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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

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Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Conformational changes of calmodulin upon Ca2+ binding studied with a microfluidic mixer.

Hye Yoon Park1, Sally A Kim, Jonas Korlach

  • 1School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853, USA.

Proceedings of the National Academy of Sciences of the United States of America
|January 8, 2008
PubMed
Summary

This study reveals distinct calmodulin (CaM) domain kinetics upon calcium binding. The C-terminal domain responds rapidly (490 µs), while the N-terminal domain is slower (20 ms), offering insights into CaM regulation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Calmodulin (CaM) is a crucial calcium-binding protein involved in numerous cellular signaling pathways.
  • Understanding the kinetics of CaM conformational changes upon calcium binding is essential for elucidating its regulatory mechanisms.

Purpose of the Study:

  • To investigate the rapid kinetics of calmodulin conformational changes induced by calcium (Ca2+) binding.
  • To differentiate the kinetic rates of Ca2+ binding in the N-terminal and C-terminal domains of calmodulin.

Main Methods:

  • Development and application of a microfluidic mixer for rapid, uniform mixing on microsecond timescales.
  • Utilizing multiphoton microscopy to observe acrylodan-labeled calmodulin dynamics.
  • Kinetic analysis of Ca2+-induced protein transitions.

Main Results:

  • The microfluidic mixer enabled the study of CaM kinetics on the timescale of tens of microseconds.
  • Significant differences in kinetic rates were observed between the two homologous globular domains of CaM.
  • Characteristic time constants were approximately 490 microseconds for the C-terminal domain and approximately 20 milliseconds for the N-terminal domain.

Conclusions:

  • The N- and C-terminal domains of calmodulin exhibit distinct Ca2+ binding kinetics, differing by over an order of magnitude.
  • These findings suggest distinct functional roles and regulatory mechanisms for each domain.
  • The study highlights the importance of a stable, half-saturated calmodulin intermediate in biological processes.