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DUSP6 dephosphorylates MAPK1. 40 / 44
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"DUSP1 is known to dephosphorylate ERK1, while DUSP6 dephosphorylates ERK1 and ERK2, rendering them inactive."

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"Interestingly, it has been demonstrated that FGF/FGFR signaling pathways are strongly regulated by feedback mechanisms: SPRoutY (SPRY), which is induced by FGF, down-regulates the activation of Growth[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"ERK2 dephosphorylation by MKP3 has been shown to proceed by a mechanism whereby MKP3 binds to ERK2 and pTpY and dephosphorylates ERK2/pY first, then dissociates and releases the monophosphorylated ERK[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"The dephosphorylation of ERK2 by the dedicated phosphatase MKP3 goes through the intermediate ERK2/T ∗ Y, with chemistry on the phosphotyrosine occurring first ( 43,44 )."

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"The type II, DFG-out ERK2 inhibitor decreased the rate of dephosphorylation of ERK2 by MKP3, whereas type I DFG-in inhibitors enhanced dephosphorylation ( xref )."

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"The same study demonstrated that recombinant ERK2 can induce catalytic activation of DUSP6, and DUSP6 expression can de-phosphorylate a co-expressed ERK2 construct and block the MEK1 driven activation of GAL4-ELK1, an ERK1/2 regulated transcription factor."

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"As a result, compared to that of controls, the overexpression of DUSP6 significantly decreased the phosphorylation of ERK2, and inhibited the secreted viral protein level (p27) in the culture supernatants (Figure 5A)."

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"On the contrary, the knockdown of DUSP6 by si-RNA significantly enhanced the phosphorylation of ERK2 (Figure 5D)."

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"This observation is consistent with ERK2 dephosphorylation by the cytoplasmic MKP-3."

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"ERK2 dephosphorylation by MKP3 has been shown to proceed by a mechanism whereby MKP3 binds to ERK2/pTpY and dephosphorylates ERK2/pY first, then dissociates and releases the monophosphorylated ERK2/pT[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Phosphorylation of Erk2 by the MAP kinase kinase Mek is distributive (22,23) , as is dephosphorylation of Erk2 by the phosphatase MKP3 (30) ."

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"MKP3 acts to dephosphorylate ERK1 and ERK2 to attenuate MAPK signalling [40] ."

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"D2 mouse carries p.Met62Ile in Dusp6, which reduces the binding of Dusp6 to Erk2 and subsequently increases Erk1/Erk2 phosphorylation."

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"Expression of LINC01503 in ESCC cell lines reduced ERK2 dephosphorylation by DUSP6, leading to activation of ERK signaling via MAPK."

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"Phosphorylation of ERK2 at the T185 and Y187 in the TEY (codon 185–187) motif results in ~6-fold increased affinity of its common docking motif to DUSP6 , which in turn dephosphorylates ERK2 in a stepwise manner ."

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"It is known that ERK2 binds and promotes the phosphatase activity of DUSP6 , which in turn dephosphorylates ERK2."

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"On the other hand, when active MAPK1 was dephosphorylated by the exogenous expression of DUSP6, promoter activity was reduced."

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"Both ERK1 and ERK2 are dephosphorylated and inactivated by dual specificity phosphatase 6 ( DUSP6 ) ( Muda et al., 1998 )."

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"Phosphorylation of Erk2 by the MAP kinase kinase Mek is distributive (22,23) , as is dephosphorylation of Erk2 by the phosphatase MKP3 (30) ."

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"DUSP1 is known to dephosphorylate ERK1, while DUSP6 dephosphorylates ERK1 and ERK2, rendering them inactive."

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"Erk2 is phosphorylated on its two activating sites by Mek and dephosphorylated by MKP3, both of which are known to be distributive, as mentioned above."

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"We note that MKP-3 preferentially dephosphorylates ERK2, and in addition to the resolved structures of the catalytic domain and BD, a structure of ERK2 complexed with the kinase interaction motif from MKP-3 BD has been determined [ xref ]."

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"We reasoned that if MKP3 dephosphorylates the bisphosphorylated ERK2 via a distributive mechanism, monophosphorylated ERK2 should be formed in excess of the MKP3 concentration in the reaction mixture."

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"Furthermore, MKP3 is capable of efficiently dephosphorylating both the pTyr and the pThr on ERK2."

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"The dephosphorylation of ERK2 by the dedicated phosphatase MKP3 goes through the intermediate ERK2/T ∗ Y, with chemistry on the phosphotyrosine occurring first ( 43,44 )."

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"Thus, the molecular basis for efficient dual dephosphorylation of ERK2 and pTpY by MKP3 may lie in the specific interactions between ERK2 and MKP3 that are not possible between nonspecific substrates [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"We note that MKP-3 preferentially dephosphorylates ERK2, and in addition to the resolved structures of the catalytic domain and BD, a structure of ERK2 complexed with the kinase interaction motif from MKP-3 BD has been determined [XREF_BIBR]."

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"Importantly, LINC01503 bound directly to ERK2 and prevented the dephosphorylation of ERK2 by DUSP-6."

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"Our results also suggest that MKP3 can dephosphorylate ERK2 in cells in the absence of its N-terminal MAPK binding domain."

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"Nevertheless, MKP3 full length displayed more efficiency in the dephosphorylation of ERK2 than MKP3 153-381, in agreement with the notion that the N-terminal MAPK binding domain plays a major role in [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"We find that ERK2 and pTpY dephosphorylation by MKP3 involves an ordered, distributive mechanism in which MKP3 binds the bisphosphorylated ERK2 and pTpY, dephosphorylates Tyr (P) first, dissociates and releases the monophosphorylated ERK2/pT, which is then subjected to dephosphorylation by a second MKP3, yielding the fully dephosphorylated ERK2."

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"Recombinant Dusp6 completely dephosphorylated pERK2 in vitro as determined by immunoblotting with pERK specific antibodies ( xref , lane 3 )."

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"Our results also suggest that MKP3 can dephosphorylate ERK2 in cells in the absence of its N-terminal MAPK-binding domain."

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"Importantly, LINC01503 bound directly to ERK2 and prevented the dephosphorylation of ERK2 by DUSP-6."

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"In the Fgf/Mapk pathway, the phosphatases Dusp4 and Dusp6 can dephosphorylate the kinases Mapk1 and Mapk3, which are necessary for Dusp4 and Dusp6 expression ( Li et al., 2007; Niwa et al., 2007; Wahl[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"In addition to the mechanism of ERK2 dephosphorylation by MKP3, we also investigated the molecular basis of MKP3 substrate specificity."

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"The dephosphorylation of ERK2 MAPK by Pyst1 (MKP-3) in mammalian cells is accompanied by the formation of a tight physical complex between the phosphatase and ERK2 [10]."

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"Silencing of DUSP6 significantly promoted the phosphorylation of MAPK1 (Figure 6C and Figure S4B,C)."

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"When expressed in COS-7 cells, MKP-3 blocks both the phosphorylation and enzymatic activation of ERK2 by mitogens."

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"MIN6 cells were infected with recombinant adenovirus encoding mitogen-activated protein kinase phosphatase 3 (MKP3), a dual-specific phosphatase that dephosphorylates the activation loop of Erk1/Erk2 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"