Modulation of Actin Filament Dynamics by Inward Rectifying of Potassium Channel Kir2.1

Lida Wu; Quanyi Wang; Junzhong Gu; Huiyuan Zhang; Yuchun Gu

doi:10.3390/ijms21207479

Modulation of Actin Filament Dynamics by Inward Rectifying of Potassium Channel Kir2.1

Lida Wu, Quanyi Wang, Junzhong Gu, Huiyuan Zhang, Yuchun Gu^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

Apart from its ion channel properties, the Kir2.1 channel has been found in tumors and cancer cells to facilitate cancer cell motility. It is assumed that Kir2.1 might be associated with cell actin filament dynamics. With the help of structured illumination microscopy (SIM), we show that Kir2.1 overexpression promotes actin filament dynamics, cell invasion, and adhesion. Mutated Kir2.1 channels, with impaired membrane expression, present much weaker actin regulatory effects, which indicates that precise Kir2.1 membrane localization is key to its actin filament remolding effect. It is found that Kir2.1 membrane expression and anchoring are associated with PIP2 affinity, and PIP2 depletion inhibits actin filament dynamics. We also report that membrane-expressed Kir2.1 regulates redistribution and phosphorylation of FLNA (filamin A), which may be the mechanism underlying Kir2.1 and actin filament dynamics. In conclusion, Kir2.1 membrane localization regulates cell actin filaments, and not the ion channel properties. These data indicate that Kir2.1 may have additional cellular functions distinct from the regulation of excitability, which provides new insight into the study of channel proteins.

Original language	English
Article number	7479
Pages (from-to)	1-14
Number of pages	14
Journal	International Journal of Molecular Sciences
Volume	21
Issue number	20
DOIs	https://doi.org/10.3390/ijms21207479
Publication status	Published - 10 Oct 2020

Bibliographical note

© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access
article distributed under the terms and conditions of the Creative Commons Attribution
(CC BY) license (http://creativecommons.org/licenses/by/4.0/).

Keywords

Actin filament dynamics
Filamin A
Kir2.1
PIP2

Access to Document

10.3390/ijms21207479Licence: CC BY 3.0

Modulation of Actin Filament Dynamics
© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
Final published version, 1.68 MBLicence: CC BY 3.0

Cite this

@article{3954b380d3374a4aa3080d5d5e97b34f,

title = "Modulation of Actin Filament Dynamics by Inward Rectifying of Potassium Channel Kir2.1",

abstract = "Apart from its ion channel properties, the Kir2.1 channel has been found in tumors and cancer cells to facilitate cancer cell motility. It is assumed that Kir2.1 might be associated with cell actin filament dynamics. With the help of structured illumination microscopy (SIM), we show that Kir2.1 overexpression promotes actin filament dynamics, cell invasion, and adhesion. Mutated Kir2.1 channels, with impaired membrane expression, present much weaker actin regulatory effects, which indicates that precise Kir2.1 membrane localization is key to its actin filament remolding effect. It is found that Kir2.1 membrane expression and anchoring are associated with PIP2 affinity, and PIP2 depletion inhibits actin filament dynamics. We also report that membrane-expressed Kir2.1 regulates redistribution and phosphorylation of FLNA (filamin A), which may be the mechanism underlying Kir2.1 and actin filament dynamics. In conclusion, Kir2.1 membrane localization regulates cell actin filaments, and not the ion channel properties. These data indicate that Kir2.1 may have additional cellular functions distinct from the regulation of excitability, which provides new insight into the study of channel proteins.",

keywords = "Actin filament dynamics, Filamin A, Kir2.1, PIP2",

author = "Lida Wu and Quanyi Wang and Junzhong Gu and Huiyuan Zhang and Yuchun Gu",

note = "{\textcopyright} 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).",

year = "2020",

month = oct,

day = "10",

doi = "10.3390/ijms21207479",

language = "English",

volume = "21",

pages = "1--14",

journal = "International Journal of Molecular Sciences",

issn = "1661-6596",

publisher = "MDPI AG",

number = "20",

}

TY - JOUR

T1 - Modulation of Actin Filament Dynamics by Inward Rectifying of Potassium Channel Kir2.1

AU - Wu, Lida

AU - Wang, Quanyi

AU - Gu, Junzhong

AU - Zhang, Huiyuan

AU - Gu, Yuchun

N1 - © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

PY - 2020/10/10

Y1 - 2020/10/10

N2 - Apart from its ion channel properties, the Kir2.1 channel has been found in tumors and cancer cells to facilitate cancer cell motility. It is assumed that Kir2.1 might be associated with cell actin filament dynamics. With the help of structured illumination microscopy (SIM), we show that Kir2.1 overexpression promotes actin filament dynamics, cell invasion, and adhesion. Mutated Kir2.1 channels, with impaired membrane expression, present much weaker actin regulatory effects, which indicates that precise Kir2.1 membrane localization is key to its actin filament remolding effect. It is found that Kir2.1 membrane expression and anchoring are associated with PIP2 affinity, and PIP2 depletion inhibits actin filament dynamics. We also report that membrane-expressed Kir2.1 regulates redistribution and phosphorylation of FLNA (filamin A), which may be the mechanism underlying Kir2.1 and actin filament dynamics. In conclusion, Kir2.1 membrane localization regulates cell actin filaments, and not the ion channel properties. These data indicate that Kir2.1 may have additional cellular functions distinct from the regulation of excitability, which provides new insight into the study of channel proteins.

AB - Apart from its ion channel properties, the Kir2.1 channel has been found in tumors and cancer cells to facilitate cancer cell motility. It is assumed that Kir2.1 might be associated with cell actin filament dynamics. With the help of structured illumination microscopy (SIM), we show that Kir2.1 overexpression promotes actin filament dynamics, cell invasion, and adhesion. Mutated Kir2.1 channels, with impaired membrane expression, present much weaker actin regulatory effects, which indicates that precise Kir2.1 membrane localization is key to its actin filament remolding effect. It is found that Kir2.1 membrane expression and anchoring are associated with PIP2 affinity, and PIP2 depletion inhibits actin filament dynamics. We also report that membrane-expressed Kir2.1 regulates redistribution and phosphorylation of FLNA (filamin A), which may be the mechanism underlying Kir2.1 and actin filament dynamics. In conclusion, Kir2.1 membrane localization regulates cell actin filaments, and not the ion channel properties. These data indicate that Kir2.1 may have additional cellular functions distinct from the regulation of excitability, which provides new insight into the study of channel proteins.

KW - Actin filament dynamics

KW - Filamin A

KW - Kir2.1

KW - PIP2

UR - https://www.mdpi.com/1422-0067/21/20/7479

UR - http://www.scopus.com/inward/record.url?scp=85092405175&partnerID=8YFLogxK

U2 - 10.3390/ijms21207479

DO - 10.3390/ijms21207479

M3 - Article

SN - 1661-6596

VL - 21

SP - 1

EP - 14

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

IS - 20

M1 - 7479

ER -

Modulation of Actin Filament Dynamics by Inward Rectifying of Potassium Channel Kir2.1

Abstract

Bibliographical note

Keywords

Access to Document

Other files and links

Fingerprint

Cite this