elegans
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DNA, Helminth
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Helminth Proteins
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Luminescent Proteins
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Receptors, Cell Surface
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Transforming Growth Factor beta
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Green Fluorescent Proteins