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Related Experiment Video

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Dissecting OGT's TPR domain to identify determinants of cellular function.

Sarah C Potter1,2, Bettine E Gibbs1, Forrest A Hammel1

  • 1Department of Microbiology, Blavatnik Institute of Harvard Medical School, Boston, MA 02115.

Proceedings of the National Academy of Sciences of the United States of America
|May 20, 2024
PubMed
Summary

Altering the tetratricopeptide repeat (TPR) domain of O-GlcNAc transferase (OGT) affects cell growth. Disrupting OGT dimerization speeds growth, while truncating the TPR domain slows it, revealing TPR

Keywords:
O-GlcNAc transferaseOGTTPRcell proliferationtetratricopeptide repeat

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • O-GlcNAc transferase (OGT) is a crucial mammalian enzyme involved in protein glycosylation and cell cycle regulation.
  • OGT's tetratricopeptide repeat (TPR) domain is vital for substrate recognition, but its specific role in cellular functions remains unclear.

Purpose of the Study:

  • To investigate how modifications to OGT's TPR domain impact cell growth and homeostasis.
  • To identify the essential components of the TPR domain for OGT's function and viability.

Main Methods:

  • Endogenous OGT deletion followed by expression of altered OGT variants.
  • Analysis of cell growth rates, subcellular localization, glycosylation activity, and protein-protein interactions.

Main Results:

  • Disrupting TPR residues for OGT dimerization accelerated cell growth.
  • Truncating the TPR domain slowed cell growth, with eight TPRs being essential for viability.
  • A viable OGT truncation variant (OGT-8) showed mislocalization, reduced glycosylation activity, and attenuated protein interactions.

Conclusions:

  • OGT's N-terminal TPRs are not essential for cell viability but are crucial for proper localization and mediating protein interactions.
  • The identified viable OGT truncation variant offers a tool to study OGT's essential functions.