Next Article in Journal
Isolation and Characterization of a Green-Tissue Promoter from Common Wild Rice (Oryza rufipogon Griff.)
Next Article in Special Issue
Effects of Sunitinib and Other Kinase Inhibitors on Cells Harboring a PDGFRB Mutation Associated with Infantile Myofibromatosis
Previous Article in Journal
Plant MicroRNAs in Cross-Kingdom Regulation of Gene Expression
Previous Article in Special Issue
Cecropin A Modulates Tight Junction-Related Protein Expression and Enhances the Barrier Function of Porcine Intestinal Epithelial Cells by Suppressing the MEK/ERK Pathway
Article Menu
Issue 7 (July) cover image

Export Article

Open AccessCommunication
Int. J. Mol. Sci. 2018, 19(7), 2008; https://doi.org/10.3390/ijms19072008

ERK5 Phosphorylates Kv4.2 and Inhibits Inactivation of the A-Type Current in PC12 Cells

1
Department of Pharmacology, Yamagata University School of Medicine, Yamagata 990-9585, Japan
2
Department of Pharmacology, Kyoto University Graduate School of Medicine, Kyoto 606-8501, Japan
*
Author to whom correspondence should be addressed.
Received: 14 June 2018 / Revised: 28 June 2018 / Accepted: 28 June 2018 / Published: 10 July 2018
Full-Text   |   PDF [1359 KB, uploaded 10 July 2018]   |  

Abstract

Extracellular signal-regulated kinase 5 (ERK5) regulates diverse physiological responses such as proliferation, differentiation, and gene expression. Previously, we demonstrated that ERK5 is essential for neurite outgrowth and catecholamine biosynthesis in PC12 cells and sympathetic neurons. However, it remains unclear how ERK5 regulates the activity of ion channels, which are important for membrane excitability. Thus, we examined the effect of ERK5 on the ion channel activity in the PC12 cells that overexpress both ERK5 and the constitutively active MEK5 mutant. The gene and protein expression levels of voltage-dependent Ca2+ and K+ channels were determined by RT-qPCR or Western blotting. The A-type K+ current was recorded using the whole-cell patch clamp method. In these ERK5-activated cells, the gene expression levels of voltage-dependent L- and P/Q-type Ca2+ channels did not alter, but the N-type Ca2+ channel was slightly reduced. In contrast, those of Kv4.2 and Kv4.3, which are components of the A-type current, were significantly enhanced. Unexpectedly, the protein levels of Kv4.2 were not elevated by ERK5 activation, but the phosphorylation levels were increased by ERK5 activation. By electrophysiological analysis, the inactivation time constant of the A-type current was prolonged by ERK5 activation, without changes in the peak current. Taken together, ERK5 inhibits an inactivation of the A-type current by phosphorylation of Kv4.2, which may contribute to the neuronal differentiation process. View Full-Text
Keywords: extracellular signal-regulated kinase 5 (ERK5); Kv4.2; PC12 cells extracellular signal-regulated kinase 5 (ERK5); Kv4.2; PC12 cells
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Kashino, Y.; Obara, Y.; Okamoto, Y.; Saneyoshi, T.; Hayashi, Y.; Ishii, K. ERK5 Phosphorylates Kv4.2 and Inhibits Inactivation of the A-Type Current in PC12 Cells. Int. J. Mol. Sci. 2018, 19, 2008.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top