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Ligation of FcγR Alters Phagosomal Processing of Protein via Augmentation of NADPH Oxidase Activity
Author(s) -
Balce Dale R.,
Rybicka Joanna M.,
Greene Catherine J.,
Ewanchuk Benjamin W.,
Yates Robin M.
Publication year - 2016
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12396
Subject(s) - nadph oxidase , microbiology and biotechnology , biology , reactive oxygen species
Protein degradation is influenced by redox conditions in the phagosome. Here we show that differential NADPH oxidase ( NOX2 ) activation, as a consequence of Fcγ‐receptor ligation, results in phagosome‐specific changes in redox‐sensitive protein processing. Phagosomes that contained opsonized cargo generated high levels of reactive oxygen species ( ROS ) which subsequently decreased the rates of reduction and hydrolysis of phagocytosed protein. This occurred in an autonomous fashion. These findings indicate that opsonized proteins are differentially degraded within phagosomes via redox control of phagosomal function.