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Related Concept Videos

Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...

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Related Experiment Video

Updated: Jun 19, 2026

In Vitro Cleavage Assays using Purified Recombinant Drosophila Caspases for Substrate Screening
08:16

In Vitro Cleavage Assays using Purified Recombinant Drosophila Caspases for Substrate Screening

Published on: October 6, 2022

Caspase substrates: easily caught in deep waters?

Dieter Demon1, Petra Van Damme, Tom Vanden Berghe

  • 1Department for Molecular Biomedical Research, VIB, B-9052 Ghent, Belgium.

Trends in Biotechnology
|November 3, 2009
PubMed
Summary

Caspases are crucial enzymes in cell processes and diseases. This review examines methods for identifying caspase substrates, aiding understanding of their roles and inhibitor design.

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Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
05:56

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Caspases are essential proteases involved in cellular processes like apoptosis, proliferation, and differentiation.
  • They play significant roles in pathological conditions such as cancer and inflammation.
  • Caspase activity is characterized by preferential cleavage at aspartic acid residues, but typically at limited sites per substrate.

Purpose of the Study:

  • To critically review recent methodologies for identifying a comprehensive set of caspase substrates.
  • To highlight the importance of understanding caspase cleavage specificity for functional insights.
  • To explore how knowledge of substrates can aid in developing targeted caspase inhibitors for diseases.

Main Methods:

  • Review of recently published proteomic procedures.
  • Analysis of techniques used to generate proteome-wide views of caspase substrates.
  • Critical evaluation of methodologies for substrate identification.

Main Results:

  • Identification of various proteomic approaches for mapping caspase substrates.
  • Emphasis on the sequence context surrounding cleavage sites as key to substrate recognition.
  • Discussion of the functional significance of identified caspase substrates and fragments.

Conclusions:

  • Understanding caspase substrate specificity is vital for elucidating their roles in health and disease.
  • Proteomic strategies are advancing the identification of a broad range of caspase substrates.
  • This knowledge is instrumental for developing targeted therapeutic interventions for caspase-mediated pathologies.