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Subunit organization and functional transitions in Ci-VSP

Nature Structural & Molecular Biology volume 15, pages 106108 (2008) | Download Citation

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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.

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References

  1. 1.

    , , , & Nature 435, 1239–1243 (2005).

  2. 2.

    , & Science 312, 589–592 (2006).

  3. 3.

    , , & Nature 440, 1213–1216 (2006).

  4. 4.

    , & Nature 413, 809–813 (2001).

  5. 5.

    , & Science 309, 897–903 (2005).

  6. 6.

    , & Annu. Rev. Cell Dev. Biol. 22, 23–52 (2006).

  7. 7.

    et al. Cell 99, 323–334 (1999).

  8. 8.

    & Nat. Methods 4, 319–321 (2007).

  9. 9.

    & J. Gen. Physiol. 115, 257–268 (2000).

  10. 10.

    & J. Gen. Physiol. 111, 313–342 (1998).

  11. 11.

    , , & Neuron 20, 1283–1294 (1998).

  12. 12.

    & J. Gen. Physiol. 113, 389–414 (1999).

  13. 13.

    , , & J. Gen. Physiol. 125, 57–69 (2005).

  14. 14.

    & J. Physiol. 583, 875–889 (2007).

  15. 15.

    , & Science 271, 213–216 (1996).

  16. 16.

    & Neuron 19, 1127–1140 (1997).

  17. 17.

    et al. PLoS ONE [online] 2, e440 (2007).

  18. 18.

    et al. Nature 423, 33–41 (2003).

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Acknowledgements

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.

Author information

Affiliations

  1. Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.

    • Susy C Kohout
    • , Maximilian H Ulbrich
    •  & Ehud Y Isacoff
  2. Department of Chemical Biology Graduate Program, University of California, Berkeley, California 94720, USA.

    • Sarah C Bell
    •  & Ehud Y Isacoff
  3. Material Science Division and Physical Bioscience Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.

    • Ehud Y Isacoff

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Corresponding author

Correspondence to Ehud Y Isacoff.

Supplementary information

PDF files

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    Supplementary Text and Figures

    Supplementary Figures 1–3, Supplementary Discussion, Supplementary Methods

Videos

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    Supplementary Video 1

    TIRF microscopy movie of oocyte coexpressing Ci-VSP-GFP-Kv1.4C and PSD-95

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DOI

https://doi.org/10.1038/nsmb1320

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