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Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
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Near-atomic model of microtubule-tau interactions

Elizabeth H Kellogg1,2, Nisreen M A Hejab2, Simon Poepsel1

  • 1QB3 Institute and Department of Molecular and Cell Biology, University of California-Berkeley, Berkeley, CA 94720, USA.

Science (New York, N.Y.)
|May 12, 2018
PubMed

Insights

Tau protein stabilizes microtubules by binding to tubulin repeats. This interaction, crucial for neuronal function, is disrupted by hyperphosphorylation, potentially leading to Alzheimer's disease.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Tau is an axonal protein essential for stabilizing microtubules (MTs).
  • Hyperphosphorylated tau detaches from MTs, aggregates, and is implicated in Alzheimer's disease.
  • The precise mechanisms of tau-MT interaction and stabilization remain unclear.

Purpose of the Study:

  • To elucidate the atomic details of tau-tubulin interactions.
  • To understand how tau stabilizes microtubules.
  • To investigate the impact of phosphorylation on tau's MT binding affinity.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) of tau constructs on microtubules.
  • Computational modeling to generate atomic models of tau-tubulin interactions.

Main Results:

  • Tau's conserved tubulin-binding repeats adopt extended structures along protofilament crests.
  • These structures stabilize the interface between tubulin dimers.
  • A model of tandem repeat binding along protofilaments was proposed, tethering tubulin dimers and stabilizing MT polymerization.

Conclusions:

  • The study provides atomic-level insights into tau-MT interactions.
  • The findings explain how tau phosphorylation affects MT binding.
  • The proposed model clarifies tau's role in microtubule stabilization.

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