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Mutual regulation between glycosylation and transforming growth factor-β isoforms signaling pathway
Zhuo Chen1, Hanjie Yu1, Xiangqin Chen1
1Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, PR China.
Abstract:
Transforming growth factor-beta (TGF-β) superfamily members orchestrate a wide breadth of biological processes. Through Sma and Mad (Smad)-related dependent or noncanonical pathways, TGF-β members involve in the occurrence and development of many diseases such as cancers, fibrosis, autoimmune diseases, cardiovascular diseases and brain diseases. Glycosylation is one kind of the most common posttranslational modifications on proteins or lipids. Abnormal protein glycosylation can lead to protein malfunction and biological process disorder, thereby causing serious diseases. Previously, researchers commonly make comprehensive systematic overviews on the roles of TGF-β signaling in a specific disease or biological process. In recent years, more and more evidences associate glycosylation modification with TGF-β signaling pathway, and we can no longer disengage and ignore the roles of glycosylation from TGF-β signaling to make investigation. In this review, we provide an overview of current findings involved in glycosylation within TGF-βs and theirs receptors, and the interaction effects between glycosylation and TGF-β subfamily signaling, concluding that there is an intricate mutual regulation between glycosylation and TGF-β signaling, hoping to present the glycosylation regulatory patterns that concealed in TGF-βs signaling pathways.
Insights
Glycosylation, a common protein modification, intricately regulates transforming growth factor-beta (TGF-β) signaling pathways. This review explores the interplay between glycosylation and TGF-β signaling, crucial for understanding various diseases.
Area of Science:
- Molecular Biology
- Biochemistry
- Cell Signaling
Background:
- Transforming growth factor-beta (TGF-β) superfamily members are critical regulators of diverse biological processes.
- TGF-β signaling pathways are implicated in numerous diseases, including cancers, fibrosis, autoimmune, cardiovascular, and brain disorders.
- Glycosylation, a prevalent post-translational modification, significantly impacts protein function and cellular processes.
Purpose of the Study:
- To provide a comprehensive overview of current findings on glycosylation within TGF-βs and their receptors.
- To elucidate the interaction effects between glycosylation and TGF-β subfamily signaling.
- To highlight the intricate mutual regulation between glycosylation and TGF-β signaling pathways.
Main Methods:
- Systematic review of existing literature.
- Analysis of research associating glycosylation modifications with TGF-β signaling.
- Integration of findings on glycosylation of TGF-β receptors and ligands.
Main Results:
- Evidence increasingly links glycosylation modifications to TGF-β signaling pathway activity.
- Glycosylation affects TGF-β receptors and ligands, influencing pathway activation.
- An intricate, mutual regulatory relationship exists between glycosylation and TGF-β signaling.
Conclusions:
- Glycosylation is a critical regulatory layer in TGF-β signaling.
- Understanding glycosylation's role is essential for investigating TGF-β-related diseases.
- This review presents glycosylation regulatory patterns within TGF-β signaling pathways.
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