Bone Morphogenetic Protein-6 Mutations Take Their Place in Iron Overload Diseases  Mark D. Kleven, Caroline A. Enns, An-Sheng Zhang  Gastroenterology  Volume 150, Issue 3, Pages 556-559 (March 2016) DOI: 10.1053/j.gastro.2016.01.016 Copyright © 2016 AGA Institute Terms and Conditions

Figure 1 Synthesis and processing of bone morphogenetic protein (BMP)6.1 BMP6 is inserted into the endoplasmic reticulum co-translationally, where it is glycosylated and its leader sequence is cleaved. Wild-type pro-BMP6 dimerizes and traffics from the endoplasmic reticulum through the Golgi and trans-Golgi network, where its sugar residues are further modified. Pro-BMP6 is then packaged into vesicles and secreted from the cell. In the extracellular matrix outside the cell the prodomain of BMP6 is cleaved creating the mature active form of BMP6. Daher et al1 show that mutations in the pro-domain of BMP6 prevent the efficient secretion of pro-BMP6. Both the mutant homodimers and the wild-type/mutant heterodimers are affected, thereby indicating that the mutation acts in a dominant manner. Gastroenterology 2016 150, 556-559DOI: (10.1053/j.gastro.2016.01.016) Copyright © 2016 AGA Institute Terms and Conditions