IndraLab

Statements


ELK1 phosphorylated on S383 is transcriptionally active. 9 / 9
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"Phosphorylation of the C-terminal domain of Elk-1, especially at serine 383, is important for its transactivation activity."

"Indeed, Ser383 plays a vital role, as mutation of Ser383 virtually eliminated hRev7-mediated enhancement of Elk-1 activity (Fig. 4D)."

"Phosphorylation of the C-terminal domain of Elk-1, especially at serine 383, is important for its transactivation activity."

"The NH(2) terminus of MKP-1 was also found to inhibit the activation of the serum response element (SRE) by preventing MAPK-mediated phosphorylation of the regulatory serine 383 residue on Elk-1."

"Elk-1-dependent transactivation is regulated by phosphorylation at serine-383 and -389, and each of the MAPK has been shown to be competent to phosphorylate this nuclear factor at these residues in vitro (33, 34, 35, 36, 37)."

"The NH(2) terminus of MKP-1 was also found to inhibit the activation of the serum response element (SRE) by preventing MAPK-mediated phosphorylation of the regulatory serine 383 residue on Elk-1."

"Subsequent studies with dominant negative Elk-1, wild type, and variant GAL4-Elk-1 fusion proteins confirmed that phosphorylation of Elk-1 at serines 383 and 389 in the C-terminal region of Elk-1 is an important downstream target associated with activation of an SRE by E2."

"Subsequent studies with dominant negative Elk-1, wild type, and variant GAL4-Elk-1 fusion proteins confirmed that phosphorylation of Elk-1 at serines 383 and 389 in the C-terminal region of Elk-1 is an important downstream target associated with activation of an SRE by E2."

"Indeed, Ser383 plays a vital role, as mutation of Ser383 virtually eliminated hRev7-mediated enhancement of Elk-1 activity (Fig. 4D)."