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Related Experiment Videos

Polycystin-1 interacts with intermediate filaments.

G M Xu1, T Sikaneta, B M Sullivan

  • 1Renal Unit, Massachusetts General Hospital and Harvard Medical School, Charlestown, Massachusetts 02129, USA.

The Journal of Biological Chemistry
|October 3, 2001
PubMed
Summary
This summary is machine-generated.

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Polycystin-1, defective in polycystic kidney disease, interacts with intermediate filament proteins like vimentin. This association suggests novel structural or signaling roles for polycystin-1 within the cell.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Polycystin-1 is a transmembrane protein implicated in autosomal dominant polycystic kidney disease.
  • Its function and specific cellular interactions, particularly with the cytoskeleton, remain largely unknown.

Purpose of the Study:

  • To identify proteins interacting with the C-tail of polycystin-1 (P1CT).
  • To investigate the in vivo and in vitro interactions between polycystin-1 and intermediate filament proteins.

Main Methods:

  • Yeast two-hybrid screening using P1CT as bait.
  • GST pull-down assays and in vitro filament assembly assays.
  • In vivo studies using recombinant P1CT and analysis of endogenous polycystin-1 localization.

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Main Results:

  • Vimentin, cytokeratins K8/K18, and desmin were identified as binding partners of P1CT.
  • Interactions are mediated by coiled-coil motifs.
  • Recombinant P1CT associated with the intermediate filament network and cytoskeleton in cells; endogenous polycystin-1 localized with intermediate filaments at desmosomal junctions.

Conclusions:

  • Polycystin-1 directly interacts with intermediate filament proteins, including vimentin.
  • These interactions are confirmed in vitro and in vivo.
  • Polycystin-1 may leverage its association with the cytoskeleton for structural, storage, or signaling functions.