Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus.

Schweizer, Anja; Fransen, J.A.M.; Bächi, Thomas; Ginsel, L.A.; Hauri, Hans‐Peter

doi:10.1083/jcb.107.5.1643

Cited by 470 publications

(388 citation statements)

References 37 publications

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“…Fixed cells were stored until use in 1% PFA. Before sectioning, cells were pelleted in 10% gelatin and postfixed in 1% PFA for 24 h. Ultrathin cryosectioning was performed as described before (33,34). Sections were incubated with a rabbit anti-mouse antiserum to visualize the internalized AZN-D2 Abs followed by protein A complexed with 5 nm gold.…”

Section: Immunohistochemistrymentioning

confidence: 99%

The Dendritic Cell-Specific Adhesion Receptor DC-SIGN Internalizes Antigen for Presentation to T Cells

Engering¹,

Geijtenbeek²,

Vliet³

et al. 2002

The Journal of Immunology

563

491

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Dendritic cells (DCs) capture Ags or viruses in peripheral tissue to transport them to lymphoid organs to induce cellular T cell responses. Recently, a DC-specific C-type lectin was identified, DC-specific ICAM-grabbing non-integrin (DC-SIGN), that functions as cell adhesion receptor mediating both DC migration and T cell activation. DC-SIGN also functions as an HIV-1R that captures HIVgp120 and facilitates DC-induced HIV transmission of T cells. Internalization motifs in the cytoplasmic tail of DC-SIGN hint to a function of DC-SIGN as endocytic receptor. In this study we demonstrate that on DCs DC-SIGN is rapidly internalized upon binding of soluble ligand. Mutating a putative internalization motif in the cytoplasmic tail reduces ligand-induced internalization. Detailed analysis using ratio fluorescence imaging and electron microscopy showed that DC-SIGN-ligand complexes are targeted to late endosomes/lysosomes. Moreover, ligands internalized by DC-SIGN are efficiently processed and presented to CD4+ T cells. The distinct pattern of expression of C-type lectins on DCs in situ and their nonoverlapping Ag recognition profile hint to selective functions of these receptors to allow a DC to recognize a wide variety of Ags and to process these to induce T cell activation. These data point to a novel function of the adhesion receptor DC-SIGN as an efficient DC-specific Ag receptor that can be used as a target to induce viral and antitumor immunity.

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Section: Immunohistochemistrymentioning

confidence: 99%

The Dendritic Cell-Specific Adhesion Receptor DC-SIGN Internalizes Antigen for Presentation to T Cells

Engering¹,

Geijtenbeek²,

Vliet³

et al. 2002

The Journal of Immunology

563

491

View full text Add to dashboard Cite

show abstract

“…However, the above experiments did not allow us to conclude whether ERGIC-53 is indeed selective for D-mannose. From its intracellular localization, that is ER, ERGIC, and to a minor extent cis-Golgi (Schweizer et al, 1988Chavrier et al, 1990), we expected the putative natural monosaccharide ligands of ERGIC-53 to be either glucose, mannose, or GlcNAc but not galactose that is attached to glycoproteins only in the transGolgi (Roth and Berger, 1982;Kornfeld and Kornfeld, 1985). To address the question of monosaccharide selectivity we tested the hexose concentration required for elution of myc/6xHis from the mannose column in a sequential elution protocol (see MATERIAL AND METHODS).…”

Section: Elution Of Ergic-53 Is Selective For D-mannosementioning

confidence: 99%

“…Ligands bind on the extracytoplasmic side to the CRDs and the ligand-receptor complex is then sorted into budding vesicles via the cytoplasmic sorting signals, a process that is likely mediated through the interaction with coat structures (Kornfeld, 1992; Schmid, 1992;Pelham, 1994). ERGIC-53 with its type I transmembrane topology (Schweizer et al, 1988;Schindler et al, 1993), a lumenal CRD (this study), and its cytoplasmic sorting signals (Itin et al, 1995b) fits the domain organization of a sorting receptor. The oligomeric structure of ERGIC-53 (disulfide-linked dimers and hexamers) also provides multiple CRDs per ERGIC-53 complex.…”

Section: Elution Of Ergic-53 Is Selective For D-mannosementioning

confidence: 99%

“…Two proteins, ERGIC-53 (Schweizer et al, 1988;Schindler et al, 1993) and VIP-36 , have recently been postulated to belong to a new class of sorting receptors in the secretory pathway . Both proteins have a type I transmembrane topology, and a stretch of about 200 amino acids in their luminal domain shows 19-24% identity to leguminous lectins.…”

Section: Introductionmentioning

confidence: 99%

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

Itin

Roche

Monsigny

et al. 1996

MBoC

Self Cite

164

140

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Based on sequence homologies with leguminous lectins, the intermediate compartment marker proposed to be a member of a putative new class of animal lectins associated with the secretory pathway. Independently, 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 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 mannosecolumn 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 glycoproteins in the early secretory pathway.

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“…These structures have been variously named: pre-Golgi vacuoles (33,36), budding compartment (42), intermediate compartment (37)(38)(39), intermediate elements (34), salvage compartment (14,22,45), and cis-Golgi network (9,13,26,32). However, the morphology of these structures has yet to be defined, and the mechanism of the transport between the ER and Golgi complex is still largely unknown (1,25,30,32).…”

mentioning

confidence: 99%

Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex

Bonatti¹,

Lotti²,

Torrisi³

et al. 1993

Molecular Mechanisms of Membrane Traffic

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Abstract. We performed an immunocytochemical analysis to study the transfer of a marker protein (G glycoprotein coded by vesicular stomatitis virus ts 045 strain) from the intermediate compartment to the Golgi stacks in infected Vero cells. The intermediate compartment seemed to consist of about 30--40 separate units of clustered small vesicles and short tubules. The units contained Rab2 protein and were spread throughout the cytoplasm, with a ratio of about 6:4 in the peripheral versus perinuclear site. Time-course experiments revealed a progressive ~ransfer of G glycoprotein from the intermediate compartment to the Golgi stacks, while the tubulo-vesicular units did not appear to change their intracellular distribution. Moreover, the labeling density of peripheral and perinuclear units decreased in parallel during the transfer. These results support the notion that the intermediate compartment is a station in the secretory pathway, and that a vesicular transport connects this station to the Golgi complex.

show abstract

Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus.

Cited by 470 publications

References 37 publications

The Dendritic Cell-Specific Adhesion Receptor DC-SIGN Internalizes Antigen for Presentation to T Cells

The Dendritic Cell-Specific Adhesion Receptor DC-SIGN Internalizes Antigen for Presentation to T Cells

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

Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex

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