A single amino acid gates the KcsA channel

Minako Hirano; Daichi Okuno; Yukiko Onishi; Toru Ide

doi:10.1016/j.bbrc.2014.07.032

A single amino acid gates the KcsA channel

Minako Hirano, Daichi Okuno, Yukiko Onishi, Toru Ide

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

6 Citations (Scopus)

Abstract

The KcsA channel is a proton-Activated potassium channel. We have previously shown that the cytoplasmic domain (CPD) acts as a pH-sensor, and the charged states of certain negatively charged amino acids in the CPD play an important role in regulating the pH-dependent gating. Here, we demonstrate the KcsA channel is constitutively open independent of pH upon mutating E146 to a neutrally charged amino acid. In addition, we found that rearrangement of the CPD following this mutation was not large. Our results indicate that minimal rearrangement of the CPD, particularly around E146, is sufficient for opening of the KcsA channel.

Original language	English
Pages (from-to)	1537-1540
Number of pages	4
Journal	Biochemical and Biophysical Research Communications
Volume	450
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2014.07.032
Publication status	Published - Aug 8 2014

Keywords

Ion channel
KcsA channel
Rearrangement
Single-channel recording
pH-dependent gating

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2014.07.032

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title = "A single amino acid gates the KcsA channel",

abstract = "The KcsA channel is a proton-Activated potassium channel. We have previously shown that the cytoplasmic domain (CPD) acts as a pH-sensor, and the charged states of certain negatively charged amino acids in the CPD play an important role in regulating the pH-dependent gating. Here, we demonstrate the KcsA channel is constitutively open independent of pH upon mutating E146 to a neutrally charged amino acid. In addition, we found that rearrangement of the CPD following this mutation was not large. Our results indicate that minimal rearrangement of the CPD, particularly around E146, is sufficient for opening of the KcsA channel.",

keywords = "Ion channel, KcsA channel, Rearrangement, Single-channel recording, pH-dependent gating",

author = "Minako Hirano and Daichi Okuno and Yukiko Onishi and Toru Ide",

note = "Funding Information: We thank Dr. Peter Karagiannis for carefully revising the manuscript. This work was supported by JSPS KAKENHI Grand Number 22370059 , 23770190 , 24657110 and 25840055 , MEXT KAKENHI Grand Number 23113519 , Grants-in-aid for Scientific Research of Foundation Advanced Technology Institute (ATI), The Science Research Promotion Fund of The Promotion and Mutual Aid Corporation for Private Schools of Japan, The Uehara Memorial Foundation , Grant for Basic Science Research Projects from The Sumitomo Foundation , Kowa Life Science Foundation , and the Center of Innovation Program from Japan Science and Technology Agency , JST.",

year = "2014",

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doi = "10.1016/j.bbrc.2014.07.032",

language = "English",

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T1 - A single amino acid gates the KcsA channel

AU - Hirano, Minako

AU - Okuno, Daichi

AU - Onishi, Yukiko

AU - Ide, Toru

N1 - Funding Information: We thank Dr. Peter Karagiannis for carefully revising the manuscript. This work was supported by JSPS KAKENHI Grand Number 22370059 , 23770190 , 24657110 and 25840055 , MEXT KAKENHI Grand Number 23113519 , Grants-in-aid for Scientific Research of Foundation Advanced Technology Institute (ATI), The Science Research Promotion Fund of The Promotion and Mutual Aid Corporation for Private Schools of Japan, The Uehara Memorial Foundation , Grant for Basic Science Research Projects from The Sumitomo Foundation , Kowa Life Science Foundation , and the Center of Innovation Program from Japan Science and Technology Agency , JST.

PY - 2014/8/8

Y1 - 2014/8/8

N2 - The KcsA channel is a proton-Activated potassium channel. We have previously shown that the cytoplasmic domain (CPD) acts as a pH-sensor, and the charged states of certain negatively charged amino acids in the CPD play an important role in regulating the pH-dependent gating. Here, we demonstrate the KcsA channel is constitutively open independent of pH upon mutating E146 to a neutrally charged amino acid. In addition, we found that rearrangement of the CPD following this mutation was not large. Our results indicate that minimal rearrangement of the CPD, particularly around E146, is sufficient for opening of the KcsA channel.

AB - The KcsA channel is a proton-Activated potassium channel. We have previously shown that the cytoplasmic domain (CPD) acts as a pH-sensor, and the charged states of certain negatively charged amino acids in the CPD play an important role in regulating the pH-dependent gating. Here, we demonstrate the KcsA channel is constitutively open independent of pH upon mutating E146 to a neutrally charged amino acid. In addition, we found that rearrangement of the CPD following this mutation was not large. Our results indicate that minimal rearrangement of the CPD, particularly around E146, is sufficient for opening of the KcsA channel.

KW - Ion channel

KW - KcsA channel

KW - Rearrangement

KW - Single-channel recording

KW - pH-dependent gating

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JO - Biochemical and Biophysical Research Communications

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ER -

A single amino acid gates the KcsA channel

Abstract

Keywords

ASJC Scopus subject areas

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