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Literature summary for 3.4.21.75 extracted from

  • Nelsen, S.M.; Christian, J.L.
    Site-specific cleavage of BMP4 by furin, PC6, and PC7 (2009), J. Biol. Chem., 284, 27157-27166.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.75

Cloned(Commentary)

Cloned (Comment) Organism
determination of polyadenylation of endogenous furin transcripts Xenopus laevis

Protein Variants

Protein Variants Comment Organism
additional information furin antisense expression leading to furin depletionin oocytes is accompanied by a corresponding decrease in the levels of both the fully cleaved prodomain and mature BMP4 Xenopus laevis

Inhibitors

Inhibitors Comment Organism Structure
alpha1-AT a naturally occurring serpin and a potent inhibitor of furin Xenopus laevis
alpha1-PDX a furin- and PC6-selective inhibitor, blocks cleavage of furin minimal consensus motifs, and of the S2 but not the S1 site of pro-BMP4 in embryos, suggesting the existence of a developmentally regulated S1 site-specific convertase Xenopus laevis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pro-BMP4 + H2O Xenopus laevis pro-BMP4 is initially cleaved at a site adjacent to the mature ligand domain (S1) and then at an upstream site (S2) within the prodomain. Cleavage at the S2 site, which appears to occur in a tissue-specific fashion, regulates the activity and signaling range of mature BMP4. In Xenopus oocytes, furin and PC6 function redundantly to cleave both the S1 and S2 sites of pro-BMP4 BMP4 + propeptide of BMP4
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Organism

Organism UniProt Comment Textmining
Xenopus laevis
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Source Tissue

Source Tissue Comment Organism Textmining
embryo
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 Xenopus laevis
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oocyte
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 Xenopus laevis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pro-BMP4 + H2O pro-BMP4 is initially cleaved at a site adjacent to the mature ligand domain (S1) and then at an upstream site (S2) within the prodomain. Cleavage at the S2 site, which appears to occur in a tissue-specific fashion, regulates the activity and signaling range of mature BMP4. In Xenopus oocytes, furin and PC6 function redundantly to cleave both the S1 and S2 sites of pro-BMP4 Xenopus laevis BMP4 + propeptide of BMP4
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pro-BMP4 + H2O i.e. pro-bone morphogenetic protein 4, site-specific cleavage by furin Xenopus laevis BMP4 + propeptide of BMP4
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General Information

General Information Comment Organism
additional information alpha1-PDX blocks cleavage of the S2 but not the S1 site of pro-BMP4 in embryos, suggesting the existence of a developmentally regulated S1 site-specific convertase, probably PC7, overview Xenopus laevis
physiological function bone morphogenetic proteins, BMPs, require proteolytic activation by members of the proprotein convertase family Xenopus laevis