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Updated: Mar 30, 2026

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
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Published on: March 15, 2014

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Structural Change in the Dynein Stalk Region Associated with Two Different Affinities for the Microtubule

Yosuke Nishikawa1, Momoko Inatomi1, Haruka Iwasaki1

  • 1Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.

Journal of Molecular Biology
|November 21, 2015
PubMed

Insights

Dynein motor proteins use a coiled-coil stalk to communicate between ATP hydrolysis sites and microtubule binding. This study reveals structural changes in the dynein stalk, proposing an "open zipper model" for affinity regulation.

Area of Science:

  • Molecular Biology
  • Biophysics
  • Structural Biology

Background:

  • Dynein is a crucial microtubule-based motor protein complex.
  • It requires coordinated ATP hydrolysis for mechanical force and track binding.
  • A significant structural gap exists between nucleotide-binding sites and the microtubule-binding domain, necessitating long-range communication.

Purpose of the Study:

  • To investigate structural changes in the dynein stalk region.
  • To understand how these changes modulate microtubule-binding affinity.
  • To elucidate the communication mechanism between ATP hydrolysis and dynein-microtubule interactions.

Main Methods:

  • Improved resolution of existing dynein stalk structures.
  • Comparative analysis of available X-ray crystal structures.
  • Examination of dynein stalk and strut/buttress regions.

Main Results:

  • Structural changes in the dynein stalk and strut/buttress regions were identified.
  • The basis for transitioning between low and high microtubule affinity was elucidated.
  • A modified "open zipper model" was proposed to explain these transitions.

Conclusions:

  • The "open zipper model" provides a specific mechanism for dynein's long-range communication.
  • Structural rearrangements in the stalk are key to regulating dynein's microtubule binding affinity.
  • This research enhances understanding of motor protein regulation and function.
Keywords:
X-ray crystallographycytoskeletal motor proteindyneinstalk coiled coil

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