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

A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an arrestin homolog.

Science (New York, N.Y.) - 27 Apr 1990

Yamada T, Takeuchi Y, Komori N, Kobayashi H, Sakai Y, Hotta Y, Matsumoto H

Abstract excerpt

The gene encoding the 49-kilodalton protein that undergoes light-induced phosphorylation in the Drosophila photoreceptor has been isolated and characterized. The encoded protein has 401 amino acid residues and a molecular mass of 44,972 daltons, and it shares approximately 42 percent amino acid sequence identity with arrestin (S-antigen), which has been proposed to quench the light-induced cascade of guanosine...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Cloning, Molecular

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

Share to Drosophila melanogaster

Share to Molecular Sequence Data

Share to Molecular Weight

Share to Mutation

Source

Identifiers

PMID: 2158671
DOI: 10.1126/science.2158671

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

A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an arrestin homolog.PMID 2158671Read ↗

Differential phosphorylation of the rhodopsin cytoplasmic tail mediates the binding of arrestin and its splice variant, p44.Semantic proximity Read ↗

Phosphorylation of rat melanopsin at Ser-381 and Ser-398 by light/dark and its importance for intrinsically photosensitive ganglion cells (ipRGCs) cellular Ca2+ signaling.Semantic proximity Read ↗

Arrestin residues involved in the functional binding of arrestin to phosphorylated, photolyzed rhodopsin.Semantic proximity Read ↗

Phosphorylation of the Drosophila transient receptor potential ion channel is regulated by the phototransduction cascade and involves several protein kinases and phosphatases.Semantic proximity Read ↗

A role for the light-dependent phosphorylation of visual arrestin.Semantic proximity Read ↗

A splice variant of arrestin. Molecular cloning and localization in bovine retina.Semantic proximity Read ↗

Isolation and structure of an arrestin gene from Drosophila.Semantic proximity Read ↗

Light-induced translocation of Drosophila visual Arrestin2 depends on Rac2.Semantic proximity Read ↗

Proteomics of Drosophila compound eyes: early studies, now, and the future--light-induced protein phosphorylation as an example.Semantic proximity Read ↗

Arrestin translocation is stoichiometric to rhodopsin isomerization and accelerated by phototransduction in Drosophila photoreceptors.Semantic proximity Read ↗

Light-dependent phosphorylation of Bardet–Biedl syndrome 5 in photoreceptor cells modulates its interaction with arrestin1Semantic proximity Read ↗

Role of rhodopsin and arrestin phosphorylation in retinal degeneration of Drosophila.Semantic proximity Read ↗

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