Nanodomain Ca2+ of Ca2+ channels detected by a tethered genetically encoded Ca2+ sensor
Lai Hock Tay,
Ivy E. Dick,
Wanjun Yang,
Marco Mank,
Oliver Griesbeck and
David T. Yue ()
Additional contact information
Lai Hock Tay: Calcium Signals Laboratory, Ross Building, Room 713, 720 Rutland Avenue, Baltimore, Maryland 21205-2196, USA.
Ivy E. Dick: Calcium Signals Laboratory, Ross Building, Room 713, 720 Rutland Avenue, Baltimore, Maryland 21205-2196, USA.
Wanjun Yang: Calcium Signals Laboratory, Ross Building, Room 713, 720 Rutland Avenue, Baltimore, Maryland 21205-2196, USA.
Marco Mank: AG Zelluläre Dynamik, Max-Planck-Institut für Neurobiologie
Oliver Griesbeck: AG Zelluläre Dynamik, Max-Planck-Institut für Neurobiologie
David T. Yue: Calcium Signals Laboratory, Ross Building, Room 713, 720 Rutland Avenue, Baltimore, Maryland 21205-2196, USA.
Nature Communications, 2012, vol. 3, issue 1, 1-11
Abstract:
Abstract Coupling of excitation to secretion, contraction and transcription often relies on Ca2+ computations within the nanodomain—a conceptual region extending tens of nanometers from the cytoplasmic mouth of Ca2+ channels. Theory predicts that nanodomain Ca2+ signals differ vastly from the slow submicromolar signals routinely observed in bulk cytoplasm. However, direct visualization of nanodomain Ca2+ far exceeds optical resolution of spatially distributed Ca2+ indicators. Here we couple an optical, genetically encoded Ca2+ indicator (TN–XL) to the carboxy tail of CaV2.2 Ca2+ channels, enabling near-field imaging of the nanodomain. Under total internal reflection fluorescence microscopy, we detect Ca2+ responses indicative of large-amplitude pulses. Single-channel electrophysiology reveals a corresponding Ca2+ influx of only 0.085 pA, and fluorescence resonance energy transfer measurements estimate TN–XL distance to the cytoplasmic mouth at ~55 Å. Altogether, these findings raise the possibility that Ca2+ exits the channel through the analogue of molecular portals, mirroring the crystallographic images of side windows in voltage-gated K channels.
Date: 2012
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/ncomms1777 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms1777
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/ncomms1777
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().