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Related Experiment Video

Updated: Apr 24, 2026

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay

Published on: September 10, 2020

Dynamic analysis of GH receptor conformational changes by split luciferase complementation.

Ying Liu¹, Philip A Berry, Yue Zhang

¹Department of Medicine (Y.L., P.A.B., Y.Z., J.J., S.J.F.), Division of Endocrinology, Diabetes, and Metabolism, and Departments of Radiology (K.R.Z.), and Cell, Developmental, and Integrative Biology (S.J.F.), University of Alabama at Birmingham, Birmingham, Alabama 35294; Cancer Science Institute of Singapore and Department of Pharmacology (P.E.L.), National University of Singapore, Singapore 119077; Department of Radiology (R.P.), Stanford University School of Medicine, Palo Alto, California 94304; Department of Biological Sciences (J.F.L., W.Y.C.), Clemson University, Clemson, South Carolina 29634; and Endocrinology Section (S.J.F.), Medical Service, Veterans Affairs Medical Center, Birmingham, Alabama 35233.

Molecular Endocrinology (Baltimore, Md.)

|September 5, 2014

Summary

This summary is machine-generated.

Growth hormone receptor (GHR) homodimerization dynamics were studied using a split luciferase assay. GH acutely enhances GHR proximity independently of JAK2, but JAK2 is required for subsequent signal reduction.

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Last Updated: Apr 24, 2026

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Published on: September 10, 2020

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High-throughput Functional Screening using a Homemade Dual-glow Luciferase Assay

High-throughput Functional Screening using a Homemade Dual-glow Luciferase Assay

Published on: June 1, 2014

Area of Science:

Cell biology
Molecular endocrinology
Signal transduction

Background:

The growth hormone receptor (GHR) mediates growth hormone (GH) signaling, existing as a cell surface homodimer.
GH binding to GHR is thought to induce conformational changes activating Janus kinase 2 (JAK2) and downstream pathways.
Previous studies lacked dynamic assessment of GH-induced GHR conformational changes.

Purpose of the Study:

To investigate the dynamic changes in GHR homodimer proximity upon GH binding.
To elucidate the roles of JAK2, GHR intracellular domain (ICD), and phosphorylation in GH-induced GHR conformational changes.

Main Methods:

Utilized a split luciferase complementation assay in living cells to detect GHR-GHR interactions.
Analyzed temporal patterns of GH-induced complementation changes.
Employed pharmacological manipulation, genetic alteration of JAK2 levels, and truncation of the GHR ICD tail.

Main Results:

GH treatment acutely increased GHR homodimer proximity, detected by enhanced luciferase complementation.
This initial proximity increase was independent of JAK2, GHR phosphorylation, or an intact ICD.
Subsequent reduction in GHR proximity required JAK2 kinase activity and the GHR ICD tail.

Conclusions:

GH acutely enhances GHR homodimer proximity independent of JAK2 and the ICD.
JAK2 kinase activity and the ICD are essential for the subsequent reduction of GHR proximity, challenging existing models.
This study reveals novel dynamics in GHR activation and signaling initiation.