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AKT phosphorylates CDKN1B on T198. 41 / 46
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"Role of AKT in the P4 induced phosphorylation of p27 at T198 and migration enhancement in T47D cells."

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"Fujita et al. found that both Akt and p90 ribosomal protein S6 kinases (RSKs) phosphorylate p27 on Thr198 and this phosphorylation promotes p27 binding to 14-3-3 and its cytoplasmic localization."

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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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"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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"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 can also phosphorylate p27 on Thr198 and promote binding to 14-3-3 in the cytoplasm ( xref ; xref ; xref )."

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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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"The finding that both nuclear relocalization of p27 kip1 and the reduction in T157 and T198 phosphorylation induced by LY294002 was prevented by overexpressing constitutively active AKT in NPA cells i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"AKT, as previously reported, leads to direct phosphorylation of p27 in Thr157 and Thr198 positions."

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"Phosphorylation of p27 at T198 by Akt leads to p27 cytoplasmic mislocalization ( xref )."

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"In general, multiple phosphorylation of p27 in three different locations leads to cytoplasmic localization including: (i)phosphorylation on Ser-10 by Akt, ERK2, CDK5 or hKIS which promotes CRM1-mediat[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"12–14 By phosphorylating p27 kip1 on T157 and T198, AKT induces binding of p27 kip1 to 14.3.3, 48,55 prevents binding to importin-α, 12 impairs nuclear import, 12,55 and overcomes p27 kip1 -induced gr[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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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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"For example, p27 phosphorylation at T157and T198 in the cytoplasm is mediated by AKT that also influences G1 progression [XREF_BIBR, XREF_BIBR, XREF_BIBR]."

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"The finding that both nuclear relocalization of p27 kip1 and the reduction in T157 and T198 phosphorylation induced by LY294002 was prevented by overexpressing constitutively active AKT in NPA cells i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"In the early G1 phase, Thr157 and Thr198 of p27 Kip1 are phosphorylated by Akt, p90RSK1 (p90 ribosomal protein S6 kinases), SGK (serum and glucocorticoid‐inducible kinase), AMPK and PIM (although this phosphorylation is relatively rare), which will prevent the nuclear transfer of p27 Kip1 . xref Moreover, Akt induces phosphorylation of Thr157 and Thr198 to form a recognition motif for 14‐3‐3 protein to prevent nuclear translocation of p27 Kip1 . xref Thus, Akt might also implicate in the nuclear and cytoplasmic distribution of p27 Kip1 ."

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"[92] Interestingly, recent evidence suggests that phosphorylation of p27 (Thr 198) by AKT promotes its association with 14-3-3, which directs it to the cytoplasm where it is degraded."

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"Distribution of p27 Kip1 into cyclin and CDK complexes seems to be affected by phosphorylation of p27 Kip1 at T198, an event that can be mediated by AKT or p90 ribosomal protein S6 kinases (RSK) XREF_BIBR - XREF_BIBR (XREF_FIG)."

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"These results show that H. pylori infection induces AKT and PI3K mediated phosphorylation of p27 at T157 and T198 to cause cytoplasmic p27 mislocalization in gastric cancer, and that p27 mislocalization is an adverse prognostic feature in gastric cancer."

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"Fujita et al. found that both Akt and p90 ribosomal protein S6 kinases (RSKs) phosphorylate p27 on Thr198 and this phosphorylation promotes p27 binding to 14-3-3 and its cytoplasmic localization."

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"AKT, RSK1 and RSK2 can phosphorylate p27 at T198 [ 20 , 52 ], and the cyclin E-CDK2 complex can phosphorylate p27 at T187 [ 50 ]."

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"AKT, RSK1 and RSK2 can phosphorylate p27 at T198 [ 20 , 52 ], and the cyclin E-CDK2 complex can phosphorylate p27 at T187 [ 50 ]."

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"Therefore, our in vitro data clearly support what we observed in vivo on the ability of VEGF-A/PlGF to control vascular leakage.More interestingly, we reported that VEGF-A/PlGF is also able to induce [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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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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"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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"Akt phosphorylates p27on Thr157, while both Akt and Rsk can phosphorylate p27 on Thr198."

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"In the early G1 phase, Thr157 and Thr198 of p27 are phosphorylated by Akt, p90RSK1 (p90 ribosomal protein S6 kinases), SGK (serum and glucocorticoid‐inducible kinase), AMPK and PIM (although this phosphorylation is relatively rare), which will prevent the nuclear transfer of p27 .62 Moreover, Akt induces phosphorylation of Thr157 and Thr198 to form a recognition motif for 14‐3‐3 protein to prevent nuclear translocation of p27 .63 Thus, Akt might also implicate in the nuclear and cytoplasmic distribution of p27 ."

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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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"Depending on the cell type and stimulus condition, RSK, AKT, and/or SGK phosphorylate p27 on Thr198 [XREF_BIBR, XREF_BIBR, XREF_BIBR]."

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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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"Mislocalization of p27 from the nucleus to the cytoplasm has been attributed to the phosphorylation of p27 on T198 by AKT and of T157 by AKT and SGK1 [40,44,45]."

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"The cyclin-dependent kinase 2 (Cdk2)-Cyclin E complex is responsible for phosphorylation of p27 at Thr187 ( Sherr and Roberts, 1999; Lee and Kay, 2007 ), while Akt phosphorylates p27 on Ser10, Thr157,[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"AKT phosphorylates p27 Kip1 at Ser10, Thr157, Thr187, and Thr198 [28] and in every case it is associated with nuclear export of p27 Kip1 ."

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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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"Akt phosphorylates p27 KIP1 not only on Thr 198, but also on Thr 157 [78-80], which creates a binding site for 14-3-3beta, epsilon, gamma, tau and zeta (but not sigma) and leads to cytoplasmic relocal[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."

sparser
"Mislocalization of p27 from the nucleus to the cytoplasm has been attributed to the phosphorylation of p27 on T198 by AKT and of T157 by AKT and SGK1 [ xref , xref , xref ]."

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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]"

sparser
"AKT phosphorylates p27 Kip1 at Ser10, Thr157, Thr187, and Thr198 [28] and in every case it is associated with nuclear export of p27 Kip1 ."

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"AKT and PIM-1 phosphorylate Thr157 and Thr198 of p27 KIP1 and promote the translocation of p27 KIP1 from nucleus to cytoplasm by 14-3-3-binding [ 10 , 14 , 15 ]."

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"AKT and PIM-1 phosphorylate Thr157 and Thr198 of p27 KIP1 and promote the translocation of p27 KIP1 from nucleus to cytoplasm by 14-3-3-binding [ 10 , 14 , 15 ]."