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

Dishevelled3 is a novel arginine methyl transferase substrate.

Scientific reports - 1 Jan 2012

Bikkavilli Rama Kamesh, Avasarala Sreedevi, Vanscoyk Michelle, Sechler Marybeth, Kelley Nicole, Malbon Craig C, Winn Robert A

Abstract excerpt

Dishevelled, a phosphoprotein scaffold, is a central component in all the Wnt-sensitive signaling pathways. In the present study, we report that Dishevelled is post-translationally modified, both in vitro and in vivo, via arginine methylation. We also show protein arginine methyl transferases 1 a...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Dishevelled Proteins
Share to Methylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phosphoproteins

Share to Protein-Arginine N-Methyltransferases

Share to Wnt Proteins

Share to Xenopus

Share to Zebrafish

Source

Open in PubMed Open full text

Identifiers

PMID: 23150776
DOI: 10.1038/srep00805
PMCID: PMC3496165

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23150776-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dishevelled3 is a novel arginine methyl transferase substrate.PMID 23150776Read ↗

Protein Arginine Methyltransferase PRMT1 Is Essential for Palatogenesis.Semantic proximity Read ↗

A mouse PRMT1 null allele defines an essential role for arginine methylation in genome maintenance and cell proliferation.Semantic proximity Read ↗

Methylation of the phosphatase-transcription activator EYA1 by protein arginine methyltransferase 1: mechanistic, functional, and structural studies.Semantic proximity Read ↗

Prmt5 promotes vascular morphogenesis independently of its methyltransferase activity.Semantic proximity Read ↗

Profiling substrates of protein arginine N-methyltransferase 3 with S-adenosyl-L-methionine analogues.Semantic proximity Read ↗

PRMT4-mediated arginine methylation negatively regulates retinoblastoma tumor suppressor protein and promotes E2F-1 dissociation.Semantic proximity Read ↗

Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor.Semantic proximity Read ↗

Leucine repeat adaptor protein 1 interacts with Dishevelled to regulate gastrulation cell movements in zebrafish.Semantic proximity Read ↗

Drosophila arginine methyltransferase 1 (DART1) is an ecdysone receptor co-repressor.Semantic proximity Read ↗

Gpr125 modulates Dishevelled distribution and planar cell polarity signaling.Semantic proximity Read ↗

Lysine methylation of nuclear co-repressor receptor interacting protein 140.Semantic proximity Read ↗

Arginine methyltransferase CARM1/PRMT4 regulates endochondral ossificationSemantic proximity Read ↗

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