Related Experiment Video
Updated: Mar 18, 2026

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
Published on: January 24, 2016
Chapter Seven - When Phosphorylation Encounters Ubiquitination: A Balanced Perspective on IGF-1R Signaling
L Girnita1, S-I Takahashi2, C Crudden1
1Department of Oncology and Pathology, Cancer Center Karolinska, Karolinska Institutet and Karolinska University Hospital, Stockholm, Sweden.
Abstract:
Cell-surface receptors govern the critical information passage from outside to inside the cell and hence control important cellular decisions such as survival, growth, and differentiation. These receptors, structurally grouped into different families, utilize common intracellular signaling-proteins and pathways, yet promote divergent biological consequences. In rapid processing of extracellular signals to biological outcomes, posttranslational modifications offer a repertoire of protein processing options. Protein ubiquitination was originally identified as a signal for protein degradation through the proteasome system. It is now becoming increasingly recognized that both ubiquitin and ubiquitin-like proteins, all evolved from a common ubiquitin structural superfold, are used extensively by the cell and encompass signal tags for many different cellular fates. In this chapter we examine the current understanding of the ubiquitin regulation surrounding the insulin-like growth factor and insulin signaling systems, major members of the larger family of receptor tyrosine kinases (RTKs) and key regulators of fundamental physiological and pathological states.
Insights
Ubiquitin modification regulates cell signaling pathways, impacting cellular decisions like growth and survival. This research reviews ubiquitin
Area of Science:
- Cellular biology
- Molecular signaling
Background:
- Cell-surface receptors control crucial cell functions like survival and growth.
- Receptor tyrosine kinases (RTKs), including insulin-like growth factor and insulin signaling, are key regulators of physiological and pathological states.
- Posttranslational modifications, particularly ubiquitination, play a vital role in processing extracellular signals.
Purpose of the Study:
- To examine the role of ubiquitin regulation in insulin-like growth factor and insulin signaling pathways.
- To explore how ubiquitination influences receptor tyrosine kinase (RTK) signaling.
- To understand the divergent biological outcomes mediated by common signaling pathways.
Main Methods:
- Review of current literature on protein ubiquitination.
- Analysis of ubiquitin-like proteins and their signaling roles.
- Examination of ubiquitin regulation within insulin and insulin-like growth factor signaling systems.
Main Results:
- Ubiquitination is increasingly recognized as a signal for diverse cellular fates beyond protein degradation.
- Ubiquitin and ubiquitin-like proteins act as critical signal tags.
- Understanding ubiquitin's role is crucial for comprehending RTK signaling.
Conclusions:
- Ubiquitin regulation is a key determinant of cellular responses mediated by RTKs.
- The study highlights the complex role of ubiquitination in fundamental physiological processes.
- Further research into ubiquitin's role in insulin signaling is warranted.
Related Concept Videos
TGF - β Signaling Pathway
Amplifying Signals via Enzymatic Cascade
PI3K/mTOR/AKT Signaling Pathway
Receptor Downregulation in MVBs
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR...
Intracellular Signaling Affects Focal Adhesions
Some...
Regulation of the Unfolded Protein Response

