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Open AccessArticle

KV1.5–KVβ1.3 Recycling Is PKC-Dependent

Instituto de Investigaciones Biomédicas Madrid CSIC-UAM. C/Arturo Duperier 4, 28029 Madrid, Spain
CIBER Enfermedades Cardiovasculares (CIBERCV), Madrid, Spain
Department of Biochemistry, School of Medicine, Universidad Autónoma de Madrid, 28029 Madrid, Spain
Instituto de Investigación Sanitaria del Hospital Universitario La Paz (IdiPAZ), 28029 Madrid, Spain
Authors to whom correspondence should be addressed.
Current address: Centro Nacional de Investigaciones Cardiovasculares (CNIC). C/ Melchor Fernandez Almagro, 3, 28029 Madrid, Spain.
Current address: Department of Physiology and Biophysics, Miller School of Medicine, University of Miami, Coral Gables, FL 33124, USA.
Academic Editor: Antonio Ferrer-Montiel
Int. J. Mol. Sci. 2021, 22(3), 1336;
Received: 17 December 2020 / Revised: 12 January 2021 / Accepted: 26 January 2021 / Published: 29 January 2021
(This article belongs to the Special Issue Membrane Channels in Health and Diseases)
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. View Full-Text
Keywords: KV1.5; KVβ1.3; PKC; calphostin C; RACK1; bisindolylmaleimide II; traffic KV1.5; KVβ1.3; PKC; calphostin C; RACK1; bisindolylmaleimide II; traffic
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MDPI and ACS Style

Macias, A.; de la Cruz, A.; Peraza, D.A.; Benito-Bueno, A.d.; Gonzalez, T.; Valenzuela, C. KV1.5–KVβ1.3 Recycling Is PKC-Dependent. Int. J. Mol. Sci. 2021, 22, 1336.

AMA Style

Macias A, de la Cruz A, Peraza DA, Benito-Bueno Ad, Gonzalez T, Valenzuela C. KV1.5–KVβ1.3 Recycling Is PKC-Dependent. International Journal of Molecular Sciences. 2021; 22(3):1336.

Chicago/Turabian Style

Macias, Alvaro; de la Cruz, Alicia; Peraza, Diego A.; Benito-Bueno, Angela d.; Gonzalez, Teresa; Valenzuela, Carmen. 2021. "KV1.5–KVβ1.3 Recycling Is PKC-Dependent" Int. J. Mol. Sci. 22, no. 3: 1336.

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