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Statements


AKT phosphorylates MAP3K5 on S83. 44 / 45
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rlimsp
"As shown in Figure 5A (top and left), Akt phosphorylates wild-type ASK1 at Ser-83 but does not phosphorylate mutant ASK1 (R89W)."

reach
"PIM1 and Akt directly phosphorylate Ask1 at Ser83, which decreases its ability to phosphorylate and activate its substrates, JNK and p38."

reach
"It has been shown that SIRT1 activates Akt, which in turn can phosphorylate ASK1 at Ser 83 to maintain ASK1 in an inactive form XREF_BIBR."

rlimsp
"The N-terminal domain of ASK1 containing the Akt phosphorylation site (pSer83) associates with Akt in resting state."

sparser
"Furthermore, AKT phosphorylation of apoptosis signal-regulating kinase 1 (ASK1) on Ser-83 was reduced by DPI and siNox4RNAs."

reach
"Akt phosphorylates apoptosis signaling kinase 1 (ASK-1) at Ser 83, which attenuates ASK-1 activity and promotes cell survival, as ASK-1 transduces stress signals to the pro apoptotic jun NH2-terminal [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"The apoptosis signal-regulating kinase 1 (Ask1) is phosphorylated by Akt at serine 83, leading to its inhibition and a reduced activation of JNK, which under certain circumstances can promote apoptosis ( xref )."

rlimsp
"Akt and apoptosis signal-regulating kinase 1 (ASK1) were physically associated, and E2 induced the phosphorylation of ASK1 at serine-83, which is a consensus Akt phosphorylation site. We confirmed a previous report showing that paclitaxel induces cell damage via the ASK1-c-Jun N-terminal protein kinase (JNK) cascade. E2 inhibited the paclitaxel-induced JNK activation, and the E2-induced inhibition of the paclitaxel-induced JNK activation was attenuated in cells treated with either ICI182,780 or LY294002 or transfected with ASK1S83A, in which a consensus Akt phosphorylation site at serine-83 was converted to alanine."

reach
"Moreover, Akt phosphorylates the apoptosis signalregulating kinase 1 (ASK1) at S83, leading to cell survival and inhibition of apoptosis [XREF_BIBR]."

reach
"Incidentally, Akt phosphorylates ASK-1 (on S83) as part of its pro survival functions, thus keeping the latter 's activation in check [XREF_BIBR - XREF_BIBR, XREF_BIBR, XREF_BIBR]."

sparser
"As shown in xref (top and left), Akt phosphorylates wild-type ASK1 at Ser-83 but does not phosphorylate mutant ASK1 (R89W)."

reach
"Furthermore, AKT phosphorylation of apoptosis signal regulating kinase 1 (ASK1) on Ser 83 was reduced by DPI and siNox4RNAs."

sparser
"AKT phosphorylates Ser83 of ASK1 which also leads to inhibition of ASK1-induce apoptosis."

sparser
"Interestingly, phosphorylation of human ASK1 Ser83 by Akt is thought to attenuate Ask1 activity and inhibit apoptosis ( xref ; xref )."

reach
"It has been reported that Akt can phosphorylate ASK1 on Ser83, which results in the inhibition of apoptosis induced by ASK1."

sparser
"Moreover, the phosphorylation of Ask-1 at Ser 83 by Akt suppress Ask-1 activity and Ask-1 mediated apoptosis xref , xref ."

reach
"Thus phosphorylation of ASK1 at Ser 83 by Akt or PIM1 maintains ASK1 in an inactive state and suppresses ASK1 mediated p38 and JNK downstream signaling."

rlimsp
"Apoptosis signal-regulating kinase 1 (ASK1) has been reported to be phosphorylated by Akt at serine 83 (Ser83) and its activity reduced (15−17)."

No evidence text available

sparser
"It has been shown that SIRT1 activates Akt, which in turn can phosphorylate ASK1 at Ser-83 to maintain ASK1 in an inactive form xref ."

rlimsp
"Akt decreased ASK1 kinase activity stimulated by both oxidative stress and overexpression in 293 cells by phosphorylating a consensus Akt site at serine 83 of ASK1."

reach
"Phosphorylation of ASK1 Ser83 by AKT attenuates ASK1 kinase activity."

sparser
"For instance, Zhang et al. reported that AKT can phosphorylate ASK1 at site Ser83 to inhibit hydrogen peroxide-induced ASK1/p38 signaling activation in endothelial cells xref ."

reach
"Crosstalk between these two pathways can occur via Akt dependent phosphorylation of ASK1 on Ser83, suppressing ASK1 activity."

sparser
"Phosphorylation of ASK1 Ser83 by AKT attenuates ASK1 kinase activity ( xref )."

sparser
"Crosstalk between these two pathways can occur via Akt-dependent phosphorylation of ASK1 on Ser83, suppressing ASK1 activity ( xref )."

rlimsp
"It has been reported that Akt can phosphorylate ASK1 on Ser83 and inactivates the apoptotic function of ASK1, leading to the enhancement of cell survival (15)."

reach
"Moreover, the phosphorylation of Ask-1 at Ser 83 by Akt suppress Ask-1 activity and Ask-1 mediated apoptosis XREF_BIBR, XREF_BIBR."

No evidence text available

reach
"For instance, Zhang et al. reported that AKT can phosphorylate ASK1 at site Ser83 to inhibit hydrogen peroxide induced ASK1 and p38 signaling activation in endothelial cells XREF_BIBR."

sparser
"One major mechanism by which this antiapoptotic effect is mediated is phosphorylation of Ser 83 of apoptosis signal-regulating kinase 1 (ASK1) by Akt, rendering this pro-apoptotic kinase inactive [ xref ]."

sparser
"Phosphorylation of ASK1 on Ser83 by AKT kinase ( xref ) and de-phosphorylation of Ser845 by protein phosphatase 5 ( xref ) decreases ASK1 activity."

sparser
"It is known that the inhibition of Akt induces an activation of p38 and JNK, whereas active Akt directly phosphorylates ASK1 Ser83, which leads to apoptosis inhibition [ xref ]."

sparser
"It has been reported that Akt can phosphorylate ASK1 on Ser83, which results in the inhibition of apoptosis induced by ASK1 (Kim et al., xref )."

"AKT phosphorylates and inhibits apoptosis signal-regulating kinase 1 (ASK1) at Ser83, thereby promoting cell survival (Yuan et al., 2003; Zhang et al., 2005; Wu et al., 2006)."

reach
"As shown in XREF_FIG (top and left), Akt phosphorylates wild-type ASK1 at Ser 83 but does not phosphorylate mutant ASK1 (R89W)."

reach
"The activated Akt on one hand phosphorylates Ask-1 at the Ser 83 site to inhibit its activation, and on the other hand it phosphorylates FoxO."

reach
"Interestingly, phosphorylation of human ASK1 Ser83 by Akt is thought to attenuate Ask1 activity and inhibit apoptosis (Kim et al., 2001; Zhang et al., 2005)."

reach
"It is known that the inhibition of Akt induces an activation of p38 and JNK, whereas active Akt directly phosphorylates ASK1 Ser83, which leads to apoptosis inhibition [XREF_BIBR]."

rlimsp
"Furthermore, AKT phosphorylation of apoptosis signal-regulating kinase 1 (ASK1) on Ser-83 was reduced by DPI and siNox4RNAs."

rlimsp
"For instance, Zhang et al. reported that AKT can phosphorylate ASK1 at site Ser83 to inhibit hydrogen peroxide-induced ASK1/p38 signaling activation in endothelial cells [52]."

rlimsp
"Akt and apoptosis signal-regulating kinase 1 (ASK1) were physically associated, and E2 induced the phosphorylation of ASK1 at serine-83, which is a consensus Akt phosphorylation site."

"Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1 akt decreased ask1 kinase activity stimulated by both oxidative stress and overexpression in 293 cells by phosphorylating a consensus akt site at serine 83 of ask1."

reach
"AKT phosphorylates Ser83 of ASK1 which also leads to inhibition of ASK1-induce apoptosis."