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The role of chordin fragments generated by partial tolloid cleavage in regulating BMP activity.

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  • معلومة اضافية
    • المصدر:
      Publisher: Portland Press On The Behalf Of The Biochemical Society Country of Publication: England NLM ID: 7506897 Publication Model: Print Cited Medium: Internet ISSN: 1470-8752 (Electronic) Linking ISSN: 03005127 NLM ISO Abbreviation: Biochem Soc Trans Subsets: MEDLINE
    • بيانات النشر:
      Original Publication: London : Portland Press On The Behalf Of The Biochemical Society
    • الموضوع:
      Models, Biological* ; Signal Transduction*; Bone Morphogenetic Protein Receptors/*antagonists & inhibitors ; Bone Morphogenetic Proteins/*antagonists & inhibitors ; Glycoproteins/*metabolism ; Intercellular Signaling Peptides and Proteins/*metabolism ; Proteins/*metabolism ; Tolloid-Like Metalloproteinases/*metabolism; Animals ; Bone Morphogenetic Protein Receptors/agonists ; Bone Morphogenetic Protein Receptors/chemistry ; Bone Morphogenetic Protein Receptors/metabolism ; Bone Morphogenetic Proteins/chemistry ; Bone Morphogenetic Proteins/metabolism ; Glycoproteins/chemistry ; Humans ; Intercellular Signaling Peptides and Proteins/chemistry ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Protein Interaction Domains and Motifs ; Protein Stability ; Proteins/chemistry ; Proteolysis ; Tolloid-Like Metalloproteinases/chemistry
    • نبذة مختصرة :
      Chordin-mediated regulation of bone morphogenetic protein (BMP) family growth factors is essential in early embryogenesis and adult homoeostasis. Chordin binds to BMPs through cysteine-rich von Willebrand factor type C (vWC) homology domains and blocks them from interacting with their cell surface receptors. These domains also self-associate and enable chordin to target related proteins to fine-tune BMP regulation. The chordin-BMP inhibitory complex is strengthened by the secreted glycoprotein twisted gastrulation (Tsg); however, inhibition is relieved by cleavage of chordin at two specific sites by tolloid family metalloproteases. As Tsg enhances this cleavage process, it serves a dual role as both promoter and inhibitor of BMP signalling. Recent developments in chordin research suggest that rather than simply being by-products, the cleavage fragments of chordin continue to play a role in BMP regulation. In particular, chordin cleavage at the C-terminus potentiates its anti-BMP activity in a type-specific manner.
      (© 2015 Authors; published by Portland Press Limited.)
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    • Grant Information:
      088785 United Kingdom Wellcome Trust; 106503/Z/14/Z United Kingdom Wellcome Trust; BB/I019286/1 United Kingdom Biotechnology and Biological Sciences Research Council
    • Contributed Indexing:
      Keywords: bone morphogenetic protein (BMP) signalling; chordin; tolloid cleavage
    • الرقم المعرف:
      0 (Bone Morphogenetic Proteins)
      0 (Glycoproteins)
      0 (Intercellular Signaling Peptides and Proteins)
      0 (Peptide Fragments)
      0 (Proteins)
      0 (TWSG1 protein, human)
      93586-27-7 (chordin)
      EC 2.7.11.30 (Bone Morphogenetic Protein Receptors)
      EC 3.4.- (Tolloid-Like Metalloproteinases)
    • الموضوع:
      Date Created: 20151031 Date Completed: 20160823 Latest Revision: 20181113
    • الموضوع:
      20240829
    • الرقم المعرف:
      PMC4613500
    • الرقم المعرف:
      10.1042/BST20150071
    • الرقم المعرف:
      26517884