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

Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled.

Molecular and cellular biology - 1 Jan 1998

Comer A R, Ahern-Djamali S M, Juang J L, Jackson P D, Hoffmann F M

Abstract excerpt

Drosophila Enabled (Ena) is a member of a family of cytoskeleton-associated proteins including mammalian vasodilator-stimulated phosphoprotein and murine Enabled that regulate actin cytoskeleton assembly. Mutations in Drosophila ena were discovered as dominant genetic suppressors of mutations in...

Read the complete abstract on PubMed

Topics

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

Share to DNA-Binding Proteins
Share to Drosophila
Share to Genes, abl

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Phosphorylation

Share to Protein Binding

Share to Signal Transduction

Share to src Homology Domains

Source

Open in PubMed Open full text

Identifiers

PMID: 9418863
DOI: 10.1128/MCB.18.1.152
PMCID: PMC121469

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-9418863-2026-09-04.2. 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

Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled.PMID 9418863Read ↗

Balancing different types of actin polymerization at distinct sites: roles for Abelson kinase and Enabled.Semantic proximity Read ↗

The tyrosine kinase Abl and its substrate enabled collaborate with the receptor phosphatase Dlar to control motor axon guidance.Semantic proximity Read ↗

Abelson kinase's intrinsically disordered region plays essential roles in protein function and protein stability.Semantic proximity Read ↗

Phosphorylated proteome analysis of a novel germline ABL1 mutation causing an autosomal dominant syndrome with ventricular septal defect.Semantic proximity Read ↗

Mena and vasodilator-stimulated phosphoprotein are required for multiple actin-dependent processes that shape the vertebrate nervous system.Semantic proximity Read ↗

Identification and functional analysis of a new phosphorylation site (Y398) in the SH3 domain of Abi-1.Semantic proximity Read ↗

Molecular and phylogenetic characterization of Zyx102, a Drosophila orthologue of the zyxin family that interacts with Drosophila Enabled.Semantic proximity Read ↗

Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration.Semantic proximity Read ↗

Characterization of a novel interaction between vasodilator-stimulated phosphoprotein and Abelson interactor 1 in human platelets: a concerted computational and experimental approach.Semantic proximity Read ↗

Targeted disruption of an EH-domain protein endocytic complex, Pan1-End3.Semantic proximity Read ↗

Regulation of actin polymerization and adhesion-dependent cell edge protrusion by the Abl-related gene (Arg) tyrosine kinase and N-WASp.Semantic proximity Read ↗

Increased levels of the Drosophila Abelson tyrosine kinase in nerves and muscles: subcellular localization and mutant phenotypes imply a role in cell-cell interactions.Semantic proximity Read ↗

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