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CCDC88A encodes a member of the Girdin family of coiled-coil domain containing proteins. Additionally we are shipping Coiled-Coil Domain Containing 88A Antibodies (75) and many more products for this protein.
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Study revealed that the downregulation of the expression of Girdin can inhibit the proliferation, invasion and migration of colorectal cancer cells through decrease in proinflammatory cytokine production and inhibition of JAK (show JAK3 ELISA Kits)/STAT (show STAT1 ELISA Kits) signaling.
Girdin may regulate cell processes.
The engulfment of platelets assisted in delaying the aging of endothelial cells via girdin and pgirdin, in which the AKT (show AKT1 ELISA Kits) signal was involved.
Girdin can regulate glycolysis in hepatocellular carcinoma cells through the PI3K (show PIK3CA ELISA Kits)/AKT (show AKT1 ELISA Kits)/HIF-1alpha (show HIF1A ELISA Kits) signaling pathway, which decreases the sensitivity of tumor cells to radiotherapy.
Girdin expression may serve as a useful prognostic factor for invasive breast cancer, especially for the HER2 (show ERBB2 ELISA Kits) subtype.
The present study therefore suggests a role for Girdin as a novel therapeutic target for breast cancer, independent of subtype.
GIV is a bifunctional modulator of G proteins; it serves as a guanine nucleotide dissociation inhibitor (GDI) for Galphas using the same motif that allows it to serve as a guanine-nucleotide exchange factor for Galphai
GIV (Girdin) expression status predicts recurrence risk in patients with T3 pMMR stage II colon cancer.
Results show that high CCDC88A expression in human pancreatic ductal adenocarcinoma (PDAC) tissues is correlated with poor prognosis. Also, the findings suggest that CCDC88A can promote PDAC cell migration and invasion through a signaling pathway that involves phosphorylation/dephosphorylation of many proteins.
Here, theauthors identify GIV/Girdin as a novel effector of AMPK (show PRKAA1 ELISA Kits), whose phosphorylation at a single site is both necessary and sufficient for strengthening mammalian epithelial tight junctions and preserving cell polarity and barrier function in the face of energetic stress.
Tyrosine Phosphorylation of an Actin-Binding Protein (show PFN1 ELISA Kits) Girdin Specifically Marks Tuft Cells in Human and Mouse Gut (show GUSB ELISA Kits)
This study aimed to prove the participation of mTORC2/Akt (show AKT1 ELISA Kits) in F-actin assembling in early-stage cleavage of mouse fertilized eggs via the function of Girdin.
Akt (show AKT1 ELISA Kits)-dependent Girdin phosphorylation regulates repair processes after acute myocardial infarction.
GIV expression is up-regulated in liver after fibrotic injury and is required for hepatic stellate cells activation.Girdin is a central hub for profibrogenic signalling networks during liver fibrosis.
GIV and its substrate Galphai3 (show GNAI3 ELISA Kits) are recruited to active integrin complexes
findings suggest a potential role of Girdin/kinesin-1 interaction in the regulation of neuroblast migration in the postnatal brain
Girdin phosphorylation at Y1798 was found at focal adhesions in NIH3T3 cells. Such phosphorylation was found where migration defects occurred in Girdin KO mice.
Girdin phosphorylation at S1416 induced by Akt (show AKT1 ELISA Kits) is crucial for NMDA receptor activation associated with LTP (show SCP2 ELISA Kits).
Girdin was identified as a new and major regulator of the insulin (show INS ELISA Kits) signal in myoblasts and skeletal muscle.
These results demonstrate that girdin and its phosphorylation play an important role in neonatal vascular development and in pathological neovascularization in the retina.
This gene encodes a member of the Girdin family of coiled-coil domain containing proteins. The encoded protein is an actin-binding protein that is activated by the serine/threonine kinase Akt and plays a role in cytoskeleton remodeling and cell migration. The encoded protein also enhances Akt signaling by mediating phosphoinositide 3-kinase (PI3K)-dependent activation of Akt by growth factor receptor tyrosine kinases and G protein-coupled receptors. Increased expression of this gene and phosphorylation of the encoded protein may play a role in cancer metastasis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
, Hook-related protein 1
, g alpha-interacting vesicle-associated protein
, girders of actin filament
, girders of actin filaments
, Akt-phosphorylation enhancer
, coiled-coil domain-containing protein 88A
, coiled-coil domain containing 88A
, Galpha-interacting vesicle-associated protein