ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

Itin, C; Roche, A C; Monsigny, M; Hauri, H P

doi:10.1091/mbc.7.3.483

Cited by 179Galectins and Cancer BiologyGlycosylation and Glycoproteins ResearchCellular transport and secretion

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

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Itin, C, Roche, A C, Monsigny, M, Hauri, H P·1996·Molecular Biology of the Cell

DOI 10.1091/mbc.7.3.483PMC PMC275899

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Abstract

Based on sequence homologies with leguminous lectins, the intermediate compartment marker ERGIC-53 was proposed to be a member of a putative new class of animal lectins associated with the secretory pathway. Independent, a promyelocytic protein, MR60, was purified by mannose-column chromatography, and a cDNA was isolated that matched MR60 peptide sequences. This cDNA was identical to that of ERGIC-53 and homologies with the animal lectin family of the galectins were noticed. Not all peptide sequences of MR60, however, were found in ERGIC-53, raising the possibility that another protein associated with ERGIC-53 may possess the lectin activity. Here, we provide the first direct evidence for a lectin function of ERGIC-53. Overexpressed ERGIC-53 binds to a mannose column in a calcium-dependent manner and also co-stains with mannosylated neoglycoprotein in a morphological binding assay. By using a sequential elution protocol we show that ERGIC-53 has selectivity for mannose and low affinity for glucose and GlcNAc, but no affinity for galactose. To experimentally address the putative homology of ERGIC-53 to leguminous lectins, a highly conserved protein family with an invariant asparagine essential for carbohydrate binding, we substituted the corresponding asparagine in ERGIC-53. This mutation, as well as a mutation affecting a second site in the putative carbohydrate recognition domain, abolished mannose-column binding and co-staining with mannosylated neoglycoprotein. These findings establish ERGIC-53 as a lectin and provide functional evidence for its relationship to leguminous lectins. Based on its monosaccharide specificity, domain organization, and recycling properties, we propose ERGIC-53 to function as a sorting receptor for glyco-proteins in the early secretory pathway.

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ERGIC-53 is a mannose-selective and calcium-dependent human homolog of leguminous L-type lectins and acts as a critical chaperone for coagulation factors V and VIII during their biosynthesis in hepatocytes and endothelial cells.
“the LMAN1 gene product ERGIC-53 in the ER-Golgi intermediate compartment is a mannose-selective and calcium-dependent human homolog of leguminous L-type lectins (892) and acts as a critical chaperone for the coagulation factors V and VIII during their biosynthesis in hepatocytes (893) and endothelial cells (894) respectively”
From Biological roles of glycans (2017) · cites this paper as [892]

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“For example, the LMAN1 gene product ERGIC-53 in the ER-Golgi intermediate compartment is a mannose-selective and calciumdependent human homologue of leguminous L-type lectins (892) and acts as a critical chaperone for the coagulation factors V and VIII during their biosynthesis in hepatocytes (893) and endothelial cel…”
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ERGIC-53, a Membrane Protein of the Endoplasmic Reticulum-Golgi Intermediate Compartment, Is Identical to MR60, an Intracellular Mannose-specific Lectin of Myelomonocytic Cells
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Crystal Structure of the Carbohydrate Recognition Domain of p58/ERGIC-53, a Protein Involved in Glycoprotein Export from the Endoplasmic Reticulum
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Structural Basis for Disparate Sugar-Binding Specificities in the Homologous Cargo Receptors ERGIC-53 and VIP36
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Authors: Itin, C., Roche, A. C., Monsigny, M., & Hauri, H. P.
Affiliations: University of Basel (CH)
Venue: Molecular Biology of the Cell
Publisher: American Society for Cell Biology (ASCB)
Published: 1996-03
Volume: 7
Issue: 3
Pages: 483-493
ISSN: 1059-1524 (ISSN-L)
1939-4586
DOI: 10.1091/mbc.7.3.483
PMC: PMC275899
OpenAlex: W2142329004
Cited by: 179
References: 61
Citations by year: 2026: 5 · 2025: 3 · 2024: 3 · 2022: 10 · 2021: 4 · 2020: 5 · 2019: 2 · 2018: 2 · 2017: 2 · 2016: 4 · 2015: 3 · 2014: 2 · 2013: 5 · 2012: 2
FWCI: 6.85
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Molecular Biology of the Cell (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
edoc (University of Basel) (acceptedVersion)
edoc (University of Basel)
Funders: Styrelsen för Internationellt Utvecklingssamarbete
Association pour la Recherche sur le Cancer
Topics: Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: ERGIC-53, galectins, lectin function, calcium-dependent binding, secretory pathway, intermediate compartment, carbohydrate recognition domain, asparagine substitution, protein recycling
MeSH terms: Amino Acid Sequence, Animals, Epitopes, Calcium, Cell Line, Transformed, Chlorocebus aethiops, Humans, Mannose, Membrane Proteins, Molecular Sequence Data, Mutation, Structure-Activity Relationship, Gene Expression, Lectins, Mannose-Binding Lectins

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ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

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