ArticleThe Journal of biological chemistry2011
Core-glycosylated mucin-like repeats from MUC1 are an apical targeting signal.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- MUC17 and the intestinal glycocalyx: structure, regulation, and barrier function in health and disease.Bioscience reports · 2026Review
- Mucin Biology as a Local Diagnostic and Promising Therapeutic Target in Endometriosis: Expression and Glycosylation Profiling.International journal of molecular sciences · 2026Article
- A size filter at the Golgi regulates apical membrane protein sorting.Nature cell biology · 2024Article
- Possible correlation of apical localization of MUC1 glycoprotein with luminal A-like status of breast cancer.Scientific reports · 2023Article
- Influence of glycoprotein MUC1 on trafficking of the CaThe Journal of biological chemistry · 2023Article
- Cloning, Expression, and Purification of Galectins for In Vitro Studies.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Membrane mucins of the intestine at a glance.Journal of cell science · 2020Review
- Cross-talk between Colon Cells and Macrophages Increases ST6GALNAC1 and MUC1-sTn Expression in Ulcerative Colitis and Colitis-Associated Colon Cancer.Cancer immunology research · 2020Article
- Sialylation of MUC4β N-glycans by ST6GAL1 orchestrates human airway epithelial cell differentiation associated with type-2 inflammation.JCI insight · 2019Article
- Novel roles for mucin 1 in the kidney.Current opinion in nephrology and hypertension · 2017Review
- Intra- and Extra-Cellular Events Related to Altered Glycosylation of MUC1 Promote Chronic Inflammation, Tumor Progression, Invasion, and Metastasis.Biomolecules · 2016Review
- The PDZ Protein Na+/H+ Exchanger Regulatory Factor-1 (NHERF1) Regulates Planar Cell Polarity and Motile Cilia Organization.PloS one · 2016Article
- Pathobiological implications of mucin glycans in cancer: Sweet poison and novel targets.Biochimica et biophysica acta · 2015Review
- Chemically tunable mucin chimeras assembled on living cells.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Roles for trafficking and O-linked glycosylation in the turnover of model cell surface proteins.The Journal of biological chemistry · 2014Article
- Altered glycosylation of MUC1 influences its association with CIN85: the role of this novel complex in cancer cell invasion and migration.Oncotarget · 2013Article
- Article
- The lectin domain of the polypeptide GalNAc transferase family of glycosyltransferases (ppGalNAc Ts) acts as a switch directing glycopeptide substrate glycosylation in an N- or C-terminal direction, further controlling mucin type O-glycosylation.The Journal of biological chemistry · 2013Article
- Multiple motifs regulate apical sorting of p75 via a mechanism that involves dimerization and higher-order oligomerization.Molecular biology of the cell · 2013Article
- Analysis of tumor-associated mucin glycotopes by Western transfer methods.Methods in molecular biology (Clifton, N.J.) · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
MUC1 is efficiently delivered to the apical surface of polarized Madin-Darby canine kidney (MDCK) cells by transit through apical recycling endosomes, a route associated with delivery of apical proteins with glycan-dependent targeting signals. However, a role for glycans in MUC1 sorting has not been established. A key feature of MUC1 is a heavily O-glycosylated mucin-like domain with a variable number of nearly perfect tandem repeats and adjacent imperfect repeats. Metabolic labeling, cell surface biotinylation, immobilized lectins, and confocal immunofluorescence microscopy were used to characterize the polarized delivery of MUC1 mutants and chimeras in MDCK cells to identify the apical targeting signal. Both the interleukin-2 receptor α subunit (Tac) and a chimera where the Tac ectodomain replaced that of MUC1 were delivered primarily to the basolateral surface. Attachment of the MUC1 mucin-like domain to the N terminus of Tac enhanced apical but not basolateral delivery when compared with Tac. Conversely, deletions within the mucin-like domain in MUC1 reduced apical but not basolateral delivery when compared with MUC1. In pull-down assays with lectins, we found a notable difference in the presence of core 1 O-glycans, but not poly-N-acetyllactosamine, in apically targeted MUC1 and chimeras when compared with Tac. Consistent with these data, we found no effect on MUC1 targeting when galectin-3, with preference for poly-N-acetyllactosamine, was depleted from polarized MDCK cells. However, we did block the apical targeting activity of the mucin-like repeats when we overexpressed CMP-Neu5Ac:GalNAc-Rα2,6-sialyltransferase-1 to block core O-glycan synthesis. The cumulative data indicate that the core-glycosylated mucin-like repeats of MUC1 constitute an apical targeting signal.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.