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Genes Cells. 1998 Apr;3(4):257-64.

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

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1
Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.

Abstract

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.

PMID:
9663660
[Indexed for MEDLINE]
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