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

Nuclear-Cytoplasmic Shuttling of the Usher Syndrome 1G Protein SANS Differs from Its Paralog ANKS4B.

Cells - 8 Nov 2024

Fritze Jacques S, Stiehler Felizitas F, Wolfrum Uwe

Abstract excerpt

The USH1G protein SANS is a small multifunctional scaffold protein. It is involved in several different cellular processes, such as intracellular transport, in the cytoplasm, or splicing of pre-mRNA, in the cell nucleus. Here, we aimed to gain insight into the regulation of the subcellular localization and the nuclear-cytoplasmic shuttling of SANS and its paralog ANKS4B, not yet reported in the nucleus. We...

Read the complete abstract on PubMed

Topics

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

Share to Active Transport, Cell Nucleus
Share to Cell Nucleus
Share to Cytoplasm

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to HeLa Cells

Share to Nuclear Export Signals

Share to Nuclear Localization Signals

Share to RNA-Binding Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 39594604
DOI: 10.3390/cells13221855
PMCID: PMC11592671

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nuclear-Cytoplasmic Shuttling of the Usher Syndrome 1G Protein SANS Differs from Its Paralog ANKS4B.PMID 39594604Read ↗

SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear transfer of tri-snRNP complexesSemantic proximity Read ↗

Pathogenic Variants in USH1G/SANS Alter the Protein Interaction With the Pre-RNA Processing Factors PRPF6 and PRPF31 of the SpliceosomeSemantic proximity Read ↗

From the sideline: Tissue-specific nucleoporin function in health and disease, an update.Semantic proximity Read ↗

Spatial proteomic mapping of human nuclear bodies reveals new functional insights into RNA regulationSemantic proximity Read ↗

The Role of Nuclear Bodies in Gene Expression and DiseaseSemantic proximity Read ↗

Nuclear speckleopathies: developmental disorders caused by variants in genes encoding nuclear speckle proteins.Semantic proximity Read ↗

UsnRNP trafficking is regulated by stress granules and compromised by mutant ALS proteins.Semantic proximity Read ↗

Characterization of the ternary Usher syndrome SANS/ush2a/whirlin protein complex.Semantic proximity Read ↗

Nuclear import sequence identification in hOAS3 protein.Semantic proximity Read ↗

Gene Expression Responses to FUS, EWS, and TAF15 Reduction and Stress Granule Sequestration Analyses Identifies FET-Protein Non-Redundant FunctionsSemantic proximity Read ↗

Mutations in nucleoporins and their roles in human diseases: Integrating evidence on specific NUP functions.Semantic proximity Read ↗

Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1.Semantic proximity Read ↗

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