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EXO70H4-dependent trichome cell wall hardening is a unique phenomenon, which may be conserved among a variety of the land plants.
PUB22-mediated degradation of Exo70B2 contributes to the attenuation of PAMP (show ADM Proteins)-induced signaling.
the results identify Exo70 as a novel transcriptional target of HNF4alpha (show HNF4A Proteins) to promote cell cycle progression in hepatoma, thus provide a basis for the development of therapeutic strategies for hepatocellular carcinoma.
the expression of CTTN (show CTTN Proteins), Exo70 and MMP-9 (show MMP9 Proteins) in HCC (show FAM126A Proteins) cells was detected and their relations with the ability of migration and invasion of hepatoma carcinoma cells were evaluated
GIV directly and constitutively binds the exocyst complex subunit Exo-70 and also associates with GLUT4 (show SLC2A4 Proteins)-storage vesicles (GSVs) exclusively upon insulin (show INS Proteins) stimulation.
We show that Exo70, a component of the exocyst complex, undergoes isoform switching mediated by ESRP1 (show ESRP1 Proteins), a pre-mRNA splicing factor (show SNRPB Proteins) that regulates epithelial mesenchymal transition.
Exo70 thus represents a membrane-bending protein that may couple actin dynamics and plasma membrane remodeling for morphogenesis.
Exo70 is involved in caveolin-1 (show CAV1 Proteins) recycling to the plasma membrane during re-adhesion of the cells to the substratum.
Exocyst component Exo70 is a direct substrate of the extracellular signal-regulated kinases 1/2, their phosphorylation enhances the binding of Exo70 to other exocyst components and promotes the assembly of the exocyst complex.
PIPKIgamma and phosphatidyl inositol phosphate pools at nascent E-cadherin (show CDH1 Proteins) contacts cue Exo70 targeting and orient the tethering of exocyst-associated E-cadherin (show CDH1 Proteins)
BIG2 and Exo70 interact in trans-Golgi network and centrosomes, as well as in exocyst structures or complexes that move along microtubules to the plasma membrane.
The exocyst complex is required for targeting of Glut4 (show SLC2A4 Proteins) to the plasma membrane by insulin (show INS Proteins)
Exo70 mediates AMPA (show GRIA3 Proteins) receptor insertion at the postsynaptic membrane, but it does not participate in receptor targeting.
Given the low level of sequence conservation within Exo70, this structure provides new insights into our understanding of many species-specific functions of the exocyst
Results show that Snapin (show SNAPIN Proteins) interacts with the exocyst Exo70 and plays a modulatory role in GLUT4 (show SLC2A4 Proteins) vesicle trafficking.
fusion of GLUT4 (show SLC2A4 Proteins) vesicles is the rate-limiting step regulated by insulin (show INS Proteins) downstream of Exo70-mediated tethering
The protein encoded by this gene is a component of the exocyst complex. The exocyst complex plays a critical role in vesicular trafficking and the secretory pathway by targeting post-Golgi vesicles to the plasma membrane. The encoded protein is required for assembly of the exocyst complex and docking of the complex to the plasma membrane. The encoded protein may also play a role in pre-mRNA splicing through interactions with pre-mRNA-processing factor 19. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome 4.
, exocyst complex component 7
, Exocyst complex component 7
, exocyst complex component Exo70
, exocyst component protein 70 kDa homolog