CYBB Membrane Protein Introduction

Introduction of CYBB

CYBB is a subunit of flavocytochrome b558 which is the central catalytic core of the NADPH oxidase, and it can generate superoxide in the absence of other cytosolic components. CYBB is encoded by the CYBB gene which is located at Xp21.1. The molecular weight of CYBB in human is about 65kDa. CYBB is detected in neutrophils at the protein level., the protein is composed of a heavy chain (beta) and a light chain (alpha), and it is heavily glycosylated (30% of the molecular mass).

Function of CYBB Membrane Protein

CYBB is the core component of the membrane-bound oxidase of phagocytes that generates superoxide. It also plays an important role in many biological functions, for instance, flavin adenine dinucleotide binding, heme binding, metal ion binding, superoxide-generating NADPH oxidase activity and so on. CYBB is also a voltage-gated proton channel which can mediate the H+ currents of resting phagocytes. It takes part in the regulation of cellular pH and is blocked by zinc. Beyond that, mutations in the CYBB gene is responsible for X-linked chronic granulomatous disease. What’ s more, the hydrophobic N-terminal domain of CYBB has 6 putative transmembrane helices that likely coordinate 2 heme groups; The more hydrophilic C-terminal domain is cytosolic and contains a flavoprotein domain. It has been suggested that CYBB is phosphorylated during activation of human neutrophils by PKC. and phosphorylation potentiates intrinsic diaphorase activity of CYBB and interaction with Rac, p67phox, and p47phox. Phosphorylation of CYBB also participates in the regulation of phagocyte NADPH oxidase.

Fig.1 Schematic representation of the CYBB molecule (Rae, 1998).

Application of CYBB Membrane Protein in Literature

1. Weaver C.J., et al. nox2/cybb, deficiency affects zebrafish retinotectal connectivity. Journal of Neuroscience. 2018. PubMed ID: 29793976
   
   

   This article reports that CYBB plays an important role in retinotectal development of zebrafish. This passage shows that a specific NADPH oxidase isoform, CYBB, is important for the establishment of axonal connections between retinal ganglion cells and the optic tectum.

2. Teimourian S., et al. Characterization of 4 New Mutations in the CYBB Gene in 10 Iranian Families With X-linked Chronic Granulomatous Disease. Journal of Pediatric Hematology/oncology. 2018:1. PubMed ID: 29702544
   
   

   This article introduces four new mutations in the CYBB gene, all of them is associated with X-linked chronic granulomatous disease (CGD). In fact, they recognized 10 male patients with X-linked CGD from a tertiary referral center for immune deficiencies in Iran, and they found 9 mutations, 4 of them is novel subjects.

3. Raad H., et al. Regulation of the phagocyte NADPH oxidase activity: phosphorylation of gp91phox/NOX2 by protein kinase C enhances its diaphorase activity and binding to Rac2, p67phox, and p47phox. Faseb Journal. 2009, 23(4): 1011-1022. PubMed ID: 19028840
   
   

   Authors in this group suggest that CYBB is phosphorylated in human neutrophils by PKC to enhance its catalytic activity and assembly of the complex. Phosphorylation of CYBB is a novel mechanism of NADPH oxidase regulation.

4. Hugues S. NOX2 controls phagosomal pH to regulate antigen processing during crosspresentation by dendritic cells. Cell. 2006, 126(1): 205-218. PubMed ID: 16839887
   
   

   This article reveals that NOX2/CYBB plays a critical role in conferring dendritic cells the ability to function as specialized phagocytes adapted to process antigens rather than kill pathogens.

5. Bustamante J., et al. Germline CYBB mutations that selectively affect macrophages in kindreds with X-linked predisposition to tuberculous mycobacterial disease. Nature Immunology. 2011, 12(3): 213-221. PubMed ID: 21278736
   
   

   This article reveals that CYBB is associated with mycobacterial disease and demonstrates that the respiratory burst in human macrophages is a crucial mechanism for protective immunity to tuberculous mycobacteria.

CYBB Preparation Options

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Reference

1. Rae, J., et al. (1998). X-linked chronic granulomatous disease: mutations in the cybb gene encoding the gp91-phox component of respiratory-burst oxidase. American Journal of Human Genetics, 62(6), 1320-1331.

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