Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor - PubMed (original) (raw)

. 2005 Jun 30;435(7046):1239-43.

doi: 10.1038/nature03650. Epub 2005 May 18.

Affiliations

• PMID: 15902207
• DOI: 10.1038/nature03650

Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor

Yoshimichi Murata et al. Nature. 2005.

Abstract

Changes in membrane potential affect ion channels and transporters, which then alter intracellular chemical conditions. Other signalling pathways coupled to membrane potential have been suggested but their underlying mechanisms are unknown. Here we describe a novel protein from the ascidian Ciona intestinalis that has a transmembrane voltage-sensing domain homologous to the S1-S4 segments of voltage-gated channels and a cytoplasmic domain similar to phosphatase and tensin homologue. This protein, named C. intestinalis voltage-sensor-containing phosphatase (Ci-VSP), displays channel-like 'gating' currents and directly translates changes in membrane potential into the turnover of phosphoinositides. The activity of the phosphoinositide phosphatase in Ci-VSP is tuned within a physiological range of membrane potential. Immunocytochemical studies show that Ci-VSP is expressed in Ciona sperm tail membranes, indicating a possible role in sperm function or morphology. Our data demonstrate that voltage sensing can function beyond channel proteins and thus more ubiquitously than previously realized.

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Comment in

• The secret lives of voltage sensors.
  Ahern CA. Ahern CA. J Physiol. 2007 Sep 15;583(Pt 3):813-4. doi: 10.1113/jphysiol.2007.141077. Epub 2007 Aug 9. J Physiol. 2007. PMID: 17690136 Free PMC article. Review. No abstract available.

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