The Phosphorylation of Kv1.3: A Modulatory Mechanism for a Multifunctional Ion Channel
The voltage-gated potassium channel Kv1.3 plays a pivotal role in a myriad of biological processes, including cell proliferation, differentiation, and apoptosis. Kv1.3 undergoes fine-tuned regulation, and its altered expression or function correlates with tumorigenesis and cancer progression. Moreov...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-05-01
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| Series: | Cancers |
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| Online Access: | https://www.mdpi.com/2072-6694/15/10/2716 |
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| author | María Navarro-Pérez Irene Estadella Anna Benavente-Garcia Ruth Orellana-Fernández Anna Petit Joan Carles Ferreres Antonio Felipe |
| author_facet | María Navarro-Pérez Irene Estadella Anna Benavente-Garcia Ruth Orellana-Fernández Anna Petit Joan Carles Ferreres Antonio Felipe |
| author_sort | María Navarro-Pérez |
| collection | DOAJ |
| description | The voltage-gated potassium channel Kv1.3 plays a pivotal role in a myriad of biological processes, including cell proliferation, differentiation, and apoptosis. Kv1.3 undergoes fine-tuned regulation, and its altered expression or function correlates with tumorigenesis and cancer progression. Moreover, posttranslational modifications (PTMs), such as phosphorylation, have evolved as rapid switch-like moieties that tightly modulate channel activity. In addition, kinases are promising targets in anticancer therapies. The diverse serine/threonine and tyrosine kinases function on Kv1.3 and the effects of its phosphorylation vary depending on multiple factors. For instance, Kv1.3 regulatory subunits (KCNE4 and Kvβ) can be phosphorylated, increasing the complexity of channel modulation. Scaffold proteins allow the Kv1.3 channelosome and kinase to form protein complexes, thereby favoring the attachment of phosphate groups. This review compiles the network triggers and signaling pathways that culminate in Kv1.3 phosphorylation. Alterations to Kv1.3 expression and its phosphorylation are detailed, emphasizing the importance of this channel as an anticancer target. Overall, further research on Kv1.3 kinase-dependent effects should be addressed to develop effective antineoplastic drugs while minimizing side effects. This promising field encourages basic cancer research while inspiring new therapy development. |
| first_indexed | 2024-03-11T03:53:20Z |
| format | Article |
| id | doaj.art-f929cc990ebb4766abf34538b01af02f |
| institution | Directory Open Access Journal |
| issn | 2072-6694 |
| language | English |
| last_indexed | 2024-03-11T03:53:20Z |
| publishDate | 2023-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cancers |
| spelling | doaj.art-f929cc990ebb4766abf34538b01af02f2023-11-18T00:47:54ZengMDPI AGCancers2072-66942023-05-011510271610.3390/cancers15102716The Phosphorylation of Kv1.3: A Modulatory Mechanism for a Multifunctional Ion ChannelMaría Navarro-Pérez0Irene Estadella1Anna Benavente-Garcia2Ruth Orellana-Fernández3Anna Petit4Joan Carles Ferreres5Antonio Felipe6Molecular Physiology Laboratory, Departament de Bioquímica i Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028 Barcelona, SpainMolecular Physiology Laboratory, Departament de Bioquímica i Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028 Barcelona, SpainMolecular Physiology Laboratory, Departament de Bioquímica i Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028 Barcelona, SpainDepartament de Patologia, Hospital de la Santa Creu i Sant Pau, 08041 Barcelona, SpainDepartament de Patologia, Hospital Universitari de Bellvitge, IDIBELL, L’Hospitalet del Llobregat, 08908 Barcelona, SpainServei d’Anatomia Patològica, Parc Taulí Hospital Universitari, Institut d’Investigació i Innovació Parc Taulí (I3PT-CERCA), 08208 Sabadell, SpainMolecular Physiology Laboratory, Departament de Bioquímica i Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028 Barcelona, SpainThe voltage-gated potassium channel Kv1.3 plays a pivotal role in a myriad of biological processes, including cell proliferation, differentiation, and apoptosis. Kv1.3 undergoes fine-tuned regulation, and its altered expression or function correlates with tumorigenesis and cancer progression. Moreover, posttranslational modifications (PTMs), such as phosphorylation, have evolved as rapid switch-like moieties that tightly modulate channel activity. In addition, kinases are promising targets in anticancer therapies. The diverse serine/threonine and tyrosine kinases function on Kv1.3 and the effects of its phosphorylation vary depending on multiple factors. For instance, Kv1.3 regulatory subunits (KCNE4 and Kvβ) can be phosphorylated, increasing the complexity of channel modulation. Scaffold proteins allow the Kv1.3 channelosome and kinase to form protein complexes, thereby favoring the attachment of phosphate groups. This review compiles the network triggers and signaling pathways that culminate in Kv1.3 phosphorylation. Alterations to Kv1.3 expression and its phosphorylation are detailed, emphasizing the importance of this channel as an anticancer target. Overall, further research on Kv1.3 kinase-dependent effects should be addressed to develop effective antineoplastic drugs while minimizing side effects. This promising field encourages basic cancer research while inspiring new therapy development.https://www.mdpi.com/2072-6694/15/10/2716K+ channelscancerphosphorylation |
| spellingShingle | María Navarro-Pérez Irene Estadella Anna Benavente-Garcia Ruth Orellana-Fernández Anna Petit Joan Carles Ferreres Antonio Felipe The Phosphorylation of Kv1.3: A Modulatory Mechanism for a Multifunctional Ion Channel Cancers K+ channels cancer phosphorylation |
| title | The Phosphorylation of Kv1.3: A Modulatory Mechanism for a Multifunctional Ion Channel |
| title_full | The Phosphorylation of Kv1.3: A Modulatory Mechanism for a Multifunctional Ion Channel |
| title_fullStr | The Phosphorylation of Kv1.3: A Modulatory Mechanism for a Multifunctional Ion Channel |
| title_full_unstemmed | The Phosphorylation of Kv1.3: A Modulatory Mechanism for a Multifunctional Ion Channel |
| title_short | The Phosphorylation of Kv1.3: A Modulatory Mechanism for a Multifunctional Ion Channel |
| title_sort | phosphorylation of kv1 3 a modulatory mechanism for a multifunctional ion channel |
| topic | K+ channels cancer phosphorylation |
| url | https://www.mdpi.com/2072-6694/15/10/2716 |
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