# G Protein Regulation of Golgi Structure and Function

> **NIH NIH R01** · THOMAS JEFFERSON UNIVERSITY · 2021 · $312,000

## Abstract

Abstract
Heterotrimeric G proteins (αβγ) are well known for their function in linking G protein-coupled receptors
(GPCRs) to a variety of intracellular responses, and thereby playing essential roles in transmitting a wide
variety of extracellular signals into regulation of countless physiological processes. In the textbook view, G
proteins carry out their function while associated with the cytoplasmic surface of a cell’s plasma membrane.
In contrast to the classical view of plasma membrane-limited G protein signaling, it is becoming increasingly
recognized that G protein localization is dynamic and regulated, such that they can reversibly traffic from the
plasma membrane to intracellular locations, and that G proteins can have important cellular functions at
intracellular sites. The research in this proposal focuses on understanding non-canonical functions of Gβγ
subunits, and specifically roles for Gβγ in regulating signaling at the Golgi. Our previous work revealed an
important role for Golgi-localized Gβγ in regulating a signaling pathway on the cytoplasmic surface of Golgi
membranes that controls the Golgi exit of select protein cargo destined for the plasma membrane. The
research in this current proposal will examine the hypothesis that Gβγ regulates signaling pathways that
control Golgi integrity by regulating the fragmentation of the Golgi under physiological and
pathophysiological conditions. Reversible Golgi fragmentation is a cellular phenomenon that occurs under
normal conditions, such as during mitosis, and that occurs in disease states, such as infection, cancer and
neurodegenerative disease. This application will focus on defining a novel role for Gβγ in regulating the
mitotic Golgi fragmentation checkpoint and by interrogating a novel role for Gβγ in regulating microtubule-
dependent Golgi fragmentation. In addition, this application will define upstream mechanisms that directly
promote signaling by Gβγ at the Golgi. These objectives will be pursued by a variety of experimental
approaches, including cultured cells, immunofluorescence microscopy, fluorescence microscopy of live
cells, biosensors, pharmacological inhibitors, mutational analysis, and biochemical assays.

## Key facts

- **NIH application ID:** 10117262
- **Project number:** 5R01GM132426-03
- **Recipient organization:** THOMAS JEFFERSON UNIVERSITY
- **Principal Investigator:** PHILIP B WEDEGAERTNER
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2021
- **Award amount:** $312,000
- **Award type:** 5
- **Project period:** 2019-05-07 → 2023-02-28

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10117262

## Citation

> US National Institutes of Health, RePORTER application 10117262, G Protein Regulation of Golgi Structure and Function (5R01GM132426-03). Retrieved via AI Analytics 2026-05-22 from https://api.ai-analytics.org/grant/nih/10117262. Licensed CC0.

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