Furin cleaves ANTXR1-bound pagA to yield pagA(197-794)

Stable Identifier
R-HSA-5210935
Type
Reaction [transition]
Species
Homo sapiens
Related Species
Bacillus anthracis
Compartment
extracellular region, plasma membrane
ReviewStatus
5/5
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Furin cleaves ANTXR1-bound pagA to yield pagA(197-794)
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Furin or a related protease at the cell surface cleaves ANTXR1-bound pagA (Anthrax Protective Antigen, full-length). The larger cleavage product, pagA(197-794), remains bound to the receptor while a smaller product, pagA(30-196), is released into the extracellular space (Klimpel et al, 1992; Molloy et al. 1992).
Literature References
PubMed ID Title Journal Year
1644824 Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen

Klimpel, KR, Leppla, SH, Molloy, S S, Thomas, G, Bresnahan, PA

J. Biol. Chem. 1992
1438214 Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin

Klimpel, KR, Leppla, SH, Molloy, S S, Thomas, G

Proc. Natl. Acad. Sci. U.S.A. 1992
Participants
Input
Output
Participates
as an event of
Catalyst Activity

serine-type endopeptidase activity of FURIN [plasma membrane]

Physical Entity
FURIN [plasma membrane] (Homo sapiens)
Activity
serine-type endopeptidase activity (GO:0004252)
This event is regulated
Negatively by
Regulator
FURIN:FURIN inhibitors [plasma membrane] (Homo sapiens)
Disease
Name Identifier Synonyms
anthrax disease DOID:7427
Authored
D'Eustachio, P  (2013-12-13)
Reviewed
Leppla, SH  (2014-05-19)
Moayeri, M  (2014-05-28)
Turk, BE  (2014-05-23)
Liu, S  (2014-05-28)
Created
D'Eustachio, P  (2013-12-07)
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