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Updated: May 2, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Three basic residues of intracellular loop 3 of the beta-1 adrenergic receptor are required for golgin-160-dependent

Catherine E Gilbert1, David M Zuckerman2, Pamela L Currier3

  • 1Department of Cell Biology, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205, USA. cgilbe15@jhmi.edu.

International Journal of Molecular Sciences
|February 26, 2014
PubMed

Golgin-160 is a member of the golgin family of proteins, which have been implicated in the maintenance of Golgi structure and in vesicle tethering. Golgin-160 is atypical; it promotes post-Golgi trafficking of specific cargo proteins, including the β-1 adrenergic receptor (β1AR), a G protein-coupled receptor. Here we show that golgin-160 binds directly to the third intracellular loop of β1AR and that this binding depends on three basic residues in this loop. Mutation of the basic residues does not affect trafficking of β1AR from the endoplasmic reticulum through the Golgi complex, but results in reduced steady-state levels at the plasma membrane. We hypothesize that golgin-160 promotes incorporation of β1AR into specific transport carriers at the trans-Golgi network to ensure efficient delivery to the cell surface. These results add to our understanding of the biogenesis of β1AR, and suggest a novel point of regulation for its delivery to the plasma membrane.

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