Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Regulation of Mac-2BP secretion is mediated by its N-glycan binding to ERGIC-53.

Glycobiology - 1 Jul 2013

Chen Yang, Hojo Sanae, Matsumoto Naoki, Yamamoto Kazuo

Abstract excerpt

The leguminous-type (L-type) lectin ER-Golgi intermediate compartment (ERGIC)-53, a homo-oligomeric endoplasmic reticulum (ER)-Golgi recycling protein, functions as a transport receptor for newly synthesized glycoproteins in the early secretory pathway. Although a limited subset of cargo glycopro...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antigens, Neoplasm
Share to Glucans
Share to HeLa Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hep G2 Cells

Share to Mannose-Binding Lectins

Share to Membrane Glycoproteins

Share to Secretory Pathway

Share to Vesicular Transport Proteins

Source

Identifiers

PMID: 23550150
DOI: 10.1093/glycob/cwt027

Genes

MCFD2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23550150-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulation of Mac-2BP secretion is mediated by its N-glycan binding to ERGIC-53.PMID 23550150Read ↗

ERGIC-53 and traffic in the secretory pathwaySemantic proximity Read ↗

Carbohydrate- and conformation-dependent cargo capture for ER-exit.Semantic proximity Read ↗

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

Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme.Semantic proximity Read ↗

ER export of ERGIC-53 is controlled by cooperation of targeting determinants in all three of its domains.Semantic proximity Read ↗

Molecular basis of LMAN1 in coordinating LMAN1-MCFD2 cargo receptor formation and ER-to-Golgi transport of FV/FVIII.Semantic proximity Read ↗

Interaction of FAM5C with UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1): Implication of N-glycosylation in FAM5C secretion.Semantic proximity Read ↗

Rescue of secretion of rare-disease-associated misfolded mutant glycoproteins in UGGT1 knock-out mammalian cells.Semantic proximity Read ↗

Bleeding due to disruption of a cargo-specific ER-to-Golgi transport complex.Semantic proximity Read ↗

Transient dimerization and interaction with ERGIC-53 occur in the fibroblast growth factor receptor 3 early secretory pathway.Semantic proximity Read ↗

Oligomerization and interacellular localization of the glycoprotein receptor ERGIC-53 is independent of disulfide bonds.Semantic proximity Read ↗

Unveiling novel signaling roles for human KDELR3 and KDELR1Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.