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Humans

Faculty Publications and Research

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Full-Text Articles in Cell Biology

N-Linked Glycosylation Of The Bone Morphogenetic Protein Receptor Type 2 (Bmpr2) Enhances Ligand Binding, Jonathan W. Lowery Ph.D., Jose M Amich, Alex Andonian, Vicki Rosen Aug 2014

N-Linked Glycosylation Of The Bone Morphogenetic Protein Receptor Type 2 (Bmpr2) Enhances Ligand Binding, Jonathan W. Lowery Ph.D., Jose M Amich, Alex Andonian, Vicki Rosen

Faculty Publications and Research

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 ...


Abnormal Trafficking Of Endogenously Expressed Bmpr2 Mutant Allelic Products In Patients With Heritable Pulmonary Arterial Hypertension, Andrea L Frump, Jonathan W. Lowery Ph.D., Rizwan Hamid, Eric D Austin, Mark De Caestecker Jan 2013

Abnormal Trafficking Of Endogenously Expressed Bmpr2 Mutant Allelic Products In Patients With Heritable Pulmonary Arterial Hypertension, Andrea L Frump, Jonathan W. Lowery Ph.D., Rizwan Hamid, Eric D Austin, Mark De Caestecker

Faculty Publications and Research

More than 200 heterozygous mutations in the type 2 BMP receptor gene, BMPR2, have been identified in patients with Heritable Pulmonary Arterial Hypertension (HPAH). More severe clinical outcomes occur in patients with BMPR2 mutations by-passing nonsense-mediated mRNA decay (NMD negative mutations). These comprise 40% of HPAH mutations and are predicted to express BMPR2 mutant products. However expression of endogenous NMD negative BMPR2 mutant products and their effect on protein trafficking and signaling function have never been described. Here, we characterize the expression and trafficking of an HPAH-associated NMD negative BMPR2 mutation that results in an in-frame deletion of BMPR2 EXON2 ...