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

Involvement of tail domains in regulation of Dictyostelium myosin II.

Biochemical and biophysical research communications - 29 Apr 2000

Liu X, Ito K, Lee R J, Uyeda T Q

Abstract excerpt

The actin-dependent ATPase activity of Dictyostelium myosin II filaments is regulated by phosphorylation of the regulatory light chain. Four deletion mutant myosins which lack different parts of subfragment 2 (S2) showed phosphorylation-independent elevations in their activities. Phosphorylation-independent elevation in the activity was also achieved by a double point mutation to replace conserved Glu932 and...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Dictyostelium
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Green Fluorescent Proteins

Share to Luminescent Proteins

Share to Myosins

Share to Point Mutation

Share to Protein Conformation

Source

Identifiers

PMID: 10777684
DOI: 10.1006/bbrc.2000.2582

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Involvement of tail domains in regulation of Dictyostelium myosin II.PMID 10777684Read ↗

Regulation of Dictyostelium myosin II by phosphorylation: what is essential and what is important?Semantic proximity Read ↗

Modulation of actin filament sliding by mutations of the SH2 cysteine in Dictyostelium myosin II.Semantic proximity Read ↗

Dictyostelium myosin heavy chain phosphorylation sites regulate myosin filament assembly and localization in vivo.Semantic proximity Read ↗

Molecular genetic truncation analysis of filament assembly and phosphorylation domains of Dictyostelium myosin heavy chain.Semantic proximity Read ↗

Conditional loss-of-myosin-II-function mutants reveal a position in the tail that is critical for filament nucleation.Semantic proximity Read ↗

Single-headed myosin II acts as a dominant negative mutation in Dictyostelium.Semantic proximity Read ↗

Evidence for a novel, strongly bound acto-S1 complex carrying ADP and phosphate stabilized in the G680V mutant of Dictyostelium myosin II.Semantic proximity Read ↗

Changes in Mg2+ ion concentration and heavy chain phosphorylation regulate the motor activity of a class I myosin.Semantic proximity Read ↗

Myosin II can be localized to the cleavage furrow and to the posterior region of Dictyostelium amoebae without control by phosphorylation of myosin heavy and light chains.Semantic proximity Read ↗

Novel Dictyostelium unconventional myosin MyoK is a class I myosin with the longest loop-1 insert and the shortest tail.Semantic proximity Read ↗

Dictyostelium myosin II G680V suppressors exhibit overlapping spectra of biochemical phenotypes including facilitated phosphate release.Semantic proximity Read ↗

Dictyostelium myosin IK is involved in the maintenance of cortical tension and affects motility and phagocytosis.Semantic proximity Read ↗

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