IndraLab

No evidence text available

No evidence text available

No evidence text available

No evidence text available

No evidence text available

"Co-expression of DUSP6 abrogated phosphorylation of wild-type ERK2, kinase impaired ERK2 (ERK2 K54R), ERK2 R191H and endogenous ERK2 (XREF_FIG)."

"This reduced expression is associated with constitutive activation of MAPK1 and ERK2 and, despite the presence of mutated KRAS, exogenous overexpression of DUSP6 induces dephosphorylation of MAPK1 and ERK2, subsequent suppression of proliferation, and eventual apoptosis of pancreatic cancer cells."

"Co-expression of DUSP6 abrogated phosphorylation of wild-type ERK2, kinase impaired ERK2 (ERK2 K54R), ERK2 R191H, and endogenous ERK2."

"Mkp3 inhibits MAPK cascade by dephosphorylating ERK2 [49]."

"33 MKP3 attenuates the FGF cascade by dephosphorylating ERK1 and ERK2, molecules important for MAPK downstream signaling."

"Co-expression of DUSP6 abrogated phosphorylation of wild-type ERK2, kinase impaired ERK2 (ERK2 K54R), ERK2 R191H, and endogenous ERK2."

"Co-expression of DUSP6 abrogated phosphorylation of wild-type ERK2, kinase impaired ERK2 (ERK2 K54R), ERK2 R191H and endogenous ERK2 (XREF_FIG)."

"Eleven different protein phosphatases, many previously suggested to be involved in ERK2 regulation, were compared, including tyrosine-specific phosphatases (PTP1B, CD45, and HePTP), dual specificity MAPK phosphatases (VHR, MKP3, and MKP5), and Ser/Thr protein phosphatases (PP1, PP2A, PP2B, PP2C alpha, and lambda PP). The results provide biochemical evidence that protein phosphatases display exquisite specificity in their substrate recognition and implicate HePTP, MKP3, and PP2A as ERK2 phosphatases. The results provide biochemical evidence that protein phosphatases display exquisite specificity in their substrate recognition and implicate HePTP, MKP3, and PP2A as ERK2 phosphatases. "