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Related Experiment Video

Updated: Feb 2, 2026

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay
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HiPLA: High-throughput imaging proximity ligation assay.

Leonid A Serebryannyy1, Tom Misteli1

  • 1Cell Biology of Genomes Group, National Cancer Institute, NIH, Building 41, 41 Library Drive, Bethesda, MD 20892, USA.

Methods (San Diego, Calif.)
|November 13, 2018
PubMed
Summary

A new method, high-throughput imaging proximity ligation assay (HiPLA), systematically visualizes protein interactions. HiPLA identified proteins with altered nuclear lamina interactions in Hutchinson-Gilford progeria syndrome, offering insights into cellular processes.

Keywords:
High-throughput imagingHutchinson-Gilford progeria syndromeLamin proteomicsProximity ligation

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Protein-protein interactions are crucial for cellular functions and understanding them is key to deciphering health and disease.
  • Existing methods for studying protein interactions lack the sensitivity and scalability required for comprehensive analysis.

Purpose of the Study:

  • To develop a novel, high-throughput method for systematically visualizing protein interactomes.
  • To investigate protein interactions with the nuclear lamina in Hutchinson-Gilford progeria syndrome (HGPS).

Main Methods:

  • Development of high-throughput imaging proximity ligation assay (HiPLA), a scalable, antibody-based imaging technique.
  • Application of HiPLA to screen interactions of 60 nuclear proteins and their post-translational modifications (PTMs) with the nuclear lamina in an HGPS model.
  • Combined HiPLA with quantitative indirect immunofluorescence to assess protein expression changes.

Main Results:

  • HiPLA successfully visualized protein interactomes at a large scale.
  • Identified a subset of proteins exhibiting differential interactions with the nuclear lamina in HGPS.
  • Found that most differential interactions correlated with changes in protein expression.

Conclusions:

  • HiPLA provides a powerful new approach for large-scale, systematic probing of cellular protein-protein interactions.
  • The study reveals mechanistic insights into protein complex assembly and provides a deeper understanding of HGPS.
  • HiPLA facilitates the study of protein interactomes in various cellular processes and disease states.