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Conserved Lysine Acetylation within the Microtubule-Binding Domain Regulates MAP2/Tau Family Members

Andrew W Hwang1, Hanna Trzeciakiewicz2, Dave Friedmann3

  • 1Department of Pathology and Laboratory Medicine, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America.

Plos One
|December 22, 2016
PubMed

Insights

Lysine acetylation regulates tau proteins in Alzheimer's disease. This study shows MAP2 and MAP4 proteins also undergo acetylation, revealing conserved mechanisms for microtubule regulation.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroscience

Background:

  • Lysine acetylation is a key post-translational modification regulating tau proteins in Alzheimer's disease (AD) and tauopathies.
  • Acetylation sites on tau cluster in the microtubule-binding region (MTBR), a conserved domain across tau, MAP2, and MAP4.

Purpose of the Study:

  • To investigate if MAP2 and MAP4 proteins are also regulated by reversible acetylation.
  • To identify conserved acetylation mechanisms within the microtubule-associated protein (MAP) family.

Main Methods:

  • Mass spectrometry to identify acetylation sites.
  • Biochemical assays to study acetylation dynamics.
  • Cell-based approaches to validate findings in a cellular context.

Main Results:

  • MAP2 and MAP4 proteins are reversibly acetylated, with conserved acetylation sites in their MTBR.
  • CBP-catalyzed acetylation of MAP2 and MAP4 lysines was demonstrated.
  • MAP2 acetylation showed cysteine-dependent auto-regulation and was reduced by tubulin binding.

Conclusions:

  • Acetylation is a conserved post-translational modification mechanism across the tau/MAP2/MAP4 protein family.
  • Tubulin binding influences MAP acetylation status, suggesting a regulatory role in microtubule dynamics.
  • These findings expand the understanding of dynamic mechanisms regulating microtubules.

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