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 chemical genetic screen for direct v-Src substrates reveals ordered assembly of a retrograde signaling pathway.

Chemistry & biology - 1 Jan 2002

Shah Kavita, Shokat Kevan M

Abstract excerpt

Using an ATP analog that is a specific substrate for an analog-specific allele of v-Src, we identified several novel cytoskeletal substrates that control actin assembly processes. A screen for less abundant v-Src substrates revealed the scaffolding protein Dok-1 as a direct substrate of v-Src. Further studies suggest that v-Src phosphorylation sites on Dok-1 are critical for its binding to RasGAP and Csk,...

Read the complete abstract on PubMed

Topics

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

Share to 3T3 Cells
Share to DNA-Binding Proteins
Share to Oncogene Protein pp60(v-src)

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phosphoproteins

Share to Phosphorylation

Share to RNA-Binding Proteins

Share to Signal Transduction

Share to Substrate Specificity

Source

Identifiers

PMID: 11841937
DOI: 10.1016/s1074-5521(02)00086-8

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

A chemical genetic screen for direct v-Src substrates reveals ordered assembly of a retrograde signaling pathway.PMID 11841937Read ↗

Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates.Semantic proximity Read ↗

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

The road to Src.Semantic proximity Read ↗

Engineered kinase activation reveals unique morphodynamic phenotypes and associated trafficking for Src family isoforms.Semantic proximity Read ↗

Development of an efficient "substrate-trapping" mutant of Src homology phosphotyrosine phosphatase 2 and identification of the epidermal growth factor receptor, Gab1, and three other proteins as target substrates.Semantic proximity Read ↗

SRC: A Century of Science Brought to the ClinicSemantic proximity Read ↗

Subcellular receptor redistribution and enhanced microspike formation by a Ret receptor preferentially recruiting Dok.Semantic proximity Read ↗

A FAK/Src chimera with gain-of-function properties promotes formation of large peripheral adhesions associated with dynamic actin assembly.Semantic proximity Read ↗

Dissecting motility signaling through activation of specific Src-effector complexes.Semantic proximity Read ↗

The evolutionarily conserved arrangement of domains in SRC family kinases is important for substrate recognition.Semantic proximity Read ↗

Design of allele-specific inhibitors to probe protein kinase signaling.Semantic proximity Read ↗

The intrinsic ability of AFAP-110 to alter actin filament integrity is linked with its ability to also activate cellular tyrosine kinases.Semantic proximity Read ↗

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