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Related Concept Videos

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...
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,...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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...

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Genetic Manipulation of Cerebellar Granule Neurons In Vitro and In Vivo to Study Neuronal Morphology and Migration
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Dcp1a phosphorylation along neuronal development and stress.

Jacob Blumenthal1, Leah Behar, Evan Elliott

  • 1Department of Neurobiology, Weizmann Institute of Science, 76100 Rehovot, Israel. Jacob.Blumenthal@weizmann.ac.il

FEBS Letters
|December 17, 2008
PubMed
Summary

Decapping protein 1a (Dcp1a) expression changes during brain development and stress. This study reveals Dcp1a undergoes hyperphosphorylation, suggesting a new regulatory mechanism for mRNA decay.

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Area of Science:

  • Molecular Biology
  • Neuroscience
  • Cell Biology

Background:

  • Decapping protein 1a (Dcp1a) is crucial for mRNA degradation, residing in processing bodies (P-bodies).
  • While Dcp1a's function and interactions are known, its expression patterns remain largely uncharacterized.
  • Understanding Dcp1a expression is key to elucidating its role in cellular regulation.

Purpose of the Study:

  • To investigate the expression pattern of Dcp1a during brain development and neuronal differentiation.
  • To examine Dcp1a expression under conditions of cellular stress.
  • To identify post-translational modifications of Dcp1a in response to physiological cues.

Main Methods:

  • Monitoring Dcp1a expression across different stages of brain development.
  • Analyzing Dcp1a expression during neuronal differentiation processes.
  • Assessing Dcp1a levels and modifications under induced cellular stress conditions.
  • Utilizing techniques to identify specific phosphorylated amino acid residues on Dcp1a.

Main Results:

  • Dcp1a expression was observed to change during brain development and neuronal differentiation.
  • Significant hyperphosphorylation of Dcp1a was detected under physiological conditions, including cellular stress.
  • Specific amino acid residues involved in Dcp1a phosphorylation were identified.

Conclusions:

  • Dcp1a undergoes dynamic changes in expression and post-translational modification during neural development and in response to stress.
  • Hyperphosphorylation of Dcp1a represents a novel regulatory mechanism potentially influencing its mRNA decapping function.
  • These findings offer new insights into the control of mRNA decay pathways in response to physiological stimuli.