ALG10B Membrane Protein Introduction

Introduction of ALG10B

ALG10B, the full protein name is putative alpha-1,2-glucosyltransferase. It is involved in the development of asparagine (N)-linked glycosylation. A mutation in this pathway results in non-syndromic hearing impairment in either mice or humans. This protein is involved in protein glycosylation. It has been reported that ALG10 is required for lipid-linked oligosaccharide biosynthesis and subsequently for abiotic stress response and normal leaf development.

Function of ALG10B Membrane Protein

ALG10B can add the third glucose residue to the lipid-linked oligosaccharide precursor to induce N-linked glycosylation. It transfers glucose from dolichol phosphate glucose (Dol-P-Glc) into the lipid-linked oligosaccharide Glc2Man9GlcNAc2-PP-Dol. When coupled to KCNH2, it may reduce the sensitivity to classic proarrhythmic drug blockade via the mechanism possibly by mediating glycosylation of KCNH2. Also, ALG10B plays a critical role in the maintenance of cochlear outer hair cell function. It has been reported that a point mutation in this gene will cause non-syndromic hearing impairment in either mice or humans. In addition, KCR1 is able to complement the growth defect in yeast strain caused by ALG10 deficiency, and KCR1 can enhance glycosylation of ALG10 in yeast. Moreover, ALG10 is required for lipid-linked oligosaccharide biosynthesis and subsequently for abiotic stress response and normal leaf development. Furthermore, it has been reported that ALG10 is associated with higher water absorption and porosity.

Fig.1 The role of ALG10B in asparagine (N)-linked glycosylation. (Probst, 2013)

Application of ALG10B Membrane Protein in Literature

1. Probst F.J., et al. A point mutation in the gene for asparagine-linked glycosylation 10B (Alg10b) causes nonsyndromic hearing impairment in mice (Mus musculus). PLoS One. 2013, 8(11): e80408. PubMed ID: 24303013
   
   

   This article is the first report of mutation in Alg10b involved in the asparagine-linked glycosylation pathway causing nonsyndromic hearing impairment. And it suggests that the hearing apparatus and the outer hair cells are exquisitely sensitive to perturbations of the N-linked glycosylation pathway.

2. Nakajima T., et al. HERG is protected from pharmacological block by alpha-1,2-glucosyltransferase function. J Biol Chem. 2007, 282(8): 5506-13. PubMed ID: 17189275
   
   

   This article shows that KCR1 and ALG10 exhibit sequence homology, and ALG10 can suppress HERG block by dofetilide. Inhibition of cellular glycosylation pathways with tunicamycin down-regulates the effects of KCR1. Furthermore, KCR1 is able to complement the growth defect in yeast strain caused by alg10 deficiency, and KCR1 can enhance glycosylation of an Alg10 substrate in yeast.

3. Burda P and Aebi M. The ALG10 locus of Saccharomyces cerevisiae encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology. 1998, 8(5): 455-62. PubMed ID: 9597543
   
   

   This article shows that hypoglycosylation of secreted proteins in alg10 deletion strains is strong evidence that the terminal alpha-1,2-linked glucose residue is a key element in substrate recognition by the oligosaccharyltransferase. This ensures that primarily completely assembled oligosaccharide is transferred to protein.

4. Farid A., et al. Arabidopsis thaliana alpha1,2-glucosyltransferase (ALG10) is required for efficient N-glycosylation and leaf growth. Plant J. 2011, 68(2): 314-25. PubMed ID: 21707802
   
   

   This article shows that Arabidopsis ALG10 is required for lipid-linked oligosaccharide biosynthesis and subsequently for normal leaf development and abiotic stress response.

5. Wang C., et al. Preparation and evaluation of chitosan/alginate porous microspheres/Bletilla striata polysaccharide composite hemostatic sponges. Carbohydr Polym. 2017, 174: 432-442. PubMed ID: 28821089
   
   

   This article reveals that CS/Alg10 composite sponges show higher water absorption and porosity. In addition, the cytotoxicity assay and hemostatic property of the CS/Alg and CS/Alg/Bsp composite sponges are tested by CCK-8 assay, in vitro blood clotting, red blood cell (RBC) adhesion, and rabbit ear artery bleeding. These ternary composite sponges could be used as potential novel hemostatic materials in surgical treatment.

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Reference

1. Probst F J, et al. (2013). A point mutation in the gene for asparagine-linked glycosylation 10B (Alg10b) causes nonsyndromic hearing impairment in mice (Mus musculus). PLoS One. 8(11): e80408.

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