Interaction of the human prostacyclin receptor and the NHERF4 family member intestinal and kidney enriched PDZ protein (IKEPP)

Biochim Biophys Acta. 2012 Oct;1823(10):1998-2012. doi: 10.1016/j.bbamcr.2012.07.015. Epub 2012 Aug 4.

Abstract

Prostacyclin and its I prostanoid receptor, the IP, play central roles in hemostasis and in re-endothelialization in response to vascular injury. Herein, intestinal and kidney enriched PDZ protein (IKEPP) was identified as an interactant of the human (h) IP mediated through binding of PDZ domain 1 (PDZ(D1)) and, to a lesser extent, PDZ(D2) of IKEPP to a carboxyl-terminal Class I 'PDZ ligand' within the hIP. While the interaction is constitutive, agonist-activation of the hIP leads to cAMP-dependent protein kinase (PK) A and PKC-phosphorylation of IKEPP, coinciding with its increased interaction with the hIP. Ectopic expression of IKEPP increases functional expression of the hIP, enhancing its ligand binding and agonist-induced cAMP generation. Originally thought to be restricted to renal and gastrointestinal tissues, herein, IKEPP was also found to be expressed in vascular endothelial cells where it co-localizes and complexes with the hIP. Furthermore, siRNA-disruption of IKEPP expression impaired hIP-induced endothelial cell migration and in vitro angiogenesis, revealing the functional importance of the IKEPP:IP interaction within the vascular endothelium. Identification of IKEPP as a functional interactant of the IP reveals novel mechanistic insights into the role of these proteins within the vasculature and, potentially, in other systems where they are co-expressed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry
  • Adaptor Proteins, Signal Transducing / metabolism*
  • Cell Adhesion Molecules
  • Cell Movement
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • HEK293 Cells
  • Human Umbilical Vein Endothelial Cells / cytology
  • Human Umbilical Vein Endothelial Cells / metabolism
  • Humans
  • Kidney / cytology
  • Ligands
  • Models, Biological
  • Neoplasm Proteins / chemistry
  • Neoplasm Proteins / metabolism*
  • Neovascularization, Physiologic
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism*
  • Protein Binding
  • Protein Kinase C / metabolism
  • Protein Structure, Tertiary
  • Receptors, Epoprostenol
  • Receptors, Prostaglandin / agonists
  • Receptors, Prostaglandin / chemistry
  • Receptors, Prostaglandin / metabolism*
  • Signal Transduction
  • Sodium-Hydrogen Exchangers / chemistry
  • Sodium-Hydrogen Exchangers / metabolism*

Substances

  • Adaptor Proteins, Signal Transducing
  • Cell Adhesion Molecules
  • Ligands
  • Neoplasm Proteins
  • PDZD2 protein, human
  • PTGIR protein, human
  • Phosphoproteins
  • Receptors, Epoprostenol
  • Receptors, Prostaglandin
  • Sodium-Hydrogen Exchangers
  • sodium-hydrogen exchanger regulatory factor
  • Cyclic AMP-Dependent Protein Kinases
  • Protein Kinase C