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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...
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,...

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Mapping Dysfunctional Protein-Protein Interactions in Disease
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Targeting Protein-Protein Interactions (PPIs) to Drive Functional Annotation: An Integrative Methodology to Study

Roberto Rosales-Rojas1,2, Christian Fernández1,3, Mariela González-Avendaño2

  • 1Millennium Institute on Immunology and Immunotherapy, Instituto de Ciencias Biomédicas (ICBM), Facultad de Medicina, Universidad de Chile, Independencia 1027, Santiago 8380453, Chile.

Biomolecules
|May 27, 2026
PubMed
Summary
This summary is machine-generated.

We developed a new proteomics method to find protein-protein interactions (PPIs) linked to cellular senescence. This approach identified a novel interaction between TMPRSS11a and HSPA8, suggesting a role in senescence.

Keywords:
nucleotide-binding domainprotein–protein interactionsselective proteomicssenescence

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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Published on: March 3, 2015

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Proteomics

Background:

  • Protein-protein interactions (PPIs) are crucial for cellular functions.
  • Identifying senescence-associated PPIs is challenging.
  • TMPRSS11a is a transmembrane serine protease involved in cellular processes.

Purpose of the Study:

  • To develop and validate an integrative methodology for identifying senescence-associated PPIs.
  • To investigate the interaction between TMPRSS11a and HSPA8 in cellular senescence.
  • To establish a workflow for senescence-associated PPI discovery.

Main Methods:

  • Selective proteomics combined with mass spectrometry.
  • Structural bioinformatics for interaction interface analysis.
  • In vitro proximity ligation assay for complex validation.

Main Results:

  • Identified co-immunoprecipitated proteins with TMPRSS11a.
  • Provided evidence for an interaction between TMPRSS11a and HSPA8.
  • Suggested the TMPRSS11a-HSPA8 interaction is associated with enhanced senescence.

Conclusions:

  • The study presents a novel workflow for investigating senescence-associated PPIs.
  • The findings support a role for the TMPRSS11a-HSPA8 interaction in cellular senescence.
  • The methodology can be applied to discover other senescence-related PPIs.