Skip to main content

The Effective Calcium/Calmodulin Concentration Determines the Sensitivity of CaMKII to the Frequency of Calcium Oscillations

  • Conference paper
Information Processign in Cells and Tissues (IPCAT 2012)

Part of the book series: Lecture Notes in Computer Science ((LNTCS,volume 7223))

Abstract

Calcium/calmodulin-dependent protein kinase II (CaMKII) is involved in the induction of many forms of synaptic plasticity in the brain. Experimental and computational studies have shown that CaMKII is sensitive to the frequency of oscillatory Ca2 +  signals. Here we demonstrate that in a simple, commonly used kinetic model of CaMKII phosphorylation, the overall phosphorylation rate under sustained application of Ca4 − CaM pulses ultimately depends on the average (‘effective’) concentration of Ca4 − CaM in the system, rather than on the pulse frequency itself. As a corollary, equal phosphorylation levels are achieved in response to pulsed and constant applications of equal effective concentrations of Ca4 − CaM.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 54.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 69.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Hanson, P., Schulman, H.: Neuronal Ca2+/calmodulin-dependent protein kinases. Annual Review of Biochemistry 61(1), 559–601 (1992)

    Article  Google Scholar 

  2. Hanson, P., Meyer, T., Stryer, L., Schulman, H.: Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals. Neuron 12(5), 943–956 (1994)

    Article  Google Scholar 

  3. Michelson, S., Schulman, H.: CaM kinase: A model for its activation and dynamics. Journal of Theoretical Biology 171, 281–290 (1994)

    Article  Google Scholar 

  4. Dosemeci, A., Albers, R.: A mechanism for synaptic frequency detection through autophosphorylation of CaM kinase II. Biophysical Journal 70(6), 2493–2501 (1996)

    Article  Google Scholar 

  5. Dupont, G., Houart, G., De Koninck, P.: Sensitivity of CaM kinase II to the frequency of Ca2+ oscillations: a simple model. Cell Calcium 34(6), 485–497 (2003)

    Article  Google Scholar 

  6. De Koninck, P., Schulman, H.: Sensitivity of CaM kinase II to the frequency of Ca2+ oscillations. Science 279(5348), 227–230 (1998)

    Article  Google Scholar 

  7. Waxham, M., Putkey, J., Tsai, A.: A mechanism for calmodulin (CaM) trapping by CaM-kinase II defined by a family of CaM-binding peptides. Journal of Biological Chemistry 273(28), 17579–17584 (1998)

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2012 Springer-Verlag Berlin Heidelberg

About this paper

Cite this paper

Pinto, T.M., Schilstra, M.J., Steuber, V. (2012). The Effective Calcium/Calmodulin Concentration Determines the Sensitivity of CaMKII to the Frequency of Calcium Oscillations. In: Lones, M.A., Smith, S.L., Teichmann, S., Naef, F., Walker, J.A., Trefzer, M.A. (eds) Information Processign in Cells and Tissues. IPCAT 2012. Lecture Notes in Computer Science, vol 7223. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-28792-3_17

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-28792-3_17

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-28791-6

  • Online ISBN: 978-3-642-28792-3

  • eBook Packages: Computer ScienceComputer Science (R0)

Publish with us

Policies and ethics