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Related Experiment Videos

Intracellular calmodulin availability accessed with two-photon cross-correlation.

Sally A Kim1, Katrin G Heinze, M Neal Waxham

  • 1Department of Neurobiology and Anatomy, University of Texas Health Science Center, Houston, TX 77030-1501, USA.

Proceedings of the National Academy of Sciences of the United States of America
|December 30, 2003
PubMed
Summary
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Cellular conditions dynamically alter calmodulin (CaM) availability and its interactions with Ca(2+)/CaM-dependent protein kinase II. Advanced spectroscopy reveals protein behavior in living cells.

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Molecular Signaling

Background:

  • Signaling protein availability and interactions are precisely regulated in time and space.
  • Calmodulin (CaM) is a crucial transducer of intracellular calcium (Ca2+) signaling.
  • CaM binding to targets initiates signaling cascades and affects its own localization and availability.

Purpose of the Study:

  • To investigate the dynamic interactions and mobility of CaM and Ca(2+)/CaM-dependent protein kinase II (CaMKII).
  • To compare these interactions in solution versus within living cells.
  • To demonstrate the utility of advanced spectroscopic techniques for studying protein behavior in native cellular environments.

Main Methods:

  • Utilized two-photon fluorescence correlation spectroscopy (FCS) and cross-correlation spectroscopy (FCCS).

Related Experiment Videos

  • Compared CaM and CaMKII mobility and molecular interactions.
  • Studied protein behavior in both solution and living cells.

    • Main Results:

    • CaM availability in cells is sensitive to changes in intracellular conditions.
    • CaMKII exhibits unique properties, including autophosphorylation-dependent CaM affinity increase and Ca(2+)/CaM-induced translocation.
    • FCCS provides insights into protein-protein interactions within the native cellular milieu.

    Conclusions:

    • Cellular conditions significantly impact CaM availability and its interactions with CaMKII.
    • Two-photon FCCS is a powerful, generally applicable method for studying protein-protein interactions in living cells.
    • This approach allows for the investigation of signaling pathway heterogeneities across different cellular compartments.