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Related Experiment Videos

An inositolphosphate-binding immunophilin, IPBP12.

E B Cunningham1

  • 1Department of Biochemistry and Molecular Biology, UMDNJ-New Jersey Medical School, Newark, NJ 07103-2714, USA. cunnineb@umdnj.edu

Blood
|October 9, 1999
PubMed
Summary
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A novel 12-kD inositol phosphate-binding protein (IPBP12) was identified as an FK506-binding protein (FKBP) in human cell membranes. This protein binds inositol phosphates and associates with protein kinases and phosphatases, suggesting a role in multiprotein complex assembly.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Immunophilins are proteins that bind to immunosuppressants and possess peptidylprolyl cis-trans isomerase activity.
  • FK506-binding proteins (FKBPs) are a class of immunophilins, with FKBP12 being a well-characterized cytosolic member.
  • Inositol phosphates (IPs) are crucial signaling molecules involved in various cellular processes.

Purpose of the Study:

  • To identify and characterize novel inositol phosphate-binding proteins.
  • To investigate the enzymatic activity and ligand-binding properties of a newly discovered membrane-associated protein.
  • To elucidate the potential cellular functions and interactions of this protein.

Main Methods:

  • Isolation and purification of proteins from human erythrocyte and K562 cell membranes.

Related Experiment Videos

  • Assay of peptidylprolyl cis-trans isomerase activity and inhibition studies using FK506, rapamycin, and various inositol phosphates.
  • Protein sequencing of tryptic peptides and immunoprecipitation assays to identify interacting proteins.

    • Main Results:

    • A novel 12-kD inositol phosphate-binding protein (IPBP12) was identified, exhibiting FKBP-like activity.
    • IPBP12's isomerase activity was inhibited by FK506 and rapamycin, but uniquely by inositol 1,4,5-trisphosphate (IP(3)) and inositol 1,3,4,5-tetrakisphosphate (IP(4)).
    • IPBP12 was found to associate with a protein kinase and phosphoprotein phosphatase 2A (PP-2A), and sequencing suggested cytoskeletal localization.

    Conclusions:

    • A novel membrane-associated immunophilin, IPBP12, binds both inositol phosphates and FK506-like compounds.
    • IPBP12's interaction with IPs and its association with kinase/phosphatase complexes suggest a role in regulating cellular signaling pathways.
    • Immunophilins may function in assembling multiprotein complexes involved in signal transduction and cellular regulation.