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 conserved sequence motif bridges two protein kinases for enhanced phosphorylation and nuclear function of a splicing factor.

The FEBS journal - 1 Jan 2021

Aubol Brandon E, Fattet Laurent, Adams Joseph A

Abstract excerpt

The assembly and activation of the spliceosome rely upon the phosphorylation of an essential family of splicing factors known as the serine-arginine (SR) proteins. Although it has been demonstrated recently that two enzyme families, the SR protein kinases (SRPKs) and the Cdc2-like kinases (CLKs), can function as a complex to efficiently phosphorylate these SR proteins in the nucleus, the molecular features...

Read the complete abstract on PubMed

Topics

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

Share to Alternative Splicing
Share to Conserved Sequence
Share to Cytoplasm

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Share to Protein Processing, Post-Translational

Share to Protein-Tyrosine Kinases

Source

Identifiers

PMID: 32359191
DOI: 10.1111/febs.15351

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

A conserved sequence motif bridges two protein kinases for enhanced phosphorylation and nuclear function of a splicing factor.PMID 32359191Read ↗

Phosphoproteomics identifies the DYRK1B protein kinase as a regulator of processing bodiesSemantic proximity Read ↗

Evidence for disulfide bonds in SR Protein Kinase 1 (SRPK1) that are required for activity and nuclear localization.Semantic proximity Read ↗

Defining novel targets and functions of the protein kinase DYRK2Semantic proximity Read ↗

SR protein kinases promote splicing of nonconsensus introns.Semantic proximity Read ↗

Splice Variants of the Dual Specificity Tyrosine Phosphorylation-regulated Kinase 4 (DYRK4) Differ in Their Subcellular Localization and Catalytic ActivitySemantic proximity Read ↗

Differential tyrosine phosphorylation controls the function of CNK1 as a molecular switch in signal transduction.Semantic proximity Read ↗

Multiple mechanisms regulate subcellular localization of human CDC6.Semantic proximity Read ↗

Comparison of the CDC2-like kinase family across eukaryotes highlights the functional conservation of these unique biological thermometersSemantic proximity Read ↗

Dsk1p kinase phosphorylates SR proteins and regulates their cellular localization in fission yeast.Semantic proximity Read ↗

Nuclear Speckle Dynamics are Controlled by Polyphosphate Inhibition of CLK ProteinsSemantic proximity Read ↗

The RNP protein, RNPS1, associates with specific isoforms of the P34CDC2 related PITSLRE protein kinase in vivoSemantic proximity Read ↗

Prp4 Kinase Grants the License to Splice: Control of Weak Splice Sites during Spliceosome Activation.Semantic proximity Read ↗

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