Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis for two-way communication between dynein and microtubules.

Nature communications - 25 Feb 2020

Nishida Noritaka, Komori Yuta, Takarada Osamu, Watanabe Atsushi, Tamura Satoko, Kubo Satoshi, Shimada Ichio, Kikkawa Masahide

Abstract excerpt

The movements of cytoplasmic dynein on microtubule (MT) tracks is achieved by two-way communication between the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk, but the structural basis of this communication remains elusive. Here, we regulate MTBD either in high-affinity or low-affinity states by introducing a disulfide bond to the stalk and analyze the resulting structures by NMR...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cryoelectron Microscopy
Share to Disulfides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dyneins

Share to Microtubules

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Domains

Share to Protein Structure, Quaternary

Share to Tubulin

Source

Open in PubMed Open full text

Identifiers

PMID: 32098965
DOI: 10.1038/s41467-020-14842-8
PMCID: PMC7042235

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for two-way communication between dynein and microtubules.PMID 32098965Read ↗

Backbone and side-chain ¹H, ¹⁵N, and ¹³C resonance assignments of the microtubule-binding domain of yeast cytoplasmic dynein in the high and low-affinity states.Semantic proximity Read ↗

Cryo-EM Reveals the Mechanochemical Cycle of Reactive Full-length Human Dynein-1Semantic proximity Read ↗

Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teamsSemantic proximity Read ↗

Tension on the linker gates the ATP-dependent release of dynein from microtubules.Semantic proximity Read ↗

Two-state displacement by the kinesin-14 Ncd stalk.Semantic proximity Read ↗

Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin.Semantic proximity Read ↗

An extended microtubule-binding structure within the dynein motor domain.Semantic proximity Read ↗

Structural model of microtubule dynamics inhibition by Kinesin-4 from the crystal structure of KLP-12 –tubulin complexSemantic proximity Read ↗

Effect of amino acid mutations on intra-dimer tubulin-tubulin binding strength of microtubules.Semantic proximity Read ↗

Role of coiled-coil registry shifts in activation of human Bicaudal D2 for dynein recruitment upon cargo-bindingSemantic proximity Read ↗

Direct observation of intermediate states during the stepping motion of kinesin-1.Semantic proximity Read ↗

Key residues on microtubule responsible for activation of kinesin ATPase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.