PT  - JOURNAL ARTICLE
AU  - Rajkumar Noubade
AU  - Qui Phung
AU  - Wilson Phung
AU  - Erik Verschueren
AU  - Laura Lau
AU  - Hiroyasu Konno
AU  - Jennie Lill
AU  - Wenjun Ouyang
TI  - Proteomic Analysis of NRROS Interactome Reveals the Presence of Chaperones and Mediators of the ERAD Pathway
AID  - 10.1101/326512
DP  - 2018 Jan 01
TA  - bioRxiv
PG  - 326512
4099  - http://biorxiv.org/content/early/2018/05/20/326512.short
4100  - http://biorxiv.org/content/early/2018/05/20/326512.full
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.