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Related Concept Videos

Protein Networks02:26

Protein Networks

3.7K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

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The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...
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Cellular Injury V: Apoptosis and Autophagy01:22

Cellular Injury V: Apoptosis and Autophagy

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Cells respond to damage and stress through highly coordinated processes that decide whether they survive or undergo controlled self-destruction. Two major pathways involved in this regulation are apoptosis, a type of programmed cell death, and autophagy, a survival mechanism that helps cells adapt to adverse conditions.ApoptosisApoptosis removes aged or injured cells to maintain tissue balance. During this process, the cell shrinks, chromatin condenses and fragments, and membrane-bound...
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Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells
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Discovering protein-protein interactions within the programmed cell death network using a protein-fragment

Yuval Gilad1, Ruth Shiloh1, Yaara Ber1

  • 1Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.

Cell Reports
|July 29, 2014
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Summary

Researchers mapped interactions between apoptosis and autophagy proteins using Gaussia luciferase protein-fragment complementation assay (GLuc PCA). This identified novel interactions, including one inhibiting DAPK2 activity, advancing cell death network research.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Apoptosis and autophagy are distinct cell death processes with complex protein-protein interactions.
  • Crosstalk between these pathways is crucial for cellular regulation and disease.
  • Understanding these interactions is key to deciphering cell death mechanisms.

Purpose of the Study:

  • To globally profile protein-protein interactions between apoptotic and autophagic proteins.
  • To identify novel interactions and understand their functional significance.
  • To demonstrate the utility of the Gaussia luciferase protein-fragment complementation assay (GLuc PCA) for mapping cell death pathways.

Main Methods:

  • Construction of a protein library of 63 apoptotic and autophagic proteins.
  • Application of the Gaussia luciferase protein-fragment complementation assay (GLuc PCA) to analyze approximately 3,600 protein-pair combinations.
  • Biochemical and functional characterization of identified interactions, including mapping binding regions and assessing effects on protein activity.

Main Results:

  • Generated a comprehensive interaction landscape of apoptotic and autophagic protein modules.
  • Identified 46 previously unknown protein-protein interactions within the cell death network.
  • Discovered and characterized a novel interaction between DAPK2 and 14-3-3τ, demonstrating that this interaction inhibits DAPK2 dimerization and kinase activity.

Conclusions:

  • The GLuc PCA platform is a powerful tool for discovering biochemical pathways and interactions within the cell death network.
  • The identified interactions provide new insights into the crosstalk between apoptosis and autophagy.
  • The characterization of the DAPK2-14-3-3τ interaction highlights a novel regulatory mechanism in cell death pathways.