A DAF-1-binding protein BRA-1 is a negative regulator of DAF-7 TGF-β signaling
Author(s) -
Kiyokazu Morita,
Miho Shimizu,
Hiroshi Shibuyà,
Naoto Ueno
Publication year - 2001
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.111409798
Subject(s) - caenorhabditis elegans , biology , gene product , transforming growth factor beta , microbiology and biotechnology , signal transduction , phenotype , receptor , acvrl1 , transforming growth factor , gene , regulator , mutation , decay accelerating factor , fusion protein , genetics , gene expression , endoglin , recombinant dna , antibody , complement system , stem cell , cd34
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.
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