IndraLab

"Immunolabeling of ERK1 and ERK2 and total and ERK1/2 Mediated Phosphorylation of RSK1 and MSK1."

"Compounds were assayed for their ability to inhibit the phosphorylation of p90Rsk-1 by ERK2 in HeLa cells."

"Generation of the GTP bound form of Ras initiates a kinase cascade whereby Raf kinases activates MAP kinase kinase (MEK), which activates ERK1 and ERK2, which in turn phosphorylates RSK1 (reviewed in [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"Compounds were assayed for their ability to inhibit the phosphorylation of p90Rsk-1 by ERK2 in HeLa cells."

"Notably, extracellular signal regulated kinase 2 (ERK2) phosphorylates ribosomal S6 kinase 1 (RSK1), which promotes cellular growth."

"Based on in vitro kinase assays using purified proteins we demonstrated that ERK2 phosphorylates both RSK1 and MK2, while p38 and ERK5 are specific to MK2 ( xref )."

"Of these, ERK2 (encoded by the gene MAPK1) was reported to increase the activity and phosphorylation of the oncoprotein RPS6KA1 (ribosomal protein S6 kinase, 90kDa, polypeptide A1), leading to cancer cell proliferation."

"The D319N D-domain mutation attenuated Rsk phosphorylation by ERK2 in KN6 γδTCR + progenitors cultured on ligand-expressing OP9 monolayers ( xref ); however, it did not disrupt the interaction of ERK2 with Egr1, as measured by co-immunoprecipitation ( xref )."

"PKA activity is also regulated by the interaction of other proteins with the regulatory (R) or catalytic (C) subunits of PKA, and a mechanism has been uncovered in which ribosomal S6 kinase (RSK1) interacts with either PKA subunit, depending on whether RSK1 has been phosphorylated and activated by extracellular signal-regulated kinase (ERK)."

"Similarly, SF-3-030 had no apparent effects on ERK2 phosphorylation of the D-domain-containing substrate RSK1 or p38alpha-MAPK-mediated phosphorylation of the F-site-containing ATF2 protein, further supporting selective inhibition of ERK mediated phosphorylation events by SF-3-030 (XREF_FIG)."

No evidence text available

No evidence text available

No evidence text available

No evidence text available

No evidence text available

"Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733."

No evidence text available

No evidence text available

"Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733."

No evidence text available

No evidence text available

No evidence text available

No evidence text available

No evidence text available

"Thus, MAPK1/ERK1 and MAPK2/ERK2 activate three closely related protein kinases known as MAPK_activated protein kinases_1a, _1b and _1c (MAPKAP_K1a/b/c; also known as RSK1/2/3)"

"Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733."

No evidence text available

"Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733."

"Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733."

"In comparison to WT ERK2, an ERK2 mutant that can not bind to DEF-sites was able to phosphorylate RSK1, yet provided reduced phosphorylation of c-Fos and Elk1 in cultured cells [23]."

"Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733."