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The adaptor proteins Crk and Crk-like (Crkl (show CRKL Proteins)), with which Dock proteins are known to interact physically, are also required for myoblast fusion.
The results suggest the involvement of Crk adaptor proteins in the early stages of T cell activation in which Crk might help recruiting effector proteins to the vicinity of the phospho-CD3zeta (show CD247 Proteins) and contribute to the fine-tuning of the TCR/CD3 (show CD3 Proteins)-coupled signal transduction pathways.
Study investigated structures and thermodynamics of the interactions mediated by N-terminal Src homology 3 domain of CrkII and proline-rich motifs (PRMs) of cAbl kinase, highlight the role of interfacial water molecules and the conformational entropy in the SH3:PRM interactions
CrkII mediates IGF-1 (show IGF1 Proteins) signaling and further balances pancreatic ductal adenocarcinoma biological behaviors via Erk1/2 and Akt (show AKT1 Proteins) pathway
In individuals with class I 17p13.3 microduplications including CRK, we recommend biochemical evaluation of the growth hormone axis. Providers caring for these patients should be aware of their possible risk for the development of central precocious puberty.
Crk Tyr251 phosphorylation regulate invasive cell phenotypes in glioblastoma.
CsA (show ERCC8 Proteins) and FK506 might interfere with selected effector T cell functions via a CrkII-, but not CrkI-dependent mechanisms.
Studied the role of PAK1/Crk axis in transduction of the oncogenic KRAS signal in non-small cell lung cancer (NSCLC).
in human c-CrkII, movement at position 239 and strain at position 272 are not tolerated because the beta-branched residues Ile239 and Val272 restrain the backbone mobility and thus destabilize the cis (show CISH Proteins) Pro238 form.
Data indicate the role of tyrosine phosphorylation in regulating modular domain utilization in v-crk sarcoma virus CT10 oncogene homolog (avian) protein (Crk).
evidence uncovered essential roles of CRK in invasive bladder cancer through the hepatocyte growth factor (show HGF Proteins)/c-Met/CRK feedback loop for epithelial-mesenchymal transition induction
the data suggest that CCRK (show CDK20 Proteins) positively regulates the kinetics by which ciliary proteins such as Smoothened and Gli2 are imported into the cilium, and that the efficiency of ciliary recruitment allows for potent responses to Hedgehog (show SHH Proteins) signaling over long time periods.
results suggest that Crk and CrkL (show CRKL Proteins) play essential overlapping roles in fibroblast growth.
both Crk and CrkL are required for the acquisition of cellular transformation by v-fos, whereas Crk plays a more prominent role than CrkL in v-ras-induced transformation.
results support a model in which Dok1 (show DOK1 Proteins) phosphorylation normally suppresses localized Ras pathway activity in Crk-transformed cells via recruitment and/or activation of RasGAP (show RASA1 Proteins)
Differential migration of CRK/CRKL (show CRKL Proteins)-deficient T cells resulted in efficient graft-versus-leukemia responses with minimal graft-versus-host disease in mice.
Crk1 (show MAPK14 Proteins)/2 and CrkL (show CRKL Proteins) are physically linked, functionally complement each other during podocyte foot process spreading, and together are required for developing typical foot process architecture.
Data suggest that interactions between Crk (proto-oncogene (show RAB1A Proteins) proteins c-crk) and Sos1 (Son of Sevenless homolog 1 (show SOS1 Proteins)) involve electrostatic interactions at binding sites.
Results suggest that Crk and CrkL (show CRKL Proteins) have critical roles in cell structure and motility by maintaining cytoskeletal integrity.
The v-Crk-myosin-1c interaction, which modulates membrane dynamics by regulating Rac1 activity, is crucial for cell adhesion and spreading.
The authors cloned SH2 domain-containing proteins they named GRBs (for growth factor receptor (show RYK Proteins)-bound). They identified GRB-3 as having 77% identity at the protein level and 80% similarity at the DNA level to v-crk.
This gene encodes a member of an adapter protein family that binds to several tyrosine-phosphorylated proteins. The product of this gene has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation. Two alternative transcripts encoding different isoforms with distinct biological activity have been described.
, adapter molecule crk
, v-crk sarcoma virus CT10 oncogene homolog (avian)
, proto-oncogene c-Crk
, avian sarcoma virus CT10 (v-crk) oncogene homolog
, proto-oncogene C-crk
, v-crk sarcoma virus CT10 oncogene homolog
, SH2/SH3 adaptor Crk2
, SH2/SH3 adaptor crk
, CT-10 related kinase 3
, proto-oncogene c-crk
, v-crk sarcoma virus CT10 oncogene-like protein