IndraLab

Statements

AKT phosphorylates CDKN1B. 10 / 192
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"The accumulation of cytoplasmic Akt-phosphorylated p27 correlates with tumor aggressiveness [38–40] ."
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"P27 KIP1 phosphorylation by PKB and Akt leads to poor breast cancer prognosis."
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"Constitutive activation of PKB and Abl or Src family kinases in cancers would drive p27 phosphorylation, increase cyclin D1-Cdk4 assembly and activation, and reduce the cyclin E-Cdk2 inhibitory function of p27."
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"Similarly, Akt inhibition by MK2206 inhibited FOXO phosphorylation and mTORC1 activity and elevated p27 expression (XREF_FIG)."
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"PKB/Akt phosphorylates p27, impairs nuclear import of p27 and opposes p27-mediated G1 arrest."
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"In earlier studies we demonstrated that human Treg treated with TLR2 ligands lose their suppressive capacity, which is based on a restoration of Akt phosphorylation and downregulation of the cdk inhibitor p27 Kip1 [ xref , xref ]."
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"AMPK-directed phosphorylation of p27 is associated with p27’s function toward autophagy [ xref ] whereas phosphorylation of p27 by Akt mediates cell survival [ xref ]."
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"Western blot revealed that down-regulation of PHLPP2 abolished the anti-miR-27a mediated regulation of Akt phosphorylation and modulation of the cell cycle regulators p21, p27 and CyclinD1 (Figs.  xref , xref )."
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"Studies reported that activated Akt induces phosphorylation of p21 Cip/WAF1 (or cyclin dependent kinase interacting protein-1, CDKI-1) and p27 Kip1 (or cyclin dependent kinase inhibitor-1B, CDKI-1B) [ xref , xref ]."
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"The activated Akt phosphorylates and prevents nuclear localization of p27, blocking inhibition of cell cycle."
19843243
AKT phosphorylates CDKN1B on T157. 10 / 84
1 1 3 | 44 30 4
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"While phosphorylation on Thr187 by Cdk2 and cyclin E complexes is essential for its ubiquitination and degradation, p27 is also phosphorylated by PKB and AKT on Thr157 in HCC, inducing its relocalization to the cytoplasm and impairing its negative effect on nuclear Cdk and cyclin complexes (XREF_FIG) [XREF_BIBR, XREF_BIBR]."
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"Separately, AKT phosphorylates p27 at Thr157 thus relocates p27 to the cytoplasm."
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"TRIP6 regulates the membrane translocation and activation of AKT and facilitates AKT mediated recognition and phosphorylation of p27 (KIP1) specifically at T157, thereby promoting the cytosolic mislocalization of p27 (KIP1)."
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"Noting that the growth inhibitory (nuclear) function of p27 is required for EGFR-TKI efficacy, IGF1R activation causes resistance to EGFR-TKIs, the IGF1R is a potent activator of Akt, and Akt phosphorylates p27 at T157 with resultant cytoplasmic sequestration of p27 and cell cycle progression, we evaluated regulation of p27 by EGFR-TKIs in an OSCC cell line in the presence or absence of simultaneous IGF1R activation."
23106397
signor
"Mtor may promote g1 progression in part through sgk1 activation and deregulate the cell cycle in cancers through both akt- and sgk-mediated p27 t157 phosphorylation and cytoplasmic p27 mislocalization."
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"We found that PP2A-B56gamma3 can counterbalance Akt phosphorylation of p27 at Thr157, and we previously showed B56gamma3 containing PP2A directly interacts with p27 and dephosphorylates p27 at Thr187 [XREF_BIBR]."
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"AKT can phosphorylate p27 on threonine 157 (p27 kip1Thr-157), suppressing nuclear import and subsequent p27 driven G 1 arrest [XREF_BIBR]; hence, confocal microscopy was used to detect nuclear p27."
23075476
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"Separately, AKT phosphorylates p27 at Thr157 thus relocates p27 to the cytoplasm."
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"Thr157 phosphorylation of p27 by cytoplasmic Akt, which prevents p27 binding to importin alpha and thus nucleus re-entry, appears itself to depend on prior Ser10 phosphorylation of p27 required for its nuclear export [XREF_BIBR]."
17092340
bel
"It is known that Akt phosphorylates Thr 157 of p27 and this reduces the nuclear import activity of p27. Using a pull-down experiment, 14-3-3 was identified as the Thr157-phosphorylated p27NLS-binding protein Although importin alpha5 bound to Thr157-phosphorylated p27NLS, 14-3-3 competed with importin alpha5 for binding to it. Thus, 14-3-3 sequestered phosphorylated p27NLS from importin alpha binding, resulting in cytoplasmic localization of NLS-phosphorylated p27. "
15057270
AKT phosphorylates CDKN1B on T198. 10 / 26
1 | 19 5 1
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"Incomplete regulation of pS 10 p27 Kip1 by JNK activity might be possible presumably due to combinatory involvement of other molecules like Akt and/or KIS.In addition to phosphorylation of Ser10, phos[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Work by several laboratories convincingly showed that phosphorylation of p27 by AKT at T157 and also at T198 is required for nucleo cytoplasmic transport [XREF_BIBR - XREF_BIBR]."
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"Less common and not well understood is the phosphorylation of p27 Kip1 at Thr 157 and Thr 198 by Akt, p90-S6 kinases, AMPK, and PIM, that impairs its nuclear import resulting in cytoplasmic localization."
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"Incomplete regulation of pS 10 p27 Kip1 by JNK activity might be possible presumably due to combinatory involvement of other molecules like Akt and/or KIS.In addition to phosphorylation of Ser10, phos[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"AKT phosphorylates the CDK inhibitor p27 on T198 and thereby inactivates p27 by preventing its localization to the nucleus ( xref ; xref )."
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"At least three PI3K effectors (AKT, SGK and RSK) contribute to T157 and T198 phosphorylation of p27, which impairs import of monomeric p27 and increases p27-cyclin D-CDK4 assembly."
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"Akt can also phosphorylate p27 on Thr198 and promote binding to 14-3-3 in the cytoplasm."
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"Akt acts downstream of PI3K to phosphorylate p27 at T157 and T198, leading to impaired nuclear p27 import, p27 accumulation in the cytoplasm, and loss of cyclin E-Cdk2 inhibition (Viglietto et al., 20[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Thus, mTOR mediated AKT and SGK activation promote p27 phosphorylation at T157 and T198, impairing p27 nuclear import and driving cellular proliferation and migration."
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"In conclusion, this study provides evidence that P4 induced RSK1 activation mediated by the cSrc and AKT signaling pathway, subsequently causing phosphorylation of p27 at T198, which in turn increased formation of the p27 and RhoA complex and RhoA activation, and finally enhanced migration in breast cancer cells."
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AKT phosphorylates CDKN1B on S10. 10 / 21
1 1 | 9 5 4
rlimsp
"Activation of RalBP1 leads to cytoplasmic accumulation of p27 by a mechanism that requires phosphorylation of Ser-10 on p27 by Akt."
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"His Akt phosphorylated p27 at S10 as determined by phospho specific S10 antibody and the reaction was inhibited by an Akt inhibitor."
16780593
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"Previous reports and the current study suggest that p27 Kip1 is phosphorylated at Ser10 by Akt, KIS [21,23,30] , or JNK (this study and [20] )."
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"AKT phosphorylates p27 at multiple residues including S10, T157, and T198, which mediates p27 stability and/or localization depending on the cellular context."
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"PKB then phosphorylates p27 Kip1 at ser10 and thr157."
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"Akt directly binds to and phosphorylates p27 Kip1 at three residues, Ser10, Thr187, and Thr198 [XREF_BIBR - XREF_BIBR]."
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rlimsp
"The results (Figure 9) demonstrate that both inhibitors abrogate the Ral-mediated effects, suggesting that the mechanisms by which RalBP1 induces Ser-10 phosphorylation on p27 and its accumulation in the cytoplasm proceeds via activation of Akt."
23576547
rlimsp
"Our results reveal a delicate balance between the RalBP1 pathway, which mediates p27 translocation to the cytoplasm and requires p27 phosphorylation at Ser-10 by Akt, and the PLD1 pathway, which is independent of Ser-10 phosphorylation and supports nuclear localization of p27."
23576547
signor
"Identification of p27kip1phosphorylation sites revealed that akt phosphorylated p27kip1at ser10(fig.4). Therefore, akt might participate in nuclear export of p27kip1as well as p27kip1degradation. Moreover, akt might be one of the unidentified ser10kinases."
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"Phosphorylation of p27 at S10 is mediated by AKT, KIS, CDK5 and CDK16 kinases whereas T187 phosphorylation is mediated by CDK2."
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AKT phosphorylates CDKN1B on threonine. 5 / 5
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"The nuclear localisation signal of p27 contains an AKT consensus site at threonine 157, and phosphorylation of this threonine residue on p27 by AKT inhibits p27 's import to the nucleus."
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"The nuclear localisation signal of p27 contains an AKT consensus site at threonine 157, and phosphorylation of this threonine residue on p27 by AKT inhibits p27's import to the nucleus."
25965299
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"Although Akt also phosphorylated p27(Kip1) at Ser(10) and Thr(187), these two sites were not involved in the binding to 14-3-3 proteins."
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"XREF_BIBR Akt directly phosphorylates p27 on multiple Threonine (T) residues, including T198, which have been shown to promote nuclear export and sequestration of p27 in the cytoplasm, resulting in the inactivation of the protein in human cells."
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"Although Akt also phosphorylated p27 (Kip1) at Ser (10) and Thr (187), these two sites were not involved in the binding to 14-3-3 proteins."
12042314
AKT phosphorylates CDKN1B on serine. 3 / 3
| 1 2
trips
"Although Akt also phosphorylated p27(Kip1) at Ser(10) and Thr(187), these two sites were not involved in the binding to 14-3-3 proteins."
12042314
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"In both cases we found that Akt phosphorylates p27 at serine 10."
16780593
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"Although Akt also phosphorylated p27 (Kip1) at Ser (10) and Thr (187), these two sites were not involved in the binding to 14-3-3 proteins."
12042314
Kinase-active AKT leads to the phosphorylation of CDKN1B on S10. 2 / 2
2 |
bel
"Although Akt also phosphorylated p27(Kip1) at Ser(10) and Thr(187), these two sites were not involved in the binding to 14-3-3 proteins."
12042314
bel
"Further analysis revealed that 14-3-3 proteins bound to p27(Kip1) through Thr(198) only when it was phosphorylated by Akt. Although Akt also phosphorylated p27(Kip1) at Ser(10) and Thr(187), these two sites were not involved in the binding to 14-3-3 proteins. p27(Kip1) phosphorylated at Thr(198) exists only in the cytoplasm"
12042314
AKT phosphorylates CDKN1B on T187. 1 / 2
| 1
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"Akt directly binds to and phosphorylates p27 Kip1 at three residues, Ser10, Thr187, and Thr198 [XREF_BIBR - XREF_BIBR]."
22481935
Kinase-active AKT leads to the phosphorylation of CDKN1B on T187. 2 / 2
2 |
bel
"Further analysis revealed that 14-3-3 proteins bound to p27(Kip1) through Thr(198) only when it was phosphorylated by Akt. Although Akt also phosphorylated p27(Kip1) at Ser(10) and Thr(187), these two sites were not involved in the binding to 14-3-3 proteins. p27(Kip1) phosphorylated at Thr(198) exists only in the cytoplasm"
12042314
bel
"Although Akt also phosphorylated p27(Kip1) at Ser(10) and Thr(187), these two sites were not involved in the binding to 14-3-3 proteins."
12042314
AKT phosphorylates CDKN1B at position 10. 1 / 1
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"In both cases we found that Akt phosphorylates p27 at serine 10."
16780593
Phosphorylated AKT leads to the phosphorylation of CDKN1B on S10. 1 / 1
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"Additionally, the HCC827-TM4SF5 clones not only enhanced and sustained EGFR and Akt phosphorylation but also enhanced TM4SF5 expression and p27 Kip1 Ser10 phosphorylation, which is known to cause its [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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Phosphorylated AKT phosphorylates CDKN1B. 1 / 1
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"P27 kip1 is one of the substrates of Akt and is phosphorylated by p-Akt XREF_BIBR."
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Active AKT phosphorylates CDKN1B. 1 / 1
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trips
"As the cyclin-dependent kinase (CDK) inhibitor p27(Kip1) (p27) is usually not expressed in ALCL, we hypothesized that activated Akt (pAkt) phosphorylates p27 resulting in increased p27 proteolysis and cell cycle progression."
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Kinase-active AKT leads to the phosphorylation of CDKN1B. 1 / 1
1 |
bel
"Modified assertion"
12042314
Kinase-active AKT phosphorylates CDKN1B on T198. 1 / 1
1 |
bel
"12042314;14504289"
15212693
Kinase-active AKT phosphorylates CDKN1B on serine. 1 / 1
1 |
bel
"The identification of p21Waf1/Cip1 and p27Kip1 as novel substrates of PKB provided new insights into mechanisms whereby hyperactivation of this lipid signaling pathway may lead to cell cycle deregulation in human cancers"
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Kinase-active AKT phosphorylates CDKN1B on T157. 1 / 1
1 |
bel
"PhosphoElm data from PMID 15212693"
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AKT phosphorylates CDKN1B-T157A. 1 / 1
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"Active (myristoylated) Akt phosphorylated wild-type p27 in vivo but was unable to phosphorylate a T157A p27 mutant."
12244301