Coiled-Coil Domain Containing 88A (CCDC88A) ELISA Kits

Human Coiled-Coil Domain Containing 88A (CCDC88A) interaction partners

1. Cytoplasmic and nuclear girdin exhibited different roles in prognosis of breast cancer: cytoplasmic girdin expression was an independent prognostic factor for progression-free survival (PFS), whereas nuclear girdin expression was an independent prognostic factor for overall survival (OS).

2. Results showed a role of Girdin in the collective invasion of skin cancer cells, where it interacts with beta-catenin. Also, Girdin is indispensable for stable cell-cell interaction, supracellular cytoskeletal organization, and the collective migration of cancer.

3. 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/STAT signaling.

4. Girdin may regulate cell processes.

5. The engulfment of platelets assisted in delaying the aging of endothelial cells via girdin and pgirdin, in which the AKT signal was involved.

6. Girdin can regulate glycolysis in hepatocellular carcinoma cells through the PI3K/AKT/HIF-1alpha signaling pathway, which decreases the sensitivity of tumor cells to radiotherapy.

7. Girdin expression may serve as a useful prognostic factor for invasive breast cancer, especially for the HER2 subtype.

8. The present study therefore suggests a role for Girdin as a novel therapeutic target for breast cancer, independent of subtype.

9. 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

10. GIV (Girdin) expression status predicts recurrence risk in patients with T3 pMMR stage II colon cancer.

11. 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.

12. Here, theauthors identify GIV/Girdin as a novel effector of AMPK, 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.

13. On the basis of the differential prognostic impact of tGIV/pYGIV within each molecular subtype, we propose a diagnostic algorithm

14. Results show that Girdin is important for formation and function of invadopodia enhanced by Dlg5-silencing in hepatocellular carcinoma cells.

15. Tyrosine Phosphorylation of an Actin-Binding Protein Girdin Specifically Marks Tuft Cells in Human and Mouse Gut

16. Overexpression of girdin is associated with invasion of hepatocellular carcinoma.

17. Heterotrimeric G protein signaling via GIV/Girdin is a ubiquitous mechanism in health and disease, and can be a target for molecular therapies. (Review)

18. miR-101 inhibits cell proliferation, migration and invasion in hepatocellular carcinoma through downregulating Girdin.

19. Phosphorylation of GIV at Tyr-1764/Tyr-1798 is also required to enhance PI3K-Akt signaling and tumor cell migration in response to integrin stimulation, indicating that GIV functions in Tyr(P)-dependent integrin signaling.

20. CCDC88A is essential for multiple aspects of normal development and loss of CCDC88A is a cause of the PEHO syndrome phenotype.

Mouse (Murine) Coiled-Coil Domain Containing 88A (CCDC88A) interaction partners

1. Tyrosine Phosphorylation of an Actin-Binding Protein Girdin Specifically Marks Tuft Cells in Human and Mouse Gut

2. This study aimed to prove the participation of mTORC2/Akt in F-actin assembling in early-stage cleavage of mouse fertilized eggs via the function of Girdin.

3. Akt-dependent Girdin phosphorylation regulates repair processes after acute myocardial infarction.

4. 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.

5. GIV and its substrate Galphai3 are recruited to active integrin complexes

6. findings suggest a potential role of Girdin/kinesin-1 interaction in the regulation of neuroblast migration in the postnatal brain

7. Girdin phosphorylation at Y1798 was found at focal adhesions in NIH3T3 cells. Such phosphorylation was found where migration defects occurred in Girdin KO mice.

8. Girdin phosphorylation at S1416 induced by Akt is crucial for NMDA receptor activation associated with LTP.

9. Girdin was identified as a new and major regulator of the insulin signal in myoblasts and skeletal muscle.

10. These results demonstrate that girdin and its phosphorylation play an important role in neonatal vascular development and in pathological neovascularization in the retina.

11. these findings indicate that loss of Girdin in the nestin cell lineage underlies the phenotype of Girdin ncKO mice.

12. Girdin regulates cell movement in biological contexts that require directional cell movement

13. Girdin and its Akt-mediated phosphorylation have major roles in the migration and proliferation of vascular smooth muscle cells and vascular remodeling.

14. A structural determinant that renders G alpha(i) sensitive to activation by GIV/girdin is required to promote cell migration.

15. HkRP1 (A430106J12Rik) is involved in the process of tubulation of sorting nexin-1 positive membranes from early endosome subdomains.

16. the Akt/Girdin signalling pathway is essential in VEGF-mediated postneonatal angiogenesis

17. Girdin has an important role in tumor progression with aberrant activation of the Akt signaling pathway

18. Girdin as an intrinsic factor in postnatal development of the dentate gyrus and provide insights into the critical role of the DISC1/girdin interaction in postnatal neurogenesis in the dentate gyrus.