ArticleThe Journal of biological chemistry2015
Alternatively Spliced Isoforms of KV10.1 Potassium Channels Modulate Channel Properties and Can Activate Cyclin-dependent Kinase in Xenopus Oocytes.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- The Kv10.1 Channel: A Promising Target in Cancer.International journal of molecular sciences · 2022Review
- Osmoregulation and the Hypothalamic Supraoptic Nucleus: From Genes to Functions.Frontiers in physiology · 2022Review
- Kv10.1 Regulates Microtubule Dynamics during Mitosis.Cancers · 2020Article
- Induction of a Spindle-Assembly-Competent M Phase in Xenopus Egg Extracts.Current biology : CB · 2019Article
- Regulation of Eag by CaJournal of neurophysiology · 2018Article
- Eag1 KOxidative medicine and cellular longevity · 2017Review
- In vivo imaging of tumour xenografts with an antibody targeting the potassium channel KEuropean biophysics journal : EBJ · 2016Article
- Kv10.1 K(+) channel: from physiology to cancer.Pflugers Archiv : European journal of physiology · 2016Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
KV10.1 is a voltage-gated potassium channel expressed selectively in the mammalian brain but also aberrantly in cancer cells. In this study we identified short splice variants of KV10.1 resulting from exon-skipping events (E65 and E70) in human brain and cancer cell lines. The presence of the variants was confirmed by Northern blot and RNase protection assays. Both variants completely lacked the transmembrane domains of the channel and produced cytoplasmic proteins without channel function. In a reconstituted system, both variants co-precipitated with the full-length channel and induced a robust down-regulation of KV10.1 current when co-expressed with the full-length form, but their effect was mechanistically different. E65 required a tetramerization domain and induced a reduction in the overall expression of full-length KV10.1, whereas E70 mainly affected its glycosylation pattern. E65 triggered the activation of cyclin-dependent kinases in Xenopus laevis oocytes, suggesting a role in cell cycle control. Our observations highlight the relevance of noncanonical functions for the oncogenicity of KV10.1, which need to be considered when ion channels are targeted for cancer therapy.
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Registered trials
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