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

Identification and characterization of Drosophila Snurportin reveals a role for the import receptor Moleskin/importin-7 in snRNP biogenesis.

Molecular biology of the cell - 1 Sept 2013

Natalizio Amanda Hicks, Matera A Gregory

Abstract excerpt

Nuclear import is an essential step in small nuclear ribonucleoprotein (snRNP) biogenesis. Snurportin1 (SPN1), the import adaptor, binds to trimethylguanosine (TMG) caps on spliceosomal small nuclear RNAs. Previous studies indicated that vertebrate snRNP import requires importin-β, the transport receptor that binds directly to SPN1. We identify CG42303/snup as the Drosophila orthologue of human snurportin1...

Read the complete abstract on PubMed

Topics

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

Share to beta Karyopherins
Share to Cell Nucleus
Share to Drosophila Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanosine

Share to Karyopherins

Share to Protein Transport

Share to Receptors, Cytoplasmic and Nuclear

Share to Ribonucleoproteins, Small Nuclear

Source

Open in PubMed Open full text

Identifiers

PMID: 23885126
DOI: 10.1091/mbc.E13-03-0118
PMCID: PMC3771954

Genes

SNUPN

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and characterization of Drosophila Snurportin reveals a role for the import receptor Moleskin/importin-7 in snRNP biogenesis.PMID 23885126Read ↗

SNUPN variants cause spinocerebellar atrophy by disrupting global splicing in cerebellar Purkinje cells.Semantic proximity Read ↗

Cross-talk between snurportin1 subdomains.Semantic proximity Read ↗

WRAP53 Is Essential for Cajal Body Formation and for Targeting the Survival of Motor Neuron Complex to Cajal BodiesSemantic proximity Read ↗

Identification and characterisation of a nuclear localisation signal in the SMN associated protein, Gemin4.Semantic proximity Read ↗

Disruption of snRNP biogenesis factors Tgs1 and pICln induces phenotypes that mirror aspects of SMN-Gemins complex perturbation in Drosophila, providing new insights into spinal muscular atrophy.Semantic proximity Read ↗

SMN and Gemins: ‘We are family’ … or are we?Semantic proximity Read ↗

Direct Interaction of the Spinal Muscular Atrophy Disease Protein SMN with the Small Nucleolar RNA-associated Protein FibrillarinSemantic proximity Read ↗

<i>Gemin4</i> is an essential gene in mice, and its overexpression in human cells causes relocalization of the SMN complex to the nucleoplasmSemantic proximity Read ↗

The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis.Semantic proximity Read ↗

Genetic<i>SNUPN</i>variants cause spinocerebellar atrophy by disrupting global splicing in Purkinje cellsSemantic proximity Read ↗

An epilepsy-associated mutation in the nuclear import receptor KPNA7 reduces nuclear localization signal binding.Semantic proximity Read ↗

The Drosophila U2 snRNP protein U2A' has an essential function that is SNF/U2B" independent.Semantic proximity Read ↗

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