High impact information on Kcnh8

• We show that Net inhibits transcription under basal conditions, in which SAP-1a is inactive and ELK-1 stimulates [1].
• In particular, the FQFP motif of ELK-1 is necessary and sufficient to direct phosphorylation of serine 383, whereas the D-domain directs phosphorylation of other (S/T)P sites in ELK-1 [2].
• RESULTS: At the doses used in the study, both the PFE and the regular pomegranate juice concentrate reduced the activation of ELK-1 and p-CREB and increased eNOS expression (which was decreased by perturbed shear stress) in cultured human endothelial cells and in atherosclerosis-prone areas of hypercholesterolemic mice [3].
• Single exposure of cells to UVC (254 nm for 30 s) or to UVB (300 nm for 10 min) was shown to activate jun-NH2 kinases which, in turn, phosphorylate their substrates ELK-1, c-jun and ATF-2 [4].
• In this communication we report the isolation of cDNAs from the mouse elk1 gene, containing the full coding sequence homologous (87% identical) to the human gene, and the structure and organization of 22 kb of the mouse elk1 locus [5].

Anatomical context of Kcnh8

• Using cDNA microarray, we identified regulators of vascular smooth muscle differentiation in bladder mesenchyme, including serum response factor (SRF) and its cofactors, ELK1 and SRF accessory protein (SAP)1, as well as two SRF-associated pathways, angiotension receptor II and transforming growth factor- beta2 [6].

Enzymatic interactions of Kcnh8

• RESULTS: In mKC, LPS treatment resulted in transient and rapid increase of kinase activity of ERK1/2 that phosphorylated their specific substrate ELK-1, with maximal value at 30 minutes and a return near to baseline within 2 hours, and LPS-induced ERK1/2 activity from LPS concentration of 10 pg/ml to the top activity at 100 ng/ml [7].

References