N-linked glycosylation of the bone morphogenetic protein receptor type 2 (BMPR2) enhances ligand binding.

ABSTRACT: The bone morphogenetic protein (BMP) signaling pathway is essential for normal development and tissue homeostasis. BMP signal transduction occurs when ligands interact with a complex of type 1 and type 2 receptors to activate downstream transcription factors. It is well established that a single BMP receptor may bind multiple BMP ligands with varying affinity, and this has been largely attributed to conformation at the amino acid level. However, all three type 2 BMP receptors (BMPR2, ACVR2A/B) contain consensus N-glycosylation sites in their extracellular domains (ECDs), which could play a role in modulating interaction with ligand. Here, we show a differential pattern of N-glycosylation between BMPR2 and ACVR2A/B. Site-directed mutagenesis reveals that BMPR2 is uniquely glycosylated near

SUBMITTER: Lowery JW 

PROVIDER: S-EPMC4058410 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature