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

Flightin is essential for thick filament assembly and sarcomere stability in Drosophila flight muscles.

The Journal of cell biology - 25 Dec 2000

Reedy M C, Bullard B, Vigoreaux J O

Abstract excerpt

Flightin is a multiply phosphorylated, 20-kD myofibrillar protein found in Drosophila indirect flight muscles (IFM). Previous work suggests that flightin plays an essential, as yet undefined, role in normal sarcomere structure and contractile activity. Here we show that flightin is associated with thick filaments where it is likely to interact with the myosin rod. We have created a null mutation for flightin,...

Read the complete abstract on PubMed

Topics

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

Share to Filamins
Share to Flight, Animal
Share to Immune Sera

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Electron, Scanning

Share to Myosins

Share to Sarcomeres

Share to Solubility

Source

Open in PubMed Open full text

Identifiers

PMID: 11134077
DOI: 10.1083/jcb.151.7.1483
PMCID: PMC2150682

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

Flightin is essential for thick filament assembly and sarcomere stability in Drosophila flight muscles.PMID 11134077Read ↗

Flightin is necessary for length determination, structural integrity, and large bending stiffness of insect flight muscle thick filaments.Semantic proximity Read ↗

Alterations in flightin phosphorylation in Drosophila flight muscles are associated with myofibrillar defects engendered by actin and myosin heavy-chain mutant alleles.Semantic proximity Read ↗

Site directed mutagenesis of Drosophila flightin disrupts phosphorylation and impairs flight muscle structure and mechanics.Semantic proximity Read ↗

A genetic deficiency that spans the flightin gene of Drosophila melanogaster affects the ultrastructure and function of the flight muscles.Semantic proximity Read ↗

Mutations in Drosophila myosin rod cause defects in myofibril assembly.Semantic proximity Read ↗

Flightless I and LRRFIP work together to regulate lateral growth of the sarcomeres in <i>Drosophila</i>Semantic proximity Read ↗

Filamin protects myofibrils from contractile damage through changes in its mechanosensory region.Semantic proximity Read ↗

COOH-terminal truncation of flightin decreases myofilament lattice organization, cross-bridge binding, and power output in Drosophila indirect flight muscle.Semantic proximity Read ↗

Troponin I is required for myofibrillogenesis and sarcomere formation in Drosophila flight muscle.Semantic proximity Read ↗

Assembly of the giant protein projectin during myofibrillogenesis in Drosophila indirect flight muscles.Semantic proximity Read ↗

Assembly of thick filaments and myofibrils occurs in the absence of the myosin head.Semantic proximity Read ↗

The Drosophila Z-disc Protein Z(210) Is an Adult Muscle Isoform of Zasp52, Which Is Required for Normal Myofibril Organization in Indirect Flight MusclesSemantic proximity Read ↗

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