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Related Experiment Videos

A cytoplasmic structure resembling large protein aggregates induced by interferons

A Meyerdierks1, B Denecke, M Rohde

  • 1Institut für Medizinische Mikrobiologie Medizinische Hochschule Hannover, Hannover, Germany.

The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society
|January 16, 1999
PubMed
Summary

Interferon-stimulated gene 15 (ISG15)-associated protein 35 (IFP 35) forms unique cytoplasmic aggregates in response to interferon treatment. These structures are distinct from known organelles, indicating a novel cellular organization.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Immunology

Background:

  • Interferon (IFN)-regulated proteins play crucial roles in cellular responses to viral infections and immune modulation.
  • IFP 35 is an IFN-stimulated leucine zipper protein found in various cell types, including monocytes, epithelial cells, and fibroblasts.
  • Understanding the subcellular localization and interactions of IFP 35 is key to elucidating its function.

Purpose of the Study:

  • To investigate the subcellular localization and structural associations of IFP 35 in interferon-treated cells.
  • To determine if IFP 35 interacts with known cellular organelles or structures.
  • To characterize the nature of the cytoplasmic structures formed by IFP 35.

Main Methods:

  • Immunofluorescence microscopy and confocal laser scanning microscopy were used to visualize IFP 35 localization.

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  • Co-localization experiments were performed with markers for various organelles and cellular components.
  • Subcellular fractionation and gel filtration were employed to assess protein complex formation and molecular mass.
  • Electron microscopy provided ultrastructural details of IFP 35 aggregates.
  • Immunoprecipitation studies were conducted using transfected cells expressing tagged IFP 35.

    • Main Results:

    • IFP 35 localizes to punctate cytoplasmic structures following IFN treatment.
    • IFP 35 did not co-localize with mitochondria, peroxisomes, endoplasmic reticulum, lysosomes, endosomes, Golgi complex, ribosomes, or actin filaments.
    • Subcellular fractionation confirmed IFP 35's cytoplasmic localization.
    • Gel filtration indicated IFP 35 exists in large protein complexes (200-440 kD).
    • Electron microscopy revealed membrane-less cytoplasmic clusters of IFP 35 aggregates.
    • Endogenous and transfected IFP 35 were shown to form complexes and co-localize.

    Conclusions:

    • IFP 35 forms unique, non-membranous cytoplasmic structures in response to IFN.
    • These structures are distinct from conventional organelles and appear to be large protein aggregates.
    • IFP 35 self-associates and potentially interacts with other proteins within these novel cellular compartments.