ArticleExperimental cell research2011
A C-terminal PDZ binding domain modulates the function and localization of Kv1.3 channels.
Article in Experimental cell research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Potassium channels in vascular smooth muscle cells.Physiological reviews · 2026Review
- Voltage-dependent potassium channel regulatory subunits in the immune system.Biophysical reviews · 2026Review
- Identification of Novel Kv1.3 Channel-Interacting Proteins Using Proximity Labelling in T-Cells.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2025Article
- Proximity Labeling Proteomics Reveals Kv1.3 Potassium Channel Immune Interactors in Microglia.Molecular & cellular proteomics : MCP · 2024Article
- Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells.International journal of molecular sciences · 2022Article
- Developmental expression of Kv1 voltage-gated potassium channels in the avian hypothalamus.Neuroscience letters · 2016Article
- Caveolin interaction governs Kv1.3 lipid raft targeting.Scientific reports · 2016Article
- The C-terminus SH3-binding domain of Kv1.3 is required for the actin-mediated immobilization of the channel via cortactin.Molecular biology of the cell · 2015Article
- The role of PSD-95 in the rearrangement of Kv1.3 channels to the immunological synapse.Pflugers Archiv : European journal of physiology · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The voltage-gated potassium channel, Kv1.3, plays an important role in regulating membrane excitability in diverse cell types ranging from T-lymphocytes to neurons. In the present study, we test the hypothesis that the C-terminal PDZ binding domain modulates the function and localization of Kv1.3. We created a mutant form of Kv1.3 that lacked the last three amino acids of the C-terminal PDZ-binding domain (Kv1.3ΔTDV). This form of Kv1.3 did not bind the PDZ domain containing protein, PSD95. We transfected wild type and mutant Kv1.3 into HEK293 cells and determined if the mutation affected current, Golgi localization, and surface expression of the channel. We found that cells transfected with Kv1.3ΔTDV had greater current and lower Golgi localization than those transfected with Kv1.3. Truncation of the C-terminal PDZ domain did not affect surface expression of Kv1.3. These findings suggest that PDZ-dependent interactions affect both Kv1.3 localization and function. The finding that current and Golgi localization changed without a corresponding change in surface expression suggests that PDZ interactions affect localization and function via independent mechanisms.
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