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

Tyrosine phosphorylation of the CrkII adaptor protein modulates cell migration.

Journal of cell science - 1 Aug 2003

Takino Takahisa, Tamura Masahito, Miyamori Hisashi, Araki Masaru, Matsumoto Kazue, Sato Hiroshi, Yamada Kenneth M

Abstract excerpt

CrkII belongs to a family of adaptor proteins that become tyrosine phosphorylated after various stimuli. We examined the role of CrkII tyrosine phosphorylation in fibronectin-induced cell migration. Overexpression of CrkII inhibited dephosphorylation of focal adhesion components such as p130 Crk-associated substrate (p130cas) and paxillin by protein tyrosine phosphatase 1B (PTP1B). Tyrosine-phosphorylated CrkII...

Read the complete abstract on PubMed

Topics

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

Share to Tyrosine
Share to Fibronectins
Share to Luminescent Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Paxillin

Share to Protein Tyrosine Phosphatase, Non-Receptor Type 1

Share to Protein Tyrosine Phosphatases

Share to Retinoblastoma-Like Protein p130

Share to RNA, Small Interfering

Source

Identifiers

PMID: 12799422
DOI: 10.1242/jcs.00632

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tyrosine phosphorylation of the CrkII adaptor protein modulates cell migration.PMID 12799422Read ↗

Calcium and calmodulin-dependent serine/threonine protein kinase type II (CaMKII)-mediated intramolecular opening of integrin cytoplasmic domain-associated protein-1 (ICAP-1α) negatively regulates β1 integrins.Semantic proximity Read ↗

Activation of Rac1 by paxillin-Crk-DOCK180 signaling complex is antagonized by Rap1 in migrating NBT-II cells.Semantic proximity Read ↗

Crk associates with a multimolecular Paxillin/GIT2/beta-PIX complex and promotes Rac-dependent relocalization of Paxillin to focal contacts.Semantic proximity Read ↗

Interactions between two cytoskeleton-associated tyrosine kinases: calcium-dependent tyrosine kinase and focal adhesion tyrosine kinase.Semantic proximity Read ↗

Novel role for CRK adaptor proteins as essential components of SRC/FAK signaling for epithelial–mesenchymal transition and colorectal cancer aggressivenessSemantic proximity Read ↗

Extracellular-regulated kinase activation and CAS/Crk coupling regulate cell migration and suppress apoptosis during invasion of the extracellular matrix.Semantic proximity Read ↗

FAK-mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation.Semantic proximity Read ↗

Essential roles of Crk and CrkL in fibroblast structure and motility.Semantic proximity Read ↗

Tyrosine phosphorylation within the SH3 domain regulates CAS subcellular localization, cell migration, and invasiveness.Semantic proximity Read ↗

Activation of the focal adhesion kinase signaling pathway by structural alterations in the carboxyl-terminal region of c-Crk II.Semantic proximity Read ↗

Differential regulation of cell migration, actin stress fiber organization, and cell transformation by functional domains of Crk-associated substrate.Semantic proximity Read ↗

Cortactin as a target for FAK in the regulation of focal adhesion dynamics.Semantic proximity Read ↗

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