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Blood, 19 February 2009, Vol. 113, No. 8, pp. 1786-1793. Prepublished online as a Blood First Edition Paper on November 24, 2008; DOI 10.1182/blood-2008-08-174565. This Article Full Text Full Text (PDF) All Versions of this Article: blood-2008-08-174565v1 113/8/1786    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Maxson, J. E. Articles by Zhang, A.-S. Search for Related Content PubMed PubMed Citation Articles by Maxson, J. E. Articles by Zhang, A.-S. Related Collections Red Cells, Iron, and Erythropoiesis Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  RED CELLS, IRON, AND ERYTHROPOIESIS Processing of hemojuvelin requires retrograde trafficking to the Golgi in HepG2 cells Julia E. Maxson1, Caroline A. Enns1, and An-Sheng Zhang1 1 Department of Cell and Developmental Biology, Oregon Health & Science University, Portland Hemojuvelin (HJV) was recently identified as a critical regulator of iron homeostasis. It is either associated with cell membranes through a glycosylphosphatidylinositol anchor or released as a soluble form. Membrane-anchored HJV acts as a coreceptor for bone morphogenetic proteins and activates the transcription of hepcidin, a hormone that regulates iron efflux from cells. Soluble HJV antagonizes bone morphogenetic protein signaling and suppresses hepcidin expression. In this study, we examined the trafficking and processing of HJV. Cellular HJV reached the plasma membrane without obtaining complex oligosaccharides, indicating that HJV avoided Golgi processing. Secreted HJV, in contrast, has complex oligosaccharides and can be derived from HJV with high-mannose oligosaccharides at the plasma membrane. Our results support a model in which retrograde trafficking of HJV before cleavage is the predominant processing pathway. Release of HJV requires it to bind to the transmembrane receptor neogenin. Neogenin does not, however, play a role in HJV trafficking to the cell surface, suggesting that it could be involved either in retrograde trafficking of HJV or in cleavage leading to HJV release. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: E. B. Maryon, J. Zhang, J. W. Jellison, and J. H. Kaplan Human Copper Transporter 1 Lacking O-Linked Glycosylation Is Proteolytically Cleaved in a Rab9-positive Endosomal Compartment J. Biol. Chem., October 9, 2009; 284(41): 28104 - 28114. [Abstract] [Full Text] [PDF] A.-S. Zhang, F. Yang, J. Wang, H. Tsukamoto, and C. A. Enns Hemojuvelin-Neogenin Interaction Is Required for Bone Morphogenic Protein-4-induced Hepcidin Expression J. Biol. Chem., August 21, 2009; 284(34): 22580 - 22589. [Abstract] [Full Text] [PDF]

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