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Related Concept Videos

Circadian Rhythms and Gene Regulation02:19

Circadian Rhythms and Gene Regulation

The biological clock is involved in many aspects of regulating complex physiology in all animals. It was in 1935 when German zoologists, Hans Kalmus and Erwin Bünning, discovered the existence of circadian rhythm in Drosophila melanogaster. However, the internal molecular mechanisms behind the circadian clock remained a mystery until 1984, when Jeffrey C. Hall, Michael Rosbash, and Michael W. Young discovered the expression of the Per gene oscillating over a 24-hour cycle. In subsequent years,...
Circadian Rhythms and Gene Regulation02:19

Circadian Rhythms and Gene Regulation

The biological clock is involved in many aspects of regulating complex physiology in all animals. It was in 1935 when German zoologists, Hans Kalmus and Erwin Bünning, discovered the existence of circadian rhythm in Drosophila melanogaster. However, the internal molecular mechanisms behind the circadian clock remained a mystery until 1984, when Jeffrey C. Hall, Michael Rosbash, and Michael W. Young discovered the expression of the Per gene oscillating over a 24-hour cycle. In subsequent years,...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
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Biological Clocks and Seasonal Responses02:45

Biological Clocks and Seasonal Responses

The circadian—or biological—clock is an intrinsic, timekeeping, molecular mechanism that allows plants to coordinate physiological activities over 24-hour cycles called circadian rhythms. Photoperiodism is a collective term for the biological responses of plants to variations in the relative lengths of dark and light periods. The period of light-exposure is called the photoperiod.

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Rapid Analysis of Circadian Phenotypes in Arabidopsis Protoplasts Transfected with a Luminescent Clock Reporter
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Reversible protein phosphorylation regulates circadian rhythms.

D M Virshup1, E J Eide, D B Forger

  • 1Department of Pediatrics, University of Utah, Salt Lake City, Utah 84112, USA.

Cold Spring Harbor Symposia on Quantitative Biology
|April 19, 2008
PubMed
Summary
This summary is machine-generated.

Protein phosphorylation by casein kinase Iepsilon regulates mammalian circadian clocks by controlling PER protein stability. This research refines quantitative models for clock manipulation, potentially aiding health by mitigating jet lag and shift work effects.

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Area of Science:

  • Biochemistry
  • Chronobiology
  • Molecular Biology

Background:

  • Circadian rhythms, approximately 24-hour cycles, govern essential biological processes like sleep, metabolism, and cell division in mammals.
  • Molecular clocks, driven by transcriptional-translational feedback loops, precisely regulate daily physiological fluctuations.
  • Disruptions to circadian clock components can lead to significant health issues.

Purpose of the Study:

  • To investigate the role of protein phosphorylation in regulating the mammalian circadian clock's period.
  • To explore how casein kinase Iepsilon (CKIε) phosphorylation of PER1 and PER2 proteins impacts clock function.
  • To refine quantitative models of the circadian clock for predicting and potentially manipulating its behavior.

Main Methods:

  • Detailed analysis of protein phosphorylation events within the circadian clock mechanism.
  • Utilizing quantitative modeling to predict the effects of altered phosphorylation on clock timing.
  • Integrating biological data to refine and validate computational models.

Main Results:

  • Casein kinase Iepsilon (CKIε) plays a critical role by phosphorylating PER1 and PER2 proteins, influencing their stability and cellular localization.
  • Phosphorylation dynamics directly impact the precision and period of the mammalian circadian clock.
  • Quantitative models accurately predict how changes in phosphorylation affect clock behavior.

Conclusions:

  • Reversible protein phosphorylation is a key regulatory mechanism for mammalian circadian rhythms.
  • Accurate quantitative models of the circadian clock can be developed and refined using experimental data.
  • Understanding and modeling these processes may lead to therapeutic interventions for circadian rhythm disorders and related health problems.