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

Gab2 phosphorylation by RSK inhibits Shp2 recruitment and cell motility.

Molecular and cellular biology - 1 Apr 2013

Zhang Xiaocui, Lavoie Genevieve, Fort Loic, Huttlin Edward L, Tcherkezian Joseph, Galan Jacob A, Gu Haihua, Gygi Steven P, Carreno Sebastien, Roux Philippe P

Abstract excerpt

The scaffolding adapter protein Gab2 (Grb2-associated binder) participates in the signaling response evoked by various growth factors and cytokines. Gab2 is overexpressed in several human malignancies, including breast cancer, and was shown to promote mammary epithelial cell migration. The role of Gab2 in the activation of different signaling pathways is well documented, but less is known regarding the feedback...

Read the complete abstract on PubMed

Topics

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

Share to RNA, Small Interfering
Share to Benzamides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to GRB2 Adaptor Protein

Share to Mitogen-Activated Protein Kinase 1

Share to Mitogen-Activated Protein Kinase 3

Share to Protein Tyrosine Phosphatase, Non-Receptor Type 11

Share to Ribosomal Protein S6 Kinases, 90-kDa

Share to RNA Interference

Source

Open in PubMed Open full text

Identifiers

PMID: 23401857
DOI: 10.1128/MCB.01353-12
PMCID: PMC3624252

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

Gab2 phosphorylation by RSK inhibits Shp2 recruitment and cell motility.PMID 23401857Read ↗

Gab2 regulates cytoskeletal organization and migration of mammary epithelial cells by modulating RhoA activation.Semantic proximity Read ↗

Receptor-specific regulation of phosphatidylinositol 3'-kinase activation by the protein tyrosine phosphatase Shp2.Semantic proximity Read ↗

G-CSF stimulates Jak2-dependent Gab2 phosphorylation leading to Erk1/2 activation and cell proliferation.Semantic proximity Read ↗

A novel role for Gab1 and SHP2 in epidermal growth factor-induced Ras activation.Semantic proximity Read ↗

Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor.Semantic proximity Read ↗

The tyrosine phosphatase SHP-2 is required for sustained activation of extracellular signal-regulated kinase and epithelial morphogenesis downstream from the met receptor tyrosine kinase.Semantic proximity Read ↗

RSK is a principal effector of the RAS-ERK pathway for eliciting a coordinate promotile/invasive gene program and phenotype in epithelial cells.Semantic proximity Read ↗

RSK2 drives cell motility by serine phosphorylation of LARG and activation of Rho GTPases.Semantic proximity Read ↗

Phosphotyrosines 627 and 659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) conferring binding and activation of SHP2.Semantic proximity Read ↗

Participation of both Gab1 and Gab2 in the activation of the ERK/MAPK pathway by epidermal growth factor.Semantic proximity Read ↗

14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activity.Semantic proximity Read ↗

A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1.Semantic proximity Read ↗

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