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Related Concept Videos

Protein Networks02:26

Protein Networks

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,...
Protein Networks02:26

Protein Networks

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,...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

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In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
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In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

A protein domain-based interactome network for C. elegans early embryogenesis.

Mike Boxem1, Zoltan Maliga, Niels Klitgord

  • 1Center for Cancer Systems Biology and Department of Cancer Biology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA. mboxem@partners.org

Cell
|August 12, 2008
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Summary

Researchers mapped protein interactions by focusing on modular domains, creating a more complete interactome network for C. elegans development. This domain-based approach offers new insights into cellular organization and function.

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The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging
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Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans
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Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans

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Last Updated: Jul 2, 2026

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging
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Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans
07:22

Protein Extract Preparation and Co-immunoprecipitation from Caenorhabditis elegans

Published on: May 23, 2020

Area of Science:

  • Molecular Biology
  • Systems Biology
  • Developmental Biology

Background:

  • Protein-protein interactions are crucial for cellular functions.
  • Existing interactome networks often overlook the modular domain organization of proteins.
  • Understanding domain-mediated interactions is key to deciphering complex biological networks.

Purpose of the Study:

  • To develop an experimental strategy for identifying protein interaction domains.
  • To construct a domain-based interactome network for C. elegans early-embryonic proteins.
  • To reveal insights into C. elegans centrosome function through interactome modeling.

Main Methods:

  • Developed a novel experimental strategy to efficiently identify protein interaction domains.
  • Generated a domain-based interactome network using proteins from C. elegans early-embryonic cell divisions.
  • Identified minimal interacting regions for over 200 proteins.

Main Results:

  • Successfully identified interaction domains and mapped domain-based interactions for over 200 proteins.
  • The developed approach enhanced the sensitivity of the two-hybrid system, leading to a more comprehensive interactome.
  • The domain-based interactome network provided novel insights into C. elegans centrosome function.

Conclusions:

  • Protein modularity is critical for understanding protein-protein interactions and network organization.
  • The developed domain-based interactome modeling strategy is effective and applicable to various biological processes.
  • This approach advances the study of interactomes and provides a foundation for future research in C. elegans and other organisms.