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

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

Proc. Natl. Acad. Sci. U.S.A. 1992
1644824 Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen

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

J. Biol. Chem. 1992
Participants
Participates
Catalyst Activity

serine-type endopeptidase activity of FURIN [plasma membrane]

This event is regulated
Disease
Name Identifier Synonyms
anthrax disease DOID:7427
Authored
Reviewed
Created
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