Magnesium transporter protein 1

Definition:

Accessory component of the STT3B-containing form of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of STT3B-dependent substrates. Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with TUSC3. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Has also oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition.; May be involved in Mg(2+) transport in epithelial cells.

References:

[1]. Angela Goytain, et al. Identification and characterization of a novel mammalian Mg2+ transporter with channel-like properties. BMC Genomics. 2005 Apr 1;6:48. [Content Brief]

[2]. Eline Blommaert, et al. Mutations in MAGT1 lead to a glycosylation disorder with a variable phenotype. Proc Natl Acad Sci U S A. 2019 May 14;116(20):9865-9870. [Content Brief]

[3]. Ana S Ramírez, et al. Cryo-electron microscopy structures of human oligosaccharyltransferase complexes OST-A and OST-B. Science. 2019 Dec 13;366(6471):1372-1375. [Content Brief]

[4]. Hao Zhou, et al. Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and vertebrate embryonic development. Proc Natl Acad Sci U S A. 2009 Sep 15;106(37):15750-5. [Content Brief]

[5]. Natalia A Cherepanova, et al. Oxidoreductase activity is necessary for N-glycosylation of cysteine-proximal acceptor sites in glycoproteins. J Cell Biol. 2014 Aug 18;206(4):525-39. [Content Brief]

[6]. Natalia A Cherepanova, et al. Mammalian cells lacking either the cotranslational or posttranslocational oligosaccharyltransferase complex display substrate-dependent defects in asparagine linked glycosylation. Sci Rep. 2016 Feb 11;6:20946. [Content Brief]

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