ArticleThe Biochemical journal1994
Asparagine-linked oligosaccharides are localized to single extracytosolic segments in multi-span membrane glycoproteins.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- The Research Progress of Metformin Regulation of Metabolic Reprogramming in Malignant Tumors.Pharmaceutical research · 2024Review
- Genome-wide identification of the opsin protein inFrontiers in microbiology · 2023Article
- N-Glycosylation at Asn291 Stabilizes TIM-4 and Promotes the Metastasis of NSCLC.Frontiers in oncology · 2022Article
- Article
- N-linked glycosylation of N48 is required for equilibrative nucleoside transporter 1 (ENT1) function.Bioscience reports · 2016Article
- N-linked glycosylation of protease-activated receptor-1 at extracellular loop 2 regulates G-protein signaling bias.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The SLC37 family of sugar-phosphate/phosphate exchangers.Current topics in membranes · 2014Review
- Regulation of protease-activated receptor signaling by post-translational modifications.IUBMB life · 2011Review
- N-glycosylation efficiency is determined by the distance to the C-terminus and the amino acid preceding an Asn-Ser-Thr sequon.Protein science : a publication of the Protein Society · 2011Article
- N-linked glycosylation of protease-activated receptor-1 second extracellular loop: a critical determinant for ligand-induced receptor activation and internalization.The Journal of biological chemistry · 2010Article
- A SLC4-like anion exchanger from renal tubules of the mosquito (Aedes aegypti): evidence for a novel role of stellate cells in diuretic fluid secretion.American journal of physiology. Regulatory, integrative and comparative physiology · 2010Article
- Triple N-glycosylation in the long S5-P loop regulates the activation and trafficking of the Kv12.2 potassium channel.The Journal of biological chemistry · 2009Article
- N-glycan-mediated quality control in the endoplasmic reticulum is required for the expression of correctly folded delta-opioid receptors at the cell surface.The Journal of biological chemistry · 2008Article
- N-linked glycosylation and its impact on the electrophoretic mobility and function of the human proton-coupled folate transporter (HsPCFT).Biochimica et biophysica acta · 2008Article
- Topology of transmembrane segments 1-4 in the human chloride/bicarbonate anion exchanger 1 (AE1) by scanning N-glycosylation mutagenesis.The Biochemical journal · 2005Article
- Allowed N-glycosylation sites on the Kv1.2 potassium channel S1-S2 linker: implications for linker secondary structure and the glycosylation effect on channel function.The Biochemical journal · 2003Article
- Evidence for the presence of three different anion exchangers in a red cell. Functional expression studies in Xenopus oocytes.The Journal of membrane biology · 2003Article
- Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.The Biochemical journal · 2002Article
- Glycosylation and the activation of proteinase-activated receptor 2 (PAR(2)) by human mast cell tryptase.British journal of pharmacology · 2001Article
- Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.The Biochemical journal · 2001Article
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Authors and funding
2 authors.
Funding
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Abstract
A comprehensive survey of mammalian multi-span (polytopic) membrane proteins showed that asparagine(N)-linked oligosaccharides are localized to single extracytosolic segments. In most membrane proteins this is because potential consensus sites for N-glycosylation (Asn-Xaa-Ser/Thr, X not equal to Pro) are not found in multiple extracytosolic segments. In functional proteins where consensus N-glycosylation sites are contained within more than one extracytosolic segment, only the first segment contains N-linked carbohydrate. An exception is the alpha-subunit of the Na+ channel, which consists of a duplicated structure containing two glycosylated segments. The average size of established N-glycosylated loops connecting two transmembrane segments is 62 residues, with the smallest glycosylated loop being 33 residues in size. N-glycosylated sites are more highly conserved than non-glycosylated (primarily cytosolic) sites and are more common toward the N-terminus of the membrane domain of multi-span membrane proteins. The optimal conditions for glycosylation of consensus sites within an extracytosolic domain of a multi-span membrane protein are (i) the acceptor site is well-spaced (greater than 10 residues) from the transmembrane domain, (ii) the loop is greater than 30 residues in size and (iii) the segment is the first in the protein to contain a suitable extracytosolic consensus site. The localization of N-linked oligosaccharide chains to a single protein segment suggests either glycosylation of multiple loops may compromise protein folding or function, or only a single polypeptide domain can be optimally glycosylated during biosynthesis in vivo.
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