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Structure, function, and pathology of protein O-glucosyltransferases
Muhammad Zubair Mehboob1, Minglin Lang2,3
1CAS Center for Excellence in Biotic Interactions, College of Life Science, University of Chinese Academy of Sciences, Beijing, 100049, China.
Cell Death & Disease
|January 13, 2021
Summary
Protein O-glucosylation, essential for protein stability and cell surface transport, is performed by POGLUTs. Aberrant O-glucosylation links to diseases, but mechanisms remain unclear, necessitating further research.
Area of Science:
- Biochemistry
- Cell Biology
- Glycobiology
Background:
- Protein O-glucosylation adds glucose to serine in EGF-like repeats, crucial for protein stability and cell surface trafficking.
- Protein O-glucosyltransferases (POGLUTs) in the ER catalyze O-glucosylation using UDP-Glc, and can also O-xylosylate.
- Dysfunctional POGLUTs are linked to various human diseases, including muscular dystrophy and leukemia.
Purpose of the Study:
- To comprehensively review literature on O-glucosyltransferases, focusing on POGLUT1 structure and function.
- To elucidate the role of POGLUTs in both health and disease.
- To identify knowledge gaps and propose future research directions.
Main Methods:
- Systematic literature review of O-glucosyltransferases and their roles.
- Analysis of POGLUT structure, function, and substrate specificity.
- Examination of POGLUT involvement in disease pathogenesis.
Main Results:
- POGLUTs modify EGF repeats, influencing protein stability and trafficking.
- POGLUTs exhibit dual O-glucosylation and O-xylosylation activities.
- Impaired POGLUT expression is associated with diverse pathologies, affecting signaling pathways like Notch and TGF-β1.
Conclusions:
- Protein O-glucosylation is vital for cellular processes and disease prevention.
- The precise disease mechanisms driven by aberrant O-glucosylation require further investigation.
- Future research should explore POGLUTs in cancer, cell communication, and muscular diseases.
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