Three basic residues of intracellular loop 3 of the beta-1 adrenergic receptor are required for golgin-160-dependent trafficking

Catherine E. Gilbert, David M. Zuckerman, Pamela L. Currier, Carolyn E Machamer

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2929-2945
Number of pages17
JournalInternational Journal of Molecular Sciences
Volume15
Issue number2
DOIs
StatePublished - Feb 20 2014

Fingerprint

Adrenergic beta-1 Receptors
adrenergics
Adrenergic Receptors
Cell membranes
Proteins
Carrier transport
proteins
Cell Membrane
delivery
trans-Golgi Network
tethering
biological evolution
membranes
endoplasmic reticulum
Golgi Apparatus
G-Protein-Coupled Receptors
cargo
Endoplasmic Reticulum
mutations
maintenance

Keywords

  • Golgi complex
  • Golgin-160
  • Trafficking
  • β-1 adrenergic receptor

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Spectroscopy
  • Inorganic Chemistry
  • Catalysis
  • Molecular Biology
  • Computer Science Applications
  • Medicine(all)

Cite this

Three basic residues of intracellular loop 3 of the beta-1 adrenergic receptor are required for golgin-160-dependent trafficking. / Gilbert, Catherine E.; Zuckerman, David M.; Currier, Pamela L.; Machamer, Carolyn E.

In: International Journal of Molecular Sciences, Vol. 15, No. 2, 20.02.2014, p. 2929-2945.

Research output: Contribution to journalArticle

@article{b169df2e4c284d61bbc9338ec026aef0,
title = "Three basic residues of intracellular loop 3 of the beta-1 adrenergic receptor are required for golgin-160-dependent trafficking",
abstract = "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.",
keywords = "Golgi complex, Golgin-160, Trafficking, β-1 adrenergic receptor",
author = "Gilbert, {Catherine E.} and Zuckerman, {David M.} and Currier, {Pamela L.} and Machamer, {Carolyn E}",
year = "2014",
month = "2",
day = "20",
doi = "10.3390/ijms15022929",
language = "English (US)",
volume = "15",
pages = "2929--2945",
journal = "International Journal of Molecular Sciences",
issn = "1661-6596",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "2",

}

TY - JOUR

T1 - Three basic residues of intracellular loop 3 of the beta-1 adrenergic receptor are required for golgin-160-dependent trafficking

AU - Gilbert, Catherine E.

AU - Zuckerman, David M.

AU - Currier, Pamela L.

AU - Machamer, Carolyn E

PY - 2014/2/20

Y1 - 2014/2/20

N2 - 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.

AB - 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.

KW - Golgi complex

KW - Golgin-160

KW - Trafficking

KW - β-1 adrenergic receptor

UR - http://www.scopus.com/inward/record.url?scp=84894258942&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84894258942&partnerID=8YFLogxK

U2 - 10.3390/ijms15022929

DO - 10.3390/ijms15022929

M3 - Article

C2 - 24566136

AN - SCOPUS:84894258942

VL - 15

SP - 2929

EP - 2945

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1661-6596

IS - 2

ER -