Subunit organization and functional transitions in Ci-VSP

Susy C. Kohout; Maximilian H. Ulbrich; Sarah C. Bell; Ehud Y. Isacoff

doi:10.1038/nsmb1320

Subunit organization and functional transitions in Ci-VSP

Susy C. Kohout
, Maximilian H. Ulbrich
, Sarah C. Bell
, Ehud Y. Isacoff

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

125 Scopus citations

Abstract

Voltage-sensing domains (VSDs) confer voltage dependence on effector domains of membrane proteins. Ion channels use four VSDs to control a gate in the pore domain, but in the recently discovered phosphatase Ci-VSP, the number of subunits has been unknown. Using single-molecule microscopy to count subunits and voltage clamp fluorometry to detect structural dynamics, we found Ci-VSP to be a monomer, which operates independently, but nevertheless undergoes multiple voltage-dependent conformational transitions.

Original language	English (US)
Pages (from-to)	106-108
Number of pages	3
Journal	Nature Structural and Molecular Biology
Volume	15
Issue number	1
DOIs	https://doi.org/10.1038/nsmb1320
State	Published - Jan 2008
Externally published	Yes

All Science Journal Classification (ASJC) codes

Structural Biology
Molecular Biology

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title = "Subunit organization and functional transitions in Ci-VSP",

abstract = "Voltage-sensing domains (VSDs) confer voltage dependence on effector domains of membrane proteins. Ion channels use four VSDs to control a gate in the pore domain, but in the recently discovered phosphatase Ci-VSP, the number of subunits has been unknown. Using single-molecule microscopy to count subunits and voltage clamp fluorometry to detect structural dynamics, we found Ci-VSP to be a monomer, which operates independently, but nevertheless undergoes multiple voltage-dependent conformational transitions.",

author = "Kohout, \{Susy C.\} and Ulbrich, \{Maximilian H.\} and Bell, \{Sarah C.\} and Isacoff, \{Ehud Y.\}",

note = "Funding Information: This work was supported by a postdoctoral fellowship (to M.H.U.) from the American Heart Association, and by grant R01NS035549 from the US National Institutes of Health. We thank Y. Okamura (Japanese National Institute for Physiological Sciences) for kindly providing the Ci-VSP cDNA and F. Tombola, H. Janovjak, M. Pathak and S. Pautot for technical assistance and helpful discussions.",

year = "2008",

month = jan,

doi = "10.1038/nsmb1320",

language = "English (US)",

volume = "15",

pages = "106--108",

journal = "Nature Structural and Molecular Biology",

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AU - Kohout, Susy C.

AU - Ulbrich, Maximilian H.

AU - Bell, Sarah C.

AU - Isacoff, Ehud Y.

N1 - Funding Information: This work was supported by a postdoctoral fellowship (to M.H.U.) from the American Heart Association, and by grant R01NS035549 from the US National Institutes of Health. We thank Y. Okamura (Japanese National Institute for Physiological Sciences) for kindly providing the Ci-VSP cDNA and F. Tombola, H. Janovjak, M. Pathak and S. Pautot for technical assistance and helpful discussions.

PY - 2008/1

Y1 - 2008/1

N2 - Voltage-sensing domains (VSDs) confer voltage dependence on effector domains of membrane proteins. Ion channels use four VSDs to control a gate in the pore domain, but in the recently discovered phosphatase Ci-VSP, the number of subunits has been unknown. Using single-molecule microscopy to count subunits and voltage clamp fluorometry to detect structural dynamics, we found Ci-VSP to be a monomer, which operates independently, but nevertheless undergoes multiple voltage-dependent conformational transitions.

AB - Voltage-sensing domains (VSDs) confer voltage dependence on effector domains of membrane proteins. Ion channels use four VSDs to control a gate in the pore domain, but in the recently discovered phosphatase Ci-VSP, the number of subunits has been unknown. Using single-molecule microscopy to count subunits and voltage clamp fluorometry to detect structural dynamics, we found Ci-VSP to be a monomer, which operates independently, but nevertheless undergoes multiple voltage-dependent conformational transitions.

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EP - 108

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 1

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Subunit organization and functional transitions in Ci-VSP

Abstract

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