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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Constam, D. B. Robertson, E. J. |
| Description | Author Affiliation: Constam DB ( Harvard University, Department of Molecular and Cellular Biology, Cambridge, Massachusetts 02138, USA.) |
| Abstract | Bone morphogenetic proteins (BMPs) are derived from inactive precursor proteins by endoproteolytic cleavage. Here we show that processing of Nodal and Myc-tagged BMP4 is significantly enhanced by SPC1/Furin or SPC4/PACE4, providing direct evidence that regulation of BMP signaling is likely to be controlled by subtilisin-like proprotein convertase (SPC) activities. Nodal processing is dramatically enhanced if two residues adjacent to the precursor cleavage site are substituted with amino acids found at the equivalent positions of Activin, demonstrating that structural constraints at the precursor cleavage site limit the processing efficiency. However, in transfection assays, mature Nodal is undetectable either in culture supernatants or in cell lysates, despite efficient cleavage of the precursor protein, suggesting that mature Nodal is highly unstable. Domain swap experiments support this conclusion since mature BMP4 or Dorsalin are also destabilized when expressed in conjunction with the Nodal pro domain. By contrast, mature Nodal is stabilized by the Dorsalin pro domain, which mediates the formation of stable complexes. Collectively, these data show that the half-life of mature BMPs is greatly influenced by the identity of their pro regions. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 1 |
| Volume Number | 144 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1999-01-11 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bone Morphogenetic Proteins Metabolism Protein Precursors Serine Endopeptidases Subtilisins Transforming Growth Factor Beta Amino Acid Sequence Animals Binding Sites Bone Morphogenetic Protein 4 Genetics COS Cells Cell Line Disulfides Furin Mice Molecular Sequence Data Molecular Weight Mutagenesis Nodal Protein Proprotein Convertases Protein Processing, Post-Translational Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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