Frontiers commentary on tallet et Al. Investigation of prolactin receptor activation and blockade using time-resolved fluorescence resonance energy transfer.

Ralf Jockers

doi:10.3389/fendo.2014.00088

Abstract

Frontiers commentary on tallet et Al. Investigation of prolactin receptor activation and blockade using time-resolved fluorescence resonance energy transfer.

Highlights

Investigation of prolactin receptor activation and blockade using time-resolved fluorescence resonance energy transfer by Tallet E, Fernandez I, Zhang C, Salsac M, Gregor N, Ayoub MA, et al (2011)
One of these receptors is the prolactin receptor (PRLR), which belongs to the cytokine receptor family that is devoid of intrinsic kinase activity but constitutively interacts with the JAK2 tyrosine kinase
A similar conclusion was reached in another study based on co-IP experiments further arguing for the existence of ligand-independent homodimers of human PRLR isoforms, with the transmembrane domain being the main dimer interface (3)

Summary

Introduction

Investigation of prolactin receptor activation and blockade using time-resolved fluorescence resonance energy transfer by Tallet E, Fernandez I, Zhang C, Salsac M, Gregor N, Ayoub MA, et al (2011). In the first model, binding of signaling molecules promotes ligand-induced dimerization/oligomerization of receptors.

Results

Conclusion