ArticleProceedings of the National Academy of Sciences of the United States of America1999
VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
82 citing papers in PubMed, 201 citations in OpenAlex.
- Research advances of MAL family members in tumorigenesis and tumor progression (Review).Molecular medicine reports · 2024Review
- Lipid Rafts: The Maestros of Normal Brain Development.Biomolecules · 2024Review
- Emerging connections between GPI-anchored proteins and their extracellular carriers in colorectal cancer.Extracellular vesicles and circulating nucleic acids · 2023Article
- MARVEL domain containing CMTM4 affects CXCR4 trafficking.Molecular biology of the cell · 2022Article
- MALL, a membrane-tetra-spanning proteolipid overexpressed in cancer, is present in membraneless nuclear biomolecular condensates.Cellular and molecular life sciences : CMLS · 2022Article
- The MAL Protein, an Integral Component of Specialized Membranes, in Normal Cells and Cancer.Cells · 2021Review
- Myelin-Associated MAL and PLP Are Unusual among Multipass Transmembrane Proteins in Preferring Ordered Membrane Domains.The journal of physical chemistry. B · 2020Article
- Lung endothelial cells are sensitive to epsilon toxin from Clostridium perfringens.Veterinary research · 2020Article
- Mal protein stabilizes luminal membrane PLC-β3 and negatively regulates ENaC in mouse cortical collecting duct cells.American journal of physiology. Renal physiology · 2019Article
- DNA hypermethylation ofTranslational cancer research · 2019Article
- On The Role of Myelin and Lymphocyte Protein (MAL) In Cancer: A Puzzle With Two Faces.Journal of Cancer · 2019Review
- The Cytotoxicity of Epsilon Toxin from Clostridium perfringens on Lymphocytes Is Mediated by MAL Protein Expression.Molecular and cellular biology · 2018Article
- Unraveling the role of membrane microdomains during microbial infections.Cell biology and toxicology · 2017Review
- Sequential and compartmentalized action of Rabs, SNAREs, and MAL in the apical delivery of fusiform vesicles in urothelial umbrella cells.Molecular biology of the cell · 2016Article
- Article
- Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface.Journal of lipid research · 2016Review
- MAL Is a Regulator of the Recruitment of Myelin Protein PLP to Membrane Microdomains.PloS one · 2016Article
- Solutions to Peto's paradox revealed by mathematical modelling and cross-species cancer gene analysis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Article
- The Myelin and Lymphocyte Protein MAL Is Required for Binding and Activity of Clostridium perfringens ε-Toxin.PLoS pathogens · 2015Article
- The unique polarity phenotype of hepatocytes.Experimental cell research · 2014Review
22 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Apical proteins are sorted and delivered from the trans-Golgi network to the plasma membrane by a mechanism involving sphingolipid-cholesterol rafts. In this paper, we report the effects of changing the levels of VIP17/MAL, a tetraspan membrane protein localized to post-Golgi transport containers and the apical cell surface in MDCK cells. Overexpression of VIP17/MAL disturbed the morphology of the MDCK cell layers by increasing apical delivery and seemingly expanding the apical cell surface domains. On the other hand, expression of antisense RNA directed against VIP17/MAL caused accumulation in the Golgi and/or impaired apical transport of different apical protein markers, i.e., influenza virus hemagglutinin, the secretory protein clusterin (gp80), the transmembrane protein gp114, and a glycosylphosphatidylinositol-anchored protein. However, antisense RNA expression did not affect the distribution of E-cadherin to the basolateral surface. Because VIP17/MAL associates with sphingolipid-cholesterol rafts, these data provide functional evidence that this protein is involved in apical transport and might be a component of the machinery clustering lipid rafts with apical cargo to form apical transport carriers.
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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.