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

Drosophila Symplekin localizes dynamically to the histone locus body and tricellular junctions.

Nucleus (Austin, Tex.) - 1 Jan 2014

Tatomer Deirdre C, Rizzardi Lindsay F, Curry Kaitlin P, Witkowski Alison M, Marzluff William F, Duronio Robert J

Abstract excerpt

The scaffolding protein Symplekin is part of multiple complexes involved in generating and modifying the 3' end of mRNAs, including cleavage-polyadenylation, histone pre-mRNA processing and cytoplasmic polyadenylation. To study these functions in vivo, we examined the localization of Symplekin during development and generated mutations of the Drosophila Symplekin gene. Mutations in Symplekin that reduce Symplekin...

Read the complete abstract on PubMed

Topics

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

Share to Cytoplasm
Share to Embryo, Nonmammalian

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Embryonic Development

Share to Histones

Share to Intranuclear Inclusion Bodies

Share to mRNA Cleavage and Polyadenylation Factors

Share to Polyadenylation

Share to S Phase

Source

Open in PubMed Open full text

Identifiers

PMID: 25493544
DOI: 10.4161/19491034.2014.990860
PMCID: PMC4615279

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

Drosophila Symplekin localizes dynamically to the histone locus body and tricellular junctions.PMID 25493544Read ↗

In vivo characterization of the Drosophila mRNA 3' end processing core cleavage complex.Semantic proximity Read ↗

A complex containing the CPSF73 endonuclease and other polyadenylation factors associates with U7 snRNP and is recruited to histone pre-mRNA for 3'-end processing.Semantic proximity Read ↗

U7 snRNA mutations in Drosophila block histone pre-mRNA processing and disrupt oogenesis.Semantic proximity Read ↗

Concentrating pre-mRNA processing factors in the histone locus body facilitates efficient histone mRNA biogenesis.Semantic proximity Read ↗

Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progression.Semantic proximity Read ↗

poly is required for nurse-cell chromosome dispersal and oocyte polarity in Drosophila.Semantic proximity Read ↗

Hrb27C, Sqd and Otu cooperatively regulate gurken RNA localization and mediate nurse cell chromosome dispersion in Drosophila oogenesis.Semantic proximity Read ↗

The Drosophila U7 snRNP proteins Lsm10 and Lsm11 are required for histone pre-mRNA processing and play an essential role in development.Semantic proximity Read ↗

Loss of the histone pre-mRNA processing factor stem-loop binding protein in Drosophila causes genomic instability and impaired cellular proliferation.Semantic proximity Read ↗

Developmental analysis of Spalt function in the Drosophila prothoracic gland.Semantic proximity Read ↗

Lead-Induced Molecular Alterations and Symplekins’ Role in Tight Junction Dynamics: Implications for CancerSemantic proximity Read ↗

Genome-wide localization of exosome components to active promoters and chromatin insulators in Drosophila.Semantic proximity Read ↗

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