Structural and functional analysis of Alg1 beta-1,4 mannosyltransferase reveals the physiological importance of its membrane topology

Author:

Xu Xin-Xin1,Li Sheng-Tao1,Wang Ning1,Kitajima Toshihiko1,Yoko-o Takehiko2,Fujita Morihisa1,Nakanishi Hideki1,Gao Xiao-Dong1ORCID

Affiliation:

1. Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Avenue, Wuxi, China

2. Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science and Technology (AIST), AIST Tsukuba Central 6, Higashi, Tsukuba, Japan

Funder

National Natural Science Foundation of China

Agriculture Science Technology Achievement Transformation

National Natural Science Foundation of Jiangsu Province

Fundamental Research Funds for the Central Universities

Light Industry Technology and Engineering

Program of Introducing Talents of Discipline to Universities

Publisher

Oxford University Press (OUP)

Subject

Biochemistry

Reference38 articles.

1. N-linked protein glycosylation in the ER;Aebi;Biochim Biophys Acta,2013

2. Structure–function relationships of membrane-associated GT-B glycosyltransferases;Albesa-Jove;Glycobiology,2014

3. The sequence and transcript heterogeneity of the yeast gene ALG1, an essential mannosyltransferase involved in N-glycosylation;Albright;J Biol Chem,1990

4. Alg13p, the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase, is a target for proteasomal degradation;Averbeck;Mol Biol Cell,2008

5. Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc2-PP-dolichol;Bickel;J Biol Chem,2005

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