ArticleProceedings of the National Academy of Sciences of the United States of America2007
MAL decreases the internalization of the aquaporin-2 water channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The trial behind it
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Who cites it
31 citing papers in PubMed, 52 citations in OpenAlex.
- Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022Review
- The MAL Protein, an Integral Component of Specialized Membranes, in Normal Cells and Cancer.Cells · 2021Review
- Review
- Mal protein stabilizes luminal membrane PLC-β3 and negatively regulates ENaC in mouse cortical collecting duct cells.American journal of physiology. Renal physiology · 2019Article
- Regulation of Transporters and Channels by Membrane-Trafficking Complexes in Epithelial Cells.Cold Spring Harbor perspectives in biology · 2017Review
- The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells-a Potential Target for Pharmacological Intervention in Cardiovascular Diseases.Frontiers in pharmacology · 2016Review
- Dynamic regulation and dysregulation of the water channel aquaporin-2: a common cause of and promising therapeutic target for water balance disorders.Clinical and experimental nephrology · 2014Review
- X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and trafficking.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- VIP17/MAL expression modulates epithelial cyst formation and ciliogenesis.American journal of physiology. Cell physiology · 2012Article
- Cell culture models and animal models for studying the patho-physiological role of renal aquaporins.Cellular and molecular life sciences : CMLS · 2012Review
- New insights into the dynamic regulation of water and acid-base balance by renal epithelial cells.American journal of physiology. Cell physiology · 2012Review
- Mechanisms of cell polarity and aquaporin sorting in the nephron.Pflugers Archiv : European journal of physiology · 2011Review
- Selective gene expression by rat gastric corpus epithelium.Physiological genomics · 2011Article
- MAL/VIP17, a new player in the regulation of NKCC2 in the kidney.Molecular biology of the cell · 2010Article
- Aquaporins in kidney pathophysiology.Nature reviews. Nephrology · 2010Review
- Galectin-3, a novel centrosome-associated protein, required for epithelial morphogenesis.Molecular biology of the cell · 2010Article
- Phosphorylation of aquaporin-2 regulates its endocytosis and protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Abnormal expression of myelination genes and alterations in white matter fractional anisotropy following prenatal viral influenza infection at E16 in mice.Schizophrenia research · 2009Article
- Aquaporin-2 in the "-omics" era.The Journal of biological chemistry · 2009Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Body water homeostasis depends critically on the hormonally regulated trafficking of aquaporin-2 (AQP2) water channels in renal collecting duct epithelial cells. Several types of posttranslational modifications are clearly involved in controlling the distribution of AQP2 between intracellular vesicles and the apical plasma membrane. Little is known, however, about the protein interactions that govern the trafficking of AQP2 between these organelles. MAL is a detergent-resistant membrane-associated protein implicated in apical sorting events. We wondered, therefore, whether MAL plays a role in the regulated trafficking of AQP2 between intracellular vesicles and the apical surface. We find that AQP2 and MAL are coexpressed in epithelial cells of the kidney collecting duct. These two proteins interact, both in the native kidney and when expressed by transfection in cultured cells. The S256-phosphorylated form of AQP2 appears to interact more extensively with MAL than does the water channel protein not phosphorylated at this serine. We find that MAL is not involved in detergent-resistant membrane association or apical delivery of AQP2 in LLC-PK(1) renal epithelial cells. Instead, MAL increases the S256 phosphorylation and apical surface expression of AQP2. Furthermore, internalization experiments show that MAL induces surface expression of AQP2 by attenuating its internalization. Thus, the involvement of MAL in the cell surface retention of apical membrane proteins could play an important role in regulated absorption and secretion in transporting epithelia.
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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.