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Vasohibins encode tubulin detyrosinating activity.

Joppe Nieuwenhuis1, Athanassios Adamopoulos1, Onno B Bleijerveld1

  • 1Division of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, Netherlands.

Science (New York, N.Y.)
|November 18, 2017
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Summary

Researchers identified vasohibins as the long-sought enzymes responsible for tubulin detyrosination, a key posttranslational modification impacting microtubule heterogeneity. This discovery sheds light on the tubulin tyrosination cycle.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Microtubules are dynamic polymers essential for cellular functions.
  • Tubulin undergoes posttranslational modifications, including detyrosination of alpha-tubulin, which generates microtubule heterogeneity.
  • The enzymes catalyzing tubulin detyrosination have remained unidentified for decades.

Purpose of the Study:

  • To identify the elusive enzymes responsible for tubulin detyrosination.
  • To elucidate the molecular mechanisms regulating the tubulin tyrosination cycle.

Main Methods:

  • Genetic screen in haploid human cells to identify regulators of tubulin detyrosination.
  • Biochemical assays using purified vasohibins.
  • Analysis of vasohibin (VASH1 and VASH2) and SVBP function.

Main Results:

  • SVBP peptide regulates the abundance of vasohibins (VASH1 and VASH2).
  • Vasohibins, but not SVBP alone, significantly increased alpha-tubulin detyrosination.
  • Purified vasohibins directly removed the C-terminal tyrosine of alpha-tubulin.
  • Vasohibins exhibit cell type-dependent roles in detyrosination, with additional detyrosinating activity present in cells.

Conclusions:

  • Vasohibins are the missing link in the tubulin tyrosination cycle, acting as the primary detyrosinating enzymes.
  • This finding redefines the known functions of vasohibins beyond angiogenesis regulation.
  • Understanding tubulin detyrosination is crucial for comprehending microtubule dynamics and cellular processes.