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Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....

Protein Glycosylation

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...

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Related Experiment Video

Updated: Jan 9, 2026

Flow Cytometry-based Drug Screening System for the Identification of Small Molecules That Promote Cellular Differentiation of Glioblastoma Stem Cells

Flow Cytometry-based Drug Screening System for the Identification of Small Molecules That Promote Cellular Differentiation of Glioblastoma Stem Cells

Published on: January 10, 2018

Protein Posttranslational Modifications in Glioma Stem Cells.

Eiichi Hinoi^1,2,3

¹Department of Bioactive Molecules, Pharmacology, Gifu Pharmaceutical University.

Biological & Pharmaceutical Bulletin

|November 30, 2025

Summary

This summary is machine-generated.

Two protein modifications in glioma stem cells (GSCs) impact glioblastoma (GBM) malignancy. Understanding SMURF2 and MEK5 pathways offers potential therapeutic targets for cancers driven by cancer stem cells.

Keywords:

glioblastoma glioma stem cell phosphorylation posttranslational modification ubiquitination

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Last Updated: Jan 9, 2026

Flow Cytometry-based Drug Screening System for the Identification of Small Molecules That Promote Cellular Differentiation of Glioblastoma Stem Cells

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Published on: January 10, 2018

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Optimization of High Grade Glioma Cell Culture from Surgical Specimens for Use in Clinically Relevant Animal Models and 3D Immunochemistry

Optimization of High Grade Glioma Cell Culture from Surgical Specimens for Use in Clinically Relevant Animal Models and 3D Immunochemistry

Published on: January 7, 2014

Area of Science:

Oncology
Molecular Biology
Biochemistry

Background:

Glioblastoma (GBM) is a highly malignant brain tumor.
Glioma stem cells (GSCs) drive GBM initiation, progression, and recurrence.
Cancer stem cell properties are linked to tumor malignancy.

Purpose of the Study:

To review the influence of two protein posttranslational modifications in GSCs.
To explore the roles of SMURF2 and MEK5 in GSC stemness and GBM malignancy.
To identify potential therapeutic targets in GSCs.

Main Methods:

Review of literature on protein posttranslational modifications in GSCs.
Analysis of ubiquitination of TGF-β receptor (TGFBR) by SMURF2.
Analysis of ERK5 phosphorylation by MEK5.

Main Results:

SMURF2Thr249 phosphorylation regulates GSC stemness and tumorigenicity via the TGFBR-SMAD-SOX axis.
SMURF2Thr249 phosphorylation is downregulated in GBM patients.
MEK5 controls GSC self-renewal and tumorigenicity by phosphorylating ERK5-STAT3 axis.

Conclusions:

Protein posttranslational modifications are key mechanisms maintaining GSC stemness and tumorigenicity.
SMURF2 and MEK5 pathways in GSCs are potential therapeutic targets.
Targeting GSC-specific modifications may offer novel cancer therapies.