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AKT phosphorylates MAP3K5 on S83. 67 / 68
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"Furthermore, AKT phosphorylation of apoptosis signal regulating kinase 1 (ASK1) on Ser 83 was reduced by DPI and siNox4RNAs."
16532036
sparser
"AKT phosphorylates ASK1 on Ser83 and this results in the inhibition of apoptosis induced by ASK1 [87] ."
16899408
rlimsp
"It was also noted that ROR1 overexpression significantly maintained ASK1 phosphorylation at serine 83, which is known to be phosphorylated by AKT and inhibits ASK1 function,19 even in the presence of hydrogen peroxide."
26661061
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 ."
24410795
rlimsp
"A previous study has shown that Akt interacts with ASK1 and negatively regulates ASK1 by phosphorylating ASK1 on Ser-83 residue (Kim et al., 2001)."
15998799
rlimsp
"AKT phosphorylates Ser83 of ASK1 which also leads to inhibition of ASK1-induce apoptosis."
19749799
reach
"It has been reported that AKT activation phosphorylates ASK1 at Ser83 and thus inactivates ASK1 signaling leading to inhibition of apoptosis ( Misra et al., 2006 )."
29444456
rlimsp
"Furthermore, AKT phosphorylation of apoptosis signal-regulating kinase 1 (ASK1) on Ser-83 was reduced by DPI and siNox4RNAs."
16532036
rlimsp
"Furthermore, a marked phosphorylation at Ser-83 of ASK1 (a specific Akt phosphorylation site) was present in Resv-treated keratinocytes indicating that Akt can inactivate ASK1 via SIRT1 pathway (Fig. 9B)."
24410795
sparser
"Akt phosphorylates ASK1 at Ser83 and thus inhibits it."
35563860
rlimsp
"It has been shown that SIRT1 activates Akt, which in turn can phosphorylate ASK1 at Ser-83 to maintain ASK1 in an inactive form [25]."
24410795
rlimsp
"Similarly, ASK1 has been reported to be phosphorylated by AKT at serine 83, which reduces its activity (37,38)."
31059045
sparser
"Furthermore, AKT phosphorylation of apoptosis signal-regulating kinase 1 (ASK1) on Ser-83 was reduced by DPI and siNox4RNAs."
16532036
sparser
"Crosstalk between these two pathways can occur via Akt-dependent phosphorylation of ASK1 on Ser83, suppressing ASK1 activity ( xref )."
19052195
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 )."
15150572
sparser
"Phosphorylation of ASK1 Ser83 by AKT attenuates ASK1 kinase activity ( xref )."
19749799
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]"
22960641
rlimsp
"It has been reported that Akt can phosphorylate ASK1 on Ser83, which results in the inhibition of apoptosis induced by ASK1 (Kim et al., 2001)."
30026697
reach
"AKT phosphorylates ASK1 on Ser83 and this results in the inhibition of apoptosis induced by ASK1 [87] ."
16899408
sparser
"10 AKT can phosphorylate ASK1 on Ser83 and inactivates the apoptotic function of ASK1, leading to the enhancement of cell survival."
24308997
rlimsp
"On the MAP3K level, phosphorylation of ASK1 at Ser 83 by AKT reduced JNK activity in response to oxidative stress and serum starvation, and decreased ASK1 dependent apoptosis in HEK 293 and L929 cells (Kim et al., 2001)."
23060802
reach
"Akt phosphorylates ASK1 at Ser83 and thus inhibits it."
35563860
rlimsp
"As shown in Figure 5A (top and left), Akt phosphorylates wild-type ASK1 at Ser-83 but does not phosphorylate mutant ASK1 (R89W)."
26912789
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."
11154276
reach
"As shown in XREF_FIG (top and left), Akt phosphorylates wild-type ASK1 at Ser 83 but does not phosphorylate mutant ASK1 (R89W)."
26912789
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"(3) Akt phosphorylates apoptosis signal-regulating kinase 1 (ASK1) on Ser83 and this results in the inhibition of apoptosis induced by ASK1 [170] ."
22261329
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"10 AKT can phosphorylate ASK1 on Ser83 and inactivates the apoptotic function of ASK1, leading to the enhancement of cell survival."
24308997
sparser
"Interestingly, phosphorylation of human ASK1 Ser83 by Akt is thought to attenuate Ask1 activity and inhibit apoptosis ( xref ; xref )."
36353511
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."
14500571
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."
14500571
reach
"Phosphorylation of ASK1 Ser83 by AKT attenuates ASK1 kinase activity."
19749799
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."
20182516
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"PIM1 and Akt directly phosphorylate Ask1 at Ser83, which decreases its ability to phosphorylate and activate its substrates, JNK and p38."
25749412
rlimsp
"A previous study also revealed that Akt negatively regulates ASK1 by phosphorylating Ser-83 residue (Kim et al., 2001) and preventing oligomerization (unpublished data)."
15998799
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]."
22194952
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"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."
24410795
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"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."
26912789
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]."
28367274
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 )."
30026697
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)."
20112989
rlimsp
"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 [49]."
28367274
sparser
"As shown in xref (top and left), Akt phosphorylates wild-type ASK1 at Ser-83 but does not phosphorylate mutant ASK1 (R89W)."
26912789
rlimsp
"Phosphorylation of ASK1 Ser83 by AKT attenuates ASK1 kinase activity (Kim et al., 2001)."
19749799
signor
"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."
11154276
sparser
"For example, PRMT5 symmetrically dimethylates ASK1 (apoptosis signal-regulating kinase 1) at the arginine 89 residue, thereby promoting the interaction between ASK1 and Akt and phosphorylating ASK1 at the serine 83 residue to negatively regulate its activity xref ."
38418849
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"Through the PubMed database, it showed that AKT could directly regulate the protein phosphorylated residues of p27 (Thr187) ( Fujita et al., 2002 ), BAD (Ser112) ( Liu et al., 2012 ), BAD (Ser136) ( D[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28651161
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"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]."
21785723
bel
"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)."
18794886
rlimsp
"The inhibitory effect of Hsp90 on ASK1-p38 activities is diminished when the Akt phosphorylation site on ASK1 (pSer83) is absent or when Akt is genetically deleted in cells, suggesting that Hsp90 and Akt function together to inhibit ASK1-p38 signaling."
15782121
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"AKT phosphorylates Ser83 of ASK1 which also leads to inhibition of ASK1-induce apoptosis."
19749799
reach
"Crosstalk between these two pathways can occur via Akt dependent phosphorylation of ASK1 on Ser83, suppressing ASK1 activity."
19052195
rlimsp
"The N-terminal domain of ASK1 containing the Akt phosphorylation site (pSer83) associates with Akt in resting state."
15782121
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)."
36353511
reach
"It has been reported that Akt can phosphorylate ASK1 on Ser83, which results in the inhibition of apoptosis induced by ASK1."
30026697
phosphoelm
No evidence text available
11154276
phosphoelm
No evidence text available
14500571
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 ]."
22583868
reach
"Moreover, Akt phosphorylates the apoptosis signalregulating kinase 1 (ASK1) at S83, leading to cell survival and inhibition of apoptosis [XREF_BIBR]."
26025205
sparser
"AKT phosphorylates Ser83 of ASK1 which also leads to inhibition of ASK1-induce apoptosis."
19749799
rlimsp
"Exposure of INS‐1 β‐cells transfected with human ASK1 to thapsigargin was found to increase phosphorylation of Thr845 and reduce phosphorylation of Ser83 in ASK1, changes that increase its enzyme activity, resulting in phosphorylation and activation of p38 MAPK and JNK, through MAPK/extracellular signal‐regulated kinase (ERK) kinase (Mek) 3/6 and Mek 4/7, respectively. Activation of PKB with GIP treatment prevented these changes in ASK1 phosphorylation and downstream targets. Suppressing ASK1 activation with GIP treatment inhibited apoptosis induced by all apoptosis‐inducing agents tested. As a result of the complexity of the system, the mechanism of GIP action is currently only open to speculation. In non‐stressed cells, ASK1 forms a high molecular weight complex that has been termed the ‘ASK1 signalosome’, and, in non‐stressed cells when ASK1 activity is inhibited, the anti‐oxidative protein, thioredoxin (Trx), is a component of the signalosome. If the oxidative state of the cell is greatly increased, the oxidized form of Trx dissociates from ASK1 and tumor necrosis factor (TNF) receptor‐associated factor 2 (TRAF2) and TRAF6 binding activates ASK1 signaling. Although GIP‐stimulated phosphorylation of Ser83 by Akt was clearly involved in inhibiting ASK1 activity, it is also possible that the binding of thioredoxin and/or TRAF2/6 to ASK1 were impacted on."
24843552
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 ."
22194952
sparser
"Phosphorylation of ASK1 on Ser83 by AKT kinase ( xref ) and de-phosphorylation of Ser845 by protein phosphatase 5 ( xref ) decreases ASK1 activity."
19749799
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)."
20112989
sparser
"Moreover, the phosphorylation of Ask-1 at Ser 83 by Akt suppress Ask-1 activity and Ask-1 mediated apoptosis xref , xref ."
20182516
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 ]."
28367274
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."
22194952
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."
20182516