IndraLab

Statements

AKT phosphorylates MAP3K5 on S83. 10 / 45
1 1 2 | 17 14 9
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
reach
"PIM1 and Akt directly phosphorylate Ask1 at Ser83, which decreases its ability to phosphorylate and activate its substrates, JNK and p38."
25749412
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."
24410795
rlimsp
"The N-terminal domain of ASK1 containing the Akt phosphorylation site (pSer83) associates with Akt in resting state."
15782121
sparser
"Furthermore, AKT phosphorylation of apoptosis signal-regulating kinase 1 (ASK1) on Ser-83 was reduced by DPI and siNox4RNAs."
16532036
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
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
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
"Moreover, Akt phosphorylates the apoptosis signalregulating kinase 1 (ASK1) at S83, leading to cell survival and inhibition of apoptosis [XREF_BIBR]."
26025205
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]."
21785723
AKT phosphorylates MAP3K5. 10 / 34
| 1 19 11 1
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."
24410795
sparser
"An important role for Akt in forestalling apoptosis has been shown in the case of poliovirus, where the Akt phosphorylation of Ask1 limits the activity of its downstream effector Jnk1 and thereby decreases apoptotic signals."
22340720
reach
"Through the pancreatic cancer cell line PANC-1, Mochizuki group reveals that inhibition of AKT phosphorylation of ASK1 alone was sufficient in inducing apoptosis."
22581366
reach
"Ling et al previously demonstrated that CHI3L1 stimulation in human skin fibroblasts or articular chondrocytes resulted in protein kinase B (Akt)-mediated serine/threonine phosphorylation of the apoptosis signal-regulator kinase, ASK1, suggesting that CHI3L1 elicits anti-catabolic and anti-apoptotic response during tissue remodeling and destruction [XREF_BIBR]."
21546314
sparser
"Another substrate of Akt is the apoptosis signal-regulating kinase 1 (ASK1); Akt phosphorylation of ASK1 prevents apoptosis induced by serum deprivation ( Kim et al., 2001b )."
12646285
sparser
"Apoptosis signal-regulating kinase 1 (ASK1) also activates the p38 MAPK cascade, but Hsp90-Akt phosphorylates ASK1 and inhibits ASK1-mediated apoptosis xref ."
23650580
sparser
"In summary, phosphorylation of Ask1 by Akt promotes survival, perhaps by keeping JNK at low levels and thus avoiding JNK-induced apoptosis, and by producing moderate levels of phospho-p38."
36353511
sparser
"Indole 1 also inhibited AKT-mediated mTOR phosphorylation in a time dependent manner as well as the anti-apoptotic factor Bcl-2 and AKT-dependent phosphorylation of ASK1, while pro-apoptotic proteins like p53 and p21 were up-regulated."
23272910
reach
"At intermediary cascade level, Akt is able to phosphorylate and inhibit the activity of ASK1 and MLK3 that belong to the MAPKKK upstream activation of JNK, and the final effect is the decrease of ASK1- and MLK3 mediated cell death [XREF_BIBR, XREF_BIBR]."
23670595
reach
"Studies show that AKT and PKB negatively regulates the phosphorylation and activation of JNK by directly phosphorylating apoptosis signal regulating kinase 1 (ASK1) and JNK interacting protein 1 (JIP1) [XREF_BIBR, XREF_BIBR]."
27657053
AKT phosphorylates MAP3K5 on T838. 3 / 3
| 1 1 1
rlimsp
"Given the results that we obtained in siRNA ASK1 (Figure 3C) that p38 phosphorylation was almost completely inhibited by siRNA ASK1, we propose that Akt may phosphorylate ASK1 at Thr838 first, followed by p38 phosphorylation."
20112989
reach
"Moreover, it has been reported that ASK1 can be phosphorylated at Thr838 directly by Akt kinases to prompt cell apoptosis."
28335665
sparser
"Moreover, it has been reported that ASK1 can be phosphorylated at Thr838 directly by Akt kinases to prompt cell apoptosis. xref By Western blot, we observed a pronounced activation of Akt in MDCK cells exposed to COM crystals ( xref )."
28335665
Kinase-active AKT phosphorylates MAP3K5 on S83. 2 / 2
1 1 |
bel
"11154276;14500571"
15212693
bel
"11154276;14500571"
15212693
AKT phosphorylates MAP3K5 on serine. 1 / 1
| 1
reach
"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 (Kim et al, 2001)."
15150572
AKT phosphorylates MAP3K5-R89W. 1 / 1
| 1
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
AKT phosphorylates MAP3K5 at position 83. 1 / 1
| 1
reach
"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 (Kim et al, 2001)."
15150572