KV1.5–KV 1.3 Recycling Is PKC-Dependent
EntityUAM. Departamento de Enfermería; Instituto de Investigaciones Biomédicas "Alberto Sols" (IIBM); Instituto de Investigación Sanitaria Hospital Universitario de La Paz (IdiPAZ)
PublisherMDPI, Basel, Switzerland
10.3390/ijms22031336International Journal of Molecular Sciences 22.3 (2021): 1336
Funded byThis research was funded by Ministerio de Ciencia e Innovación (MICINN) Spain SAF2016-75021-R and PID2019-104366RB-C21 (to C.V. and T.G.), the Instituto de Salud Carlos III CIBERCV program CB/11/00222 (to C.V.), and the Consejo Superior de Investigaciones Científicas grants: PIE 201820E104 and 2019AEP148 (to C.V.). The cost of this publication was paid in part by funds from the European Fund for Economic and Regional Development (FEDER). A.M. holds a postdoctoral contract at CNIC. A.d.l.C. and D.A.P. held CSIC contracts. A.d.B.-B. holds an MICINN predoctoral contract (BES-2017-080184)
ProjectGobierno de España. SAF2016-75021-R; Gobierno de España. PID2019-104366RB-C21; Gobierno de España. CB/11/00222
Editor's Versionhttps://doi.org/10.3390 /ijms22031336
SubjectsBisindolylmaleimide II; Calphostin C; K 1.5 V; K β1.3 V; PKC; RACK1; Traffic; Enfermería
Rights© 2021 The authors
Esta obra está bajo una Licencia Creative Commons Atribución 4.0 Internacional.
KV1.5 channel function is modified by different regulatory subunits. KVβ1.3 subunits assemble with KV1.5 channels and induce a fast and incomplete inactivation. Inhibition of PKC abolishes the KVβ1.3-induced fast inactivation, decreases the amplitude of the current KV1.5–KVβ1.3 and modifies their pharmacology likely due to changes in the traffic of KV1.5–KVβ1.3 channels in a PKC-dependent manner. In order to analyze this hypothesis, HEK293 cells were transfected with KV1.5–KVβ1.3 channels, and currents were recorded by whole-cell configuration of the patch-clamp technique. The presence of KV1.5 in the membrane was analyzed by biotinylation techniques, live cell imaging and confocal microscopy approaches. PKC inhibition resulted in a decrease of 33 ± 7% of channels in the cell surface due to reduced recycling to the plasma membrane, as was confirmed by confocal microscopy. Live cell imaging indicated that PKC inhibition almost abolished the recycling of the KV1.5–KVβ1.3 channels, generating an accumulation of channels into the cytoplasm. All these results suggest that the trafficking regulation of KV1.5–KVβ1.3 channels is dependent on phosphorylation by PKC and, therefore, they could represent a clinically relevant issue, mainly in those diseases that exhibit modifications in PKC activity.
Google Scholar:Macias, Alvaro - Cruz, Alicia de la - Peraza, Diego A. - Benito-Bueno, Angela de - González Gallego, Teresa - Valenzuela, Carmen
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