ArticleProceedings of the National Academy of Sciences of the United States of America2001
Basolateral membrane expression of a K+ channel, Kir 2.3, is directed by a cytoplasmic COOH-terminal domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 46 citations in OpenAlex.
- KCNJ4 variants disrupt inward-rectifier potassium channel function and cause refractory epilepsy.Epilepsia · 2026Article
- Expression, localization, and functional properties of inwardly rectifying KAmerican journal of physiology. Renal physiology · 2020Review
- Role and mechanisms of regulation of the basolateral KActa physiologica (Oxford, England) · 2017Review
- PDZ Domain Recognition: Insight from Human Tax-Interacting Protein 1 (TIP-1) Interaction with Target Proteins.Biology · 2015Review
- Dominant negative RPW8.2 fusion proteins reveal the importance of haustorium-oriented protein trafficking for resistance against powdery mildew in Arabidopsis.Plant signaling & behavior · 2015Article
- Regulation of potassium channel trafficking in the distal nephron.Current opinion in nephrology and hypertension · 2013Review
- Specificity and promiscuity in human glutaminase interacting protein recognition: insight from the binding of the internal and C-terminal motif.Biochemistry · 2012Article
- Basolateral membrane K+ channels in renal epithelial cells.American journal of physiology. Renal physiology · 2012Review
- Promiscuous binding at the crossroads of numerous cancer pathways: insight from the binding of glutaminase interacting protein with glutaminase L.Biochemistry · 2011Article
- KCNQ1 channels voltage dependence through a voltage-dependent binding of the S4-S5 linker to the pore domain.The Journal of biological chemistry · 2011Article
- SAP97 regulates Kir2.3 channels by multiple mechanisms.American journal of physiology. Heart and circulatory physiology · 2009Article
- A PDZ-binding motif controls basolateral targeting of syndecan-1 along the biosynthetic pathway in polarized epithelial cells.Traffic (Copenhagen, Denmark) · 2008Article
- Compartmentalization of aquaporins in the human intestine.International journal of environmental research and public health · 2008Article
- TIP-1 has PDZ scaffold antagonist activity.Molecular biology of the cell · 2006Article
- Selective mobility and sensitivity to SNAREs is exhibited by the Arabidopsis KAT1 K+ channel at the plasma membrane.The Plant cell · 2006Article
- Molecular diversity and regulation of renal potassium channels.Physiological reviews · 2005Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The inwardly rectifying potassium channel Kir 2.3 is specifically targeted and expressed on the basolateral membrane of certain renal epithelial cells. In the present study, the structural basis for polarized targeting was elucidated. Deletion of a unique COOH-terminal domain produced channels that were mistargeted to the apical membrane, consistent with the removal of a basolateral membrane-sorting signal. By characterizing a series of progressively smaller truncation mutants, an essential targeting signal was defined (residues 431-442) within a domain that juxtaposes or overlaps with a type I PDZ binding motif (442). Fusion of the COOH-terminal structure onto CD4 was sufficient to change a random membrane-trafficking and expression pattern into a basolateral membrane one. Using metabolic labeling and pulse-chase and surface immunoprecipitation, we found that CD4-Kir2.3 COOH-terminal chimeras were rapidly and directly targeted to the basolateral membrane, consistent with a sorting signal that is processed in the biosynthetic pathway. Collectively, the data indicate that the basolateral sorting determinant in Kir 2.3 is composed of a unique arrangement of trafficking motifs, containing tandem, conceivably overlapping, biosynthetic targeting and PDZ-based signals. The previously unrecognized domain corresponds to a highly degenerate structure within the Kir channel family, raising the possibility that the extreme COOH terminus of Kir channels may differentially coordinate membrane targeting of different channel isoforms.
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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.