RT Journal Article
SR Electronic
T1 Proteomic Analysis of NRROS Interactome Reveals the Presence of Chaperones and Mediators of the ERAD Pathway
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 326512
DO 10.1101/326512
A1 Rajkumar Noubade
A1 Qui Phung
A1 Wilson Phung
A1 Erik Verschueren
A1 Laura Lau
A1 Hiroyasu Konno
A1 Jennie Lill
A1 Wenjun Ouyang
YR 2018
UL http://biorxiv.org/content/early/2018/05/20/326512.abstract
AB Negative regulator of reactive oxygen species (NRROS, previously called LRRC33) is a leucine-rich repeat (LRR) domain containing, ER-resident transmembrane protein expressed primarily in lymphoid organs, especially in myeloid cells. We have previously demonstrated that NRROS regulates reactive oxygen species production by phagocytic cells by mediating degradation of NOX2 (gp91phox), a component of NOX2 complex responsible for the oxidative burst in these cells. Since LRR is the only functional domain in NRROS, it is likely to interact with other proteins for its biological functions. Here, by performing immunoprecipitation of NRROS and mass spectrometric analysis, we describe the NRROS interactome in macrophages and demonstrate that NRROS interacts with molecular chaperones/co-chaperones and mediators of the endoplasmic reticulum associated degradation (ERAD) pathway such as calnexin, suggesting a broader role for NRROS in protein biosynthesis and the ER quality control machinery.