Related Experiment Video

Updated: Feb 22, 2026

Visualization of G3BP Stress Granules Dynamics in Live Primary Cells
10:12

Visualization of G3BP Stress Granules Dynamics in Live Primary Cells

Published on: May 21, 2014

18.8K

Proteomics Identifies Golgi phosphoprotein 3 (GOLPH3) with A Link Between Golgi Structure, Cancer, DNA Damage and

John J M Bergeron1, Catherine E Au2, David Y Thomas3

  • 1From the ‡Department of Medicine, McGill University Hospital Research Institute, Montreal, Quebec, Canada H4A 3J1; john.bergeron@mcgill.ca.

Molecular & Cellular Proteomics : MCP
|September 29, 2017
PubMed

Insights

Golgi phosphoprotein 3 (GOLPH3) is an oncogene protein found in the Golgi apparatus. It associates with phosphatidyl inositol 4 phosphate (PI4P) to maintain Golgi structure and protein transport.

Area of Science:

  • Cell Biology
  • Molecular Oncology
  • Biochemistry

Background:

  • Golgi phosphoprotein 3 (GOLPH3) is identified as a Golgi-resident protein and an oncogene.
  • GOLPH3 has been discovered through multiple independent screening methods.
  • Its role in cancer development and Golgi structure is under investigation.

Purpose of the Study:

  • To elucidate the function of GOLPH3 in maintaining Golgi apparatus structure.
  • To understand the association between GOLPH3 and phosphatidyl inositol 4 phosphate (PI4P).
  • To explore the implications of GOLPH3's function in cancer.

Main Methods:

  • Proteomic-based screening to identify Golgi resident proteins.
  • Cancer gene amplification screening to identify oncogenes.
  • Biochemical assays to investigate protein-lipid interactions.

Main Results:

  • GOLPH3 was identified as a Golgi-resident oncogene protein.
  • GOLPH3 was found to associate with phosphatidyl inositol 4 phosphate (PI4P).
  • This association is crucial for maintaining the Golgi ribbon structure and vesicular transport.

Conclusions:

  • GOLPH3 plays a critical role in Golgi apparatus organization and function.
  • The interaction of GOLPH3 with PI4P is essential for maintaining Golgi structure.
  • GOLPH3's oncogenic nature and role in Golgi function highlight its significance in cancer biology.

More Related Videos

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments10:59

Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments

Published on: February 7, 2025

1.8K
Detection and Visualization of DNA Damage-induced Protein Complexes in Suspension Cell Cultures Using the Proximity Ligation Assay13:10

Detection and Visualization of DNA Damage-induced Protein Complexes in Suspension Cell Cultures Using the Proximity Ligation Assay

Published on: June 9, 2017

10.7K

Related Concept Videos

Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.5K
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
5.0K
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
9.9K
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
5.5K
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.6K