BRAM1, a BMP receptor-associated molecule involved in BMP signalling.

BACKGROUND: TGF-beta superfamily members elicit signals through the stimulation of serine/threonine-kinase receptors. Recently, molecules associated with several TGF-beta family receptors have been cloned. One such molecule, the immunophilin FKBP12, has been reported to interact with TGF-beta family type I receptors. However, the identity of signalling specific molecules interacting with the ...
receptor was unknown. RESULTS: To clarify the factors mediating bone morphogenetic protein (BMP) receptor signalling, a cytoplasmic molecule associated with the BMP type IA receptor (BMPR-IA) was isolated using the yeast two-hybrid system. We designated the molecule BMP receptor associated molecule 1 (BRAM1). BRAM1 is an alternatively spliced form of BS69, a factor previously identified as an adenovirus E1A-associated protein. BRAM1 was localized to the cytoplasmic region in mammalian cells, whereas BS69 is localized to the nucleus. BRAM1 bound specifically to BMPR-IA in mammalian cells. The C-terminal half of BRAM1 was found to be sufficient for binding to BMPR-IA. CONCLUSIONS: BRAM1, a BMPR-IA associated molecule, was isolated using the yeast two-hybrid system, and found to associate specifically with BMPR-IA. BRAM1 may thus serve as an interacting protein in the BMP signal pathway.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Alternative Splicing, Bone Morphogenetic Protein Receptors, Type I, Bone Morphogenetic Proteins, Carrier Proteins, Cell Compartmentation, Cloning, Molecular, DNA, Complementary, Humans, Intracellular Signaling Peptides and Proteins, Peptide Fragments, Protein Binding, Protein-Serine-Threonine Kinases, Receptors, Growth Factor, Saccharomyces cerevisiae, Signal Transduction, Tissue Distribution, Transforming Growth Factor beta
Genes Cells
Date: Apr. 01, 1998
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