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Updated: Aug 17, 2026

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
08:07

Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry

Published on: July 26, 2019

Inositol 1,4,5-trisphosphate receptor phosphorylation in breast cancer

Damien Soghoian1, Vinodh Jayaraman, Michael Silane

  • 1Vascular Biology Laboratory, Department of Neurosurgery, St. Luke's Roosevelt Hospital Center, New York, N.Y. 10025, USA.

Tumour Biology : the Journal of the International Society for Oncodevelopmental Biology and Medicine
|July 12, 2005
PubMed

Insights

Inositol 1,4,5-trisphosphate receptors (IP3Rs), specifically IP3R3, interact with cyclins (Cy) in breast cancer cells. This interaction influences intracellular calcium release and signaling during cell cycle progression.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Inositol 1,4,5-trisphosphate receptors (IP3Rs) are critical for regulating intracellular calcium (Ca2+) release.
  • Cyclins (Cy) are key regulators of cyclin-dependent kinases (cdk) and cell cycle progression.
  • The interplay between IP3Rs, Ca2+ signaling, and cell cycle regulators in breast cancer remains incompletely understood.

Purpose of the Study:

  • To identify the types of IP3Rs present in T47D breast cancer cells.
  • To investigate the interaction between IP3Rs and cyclins (Cy) during cell cycle progression.
  • To elucidate the role of this interaction in regulating intracellular Ca2+ and breast cancer signaling.

Main Methods:

  • Immunoblotting to detect IP3R expression.
  • Immunoprecipitation and pull-down assays to assess protein interactions.
  • Analysis of IP3R expression levels and their interaction with cyclins A and B.

Main Results:

  • T47D breast cancer cells express IP3Rs, with a higher relative expression of IP3R3 compared to IP3R1.
  • IP3R3 was found to interact with both cyclin A (CyA) and cyclin B (CyB).
  • The interaction between IP3Rs and cyclins suggests a novel regulatory pathway.

Conclusions:

  • IP3R3 is a key player in T47D breast cancer cells, interacting with cyclins A and B.
  • This interaction, along with potential phosphorylation by Cy/cdk complexes, offers a new mechanism for controlling intracellular Ca2+ release.
  • The findings highlight a novel pathway for regulating Ca2+-dependent signaling in breast cancer progression.

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