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

Lipid binding by the Unique and SH3 domains of c-Src suggests a new regulatory mechanism.

Scientific reports - 1 Jan 2013

Pérez Yolanda, Maffei Mariano, Igea Ana, Amata Irene, Gairí Margarida, Nebreda Angel R, Bernadó Pau, Pons Miquel

Abstract excerpt

c-Src is a non-receptor tyrosine kinase involved in numerous signal transduction pathways. The kinase, SH3 and SH2 domains of c-Src are attached to the membrane-anchoring SH4 domain through the flexible Unique domain. Here we show intra- and intermolecular interactions involving the Unique and SH3 domains suggesting the presence of a previously unrecognized additional regulation layer in c-Src. We have...

Read the complete abstract on PubMed

Topics

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

Share to src-Family Kinases
Share to Allosteric Regulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Calmodulin

Share to CSK Tyrosine-Protein Kinase

Share to Oocytes

Share to Phosphatidylglycerols

Share to src Homology Domains

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 23416516
DOI: 10.1038/srep01295
PMCID: PMC3575015

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

Lipid binding by the Unique and SH3 domains of c-Src suggests a new regulatory mechanism.PMID 23416516Read ↗

Regulation of Src tumor activity by its N-terminal intrinsically disordered regionSemantic proximity Read ↗

Lipid-driven Src self-association modulates its transformation capacity.Semantic proximity Read ↗

Lipid-driven SRC self-association modulates its transformation capacitySemantic proximity Read ↗

The Src module: an ancient scaffold in the evolution of cytoplasmic tyrosine kinases.Semantic proximity Read ↗

Characterization of unique functionalities in c-Src domains required for osteoclast podosome belt formationSemantic proximity Read ↗

Disruption of Ca2+/calmodulin:KSR1 interaction lowers ERK activation.Semantic proximity Read ↗

Proteomic Analysis of Src Family Kinase Phosphorylation States in Cancer Cells Suggests Deregulation of the Unique Domain.Semantic proximity Read ↗

Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src.Semantic proximity Read ↗

Identification of targets of c-Src tyrosine kinase by chemical complementation and phosphoproteomics.Semantic proximity Read ↗

The role of Src in solid and hematologic malignancies: development of new-generation Src inhibitors.Semantic proximity Read ↗

Phenotypic profiling of the human genome reveals gene products involved in plasma membrane targeting of SRC kinases.Semantic proximity Read ↗

c-Src signaling induced by the adapters Sin and Cas is mediated by Rap1 GTPase.Semantic proximity Read ↗

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