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

Regulatory ATPase sites of cytoplasmic dynein affect processivity and force generation.

The Journal of biological chemistry - 19 Sept 2008

Cho Carol, Reck-Peterson Samara L, Vale Ronald D

Abstract excerpt

The heavy chain of cytoplasmic dynein contains four nucleotide-binding domains referred to as AAA1-AAA4, with the first domain (AAA1) being the main ATP hydrolytic site. Although previous studies have proposed regulatory roles for AAA3 and AAA4, the role of ATP hydrolysis at these sites remains elusive. Here, we have analyzed the single molecule motility properties of yeast cytoplasmic dynein mutants bearing...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Allosteric Site
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dyneins

Share to Hydrolysis

Share to Molecular Conformation

Share to Nucleotides

Share to Stress, Mechanical

Source

Open in PubMed Open full text

Identifiers

PMID: 18650442
DOI: 10.1074/jbc.M802951200
PMCID: PMC2533788

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulatory ATPase sites of cytoplasmic dynein affect processivity and force generation.PMID 18650442Read ↗

Molecular dissection of the roles of nucleotide binding and hydrolysis in dynein's AAA domains in Saccharomyces cerevisiae.Semantic proximity Read ↗

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

The myosin superfamily at a glanceSemantic proximity Read ↗

Cytoplasmic dynein-2 at a glanceSemantic proximity Read ↗

The role of ATP hydrolysis for kinesin processivity.Semantic proximity Read ↗

Cytoplasmic dynein ATPase activity is regulated by dynactin-dependent phosphorylation.Semantic proximity Read ↗

Lethal kinesin mutations reveal amino acids important for ATPase activation and structural coupling.Semantic proximity Read ↗

Intracellular force comparison of pathogenic KIF1A, KIF5, and dynein by fluctuation analysisSemantic proximity Read ↗

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

Pac1/LIS1 promotes an uninhibited conformation of dynein that coordinates its localization and activitySemantic proximity Read ↗

Differential effects of the dynein-regulatory factor Lissencephaly-1 on processive dynein-dynactin motility.Semantic proximity Read ↗

The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.Semantic proximity Read ↗

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