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PDPK1 phosphorylates AKT1. 57 / 61
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"Mechanistically, PDK1 phosphorylates AKT1 in a critical activation site at T308 (T309 in AKT2) in the activation loop of the kinase domain, while mTORC2 phosphorylates AKT on S473 (S474 in AKT2) in the C-terminal hydrophobic motif [XREF_BIBR, XREF_BIBR]."
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"Akt1 is phosphorylated by PDK1, and thereby activated upon translocation to the membrane [22,23] ."
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"The binding of circAmotl1 to 3-phosphoinositide-dependent protein kinase 1 (PDK1) and protein kinase B (AKT1) facilitates the PDK1 dependent phosphorylation of AKT1 [51]."
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"PIP3 generates membrane docking sites for both Phosphotidylinositol Dependent Kinase 1 (PDK1) and for the serine/threonine protein kinase AKT-1 through their pleckstrin homology domains, where PDK1 phosphorylates and activates AKT-1."
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"Akt1, Akt2 and Akt3 were phosphorylated and activated by PDK1 at similar rates and to similar extents."
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"PDK-dependent Akt1 phosphorylation is reversed by protein phosphatase 2A (PP2A) which dephosphorylates pT308 and, to a lesser extent, pS473."
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"The binding of circAmotl1 to 3-phosphoinositide-dependent protein kinase 1 (PDK1) and protein kinase B (AKT1) facilitates the PDK1-dependent phosphorylation of AKT1 [51]."
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"PDK1 then phosphorylates AKT1 at one of its two key sites, T308."
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"PDK1 phosphorylates Akt1 at Thr xref , suggesting that another protein kinase, namely PDK2, is responsible for Ser 473 phosphorylation."
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"For example, circAmotl1 physically binds to 3-phosphoinositide-dependent protein kinase 1 (PDK1) and protein kinase B (AKT1) to promote PDK1-dependent AKT1 phosphorylation."
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"PI3K-independent AKT1 phosphorylation and activation by PDK1."
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"PDK1 and PDK2 phosphorylate AKT (protein kinase B serine/threonine kinase) which in turn inhibits the TSC complex."
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"PIP3 in turn recruits PIP3 dependent kinase (PDK), which phosphorylates and activates the survival kinase, protein kinase B (PKB and Akt) (Alessi et al., 1997; Stokoe et al., 1997)."
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"After phosphoinositide-dependent protein kinase (PDK) phosphorylating Akt-1, glycogen synthase kinase (Gsk) 3β, a serine/threonine kinase, is inhibited (Grimes and Jope, xref ; Hur and Zhou, xref )."
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"Activated α2-Macroglobulin Binding to Cell Surface GRP78 Induces T-Loop Phosphorylation of Akt1 by PDK1 in Association with Raptor."
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"AKT1 is phosphorylated by the PDK1 and by PDK2 [ xref ]."
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"In the classical model of Akt1 regulation, phospholipid PIP3 recruits Akt1 to the plasma membrane (James et al., 1996) where it is acted upon by two protein kinases, mTORC2 and PDK1, which phosphoryla[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Binding of the PH domains of both PDK1 and Akt1 to PIP 3 results in their colocalization at the plasma membrane, where PDK1 can phosphorylate and activate Akt1 ( xref , xref )."
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"In summary, we have employed PCA as a novel tool to characterize AKT1 phosphorylation by PDK1 and provided direct evidence showing stabilized AKT1 association with PDK1 by the reconstituted IFP is sufficient for AKT1 phosphorylation by PDK1 independent of PI3K and membrane localization."
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"Therefore, after phosphorylation of Akt1 by the PDK1 at the membrane, a conformational change occurs ( xref ), and Akt1 detaches from the membrane, leaving less Akt1 on the membrane at the time of observation."
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"Phosphorylation of PI(4,5)P2 to PI(3,4,5)P3 by PI3K activates the PH-domain-containing kinase 3-phosphoinositide dependent protein kinase 1 (PDPK1), which in turn phosphorylates serine/threonine kinase AKT serine/threonine kinase 1 (AKT) [41]."
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"This basal phosphorylation is consistent with our observations that D1 ' has high basal activity relative to the serum stimulated activity level, and that expression of a kinase-inactive PDK1 can decr[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The production of PIP3 drives the recruitment of PDK1 and Akt1 to membranes via their PH domains where Akt1 can be phosphorylated by PDK1 on its activation loop (Thr308) [ xref , xref ]."
30901610
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"Activated α2-macroglobulin binding to cell surface GRP78 induces T-loop phosphorylation of Akt1 by PDK1 in association with Raptor."
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"PIP3 promotes the membrane localization of PDK1 (NM_008960.2) and Akt1 (NM_011062.4), where PDK1 and PDK2 phosphorylate Akt1, resulting in glucose uptake and metabolism."
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"Activated alpha 2 -Macroglobulin Binding to Cell Surface GRP78 Induces T-Loop Phosphorylation of Akt1 by PDK1 in Association with Raptor."
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"In contrast, PDK1 phosphorylates Akt1 at Thr308 and Akt2 at Thr309."
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"Allosteric signals can however be boosted by phosphorylation, as in the case of mammalian target of rapamycin complex 2 (mTORC2) and phosphoinositide-dependent protein kinase 1 (PDK1), which phosphorylate AKT1 on its C terminus (Ser473) and activation loop (Thr308), respectively."
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"The binding of circAmotl1 to 3-phosphoinositide-dependent protein kinase 1 (PDK1) and protein kinase B (AKT1) facilitates the PDK1-dependent phosphorylation of AKT1 [ xref ]."
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"PI3K phosphorylates the membrane phospholipid phosphatidylinositol-4,5-bisphosphate to phosphatidylinositol 3,4,5 trisphosphate, recruiting PDK1 (a Ser/Thr kinase), which can phosphorylate and activate protein kinase B (AKT)."
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"Following its recruitment to the plasma membrane by PIP3, protein kinase B (Akt) is phosphorylated by 3-phosphoinositide-dependent protein kinase 1 (PDK1) [XREF_BIBR, XREF_BIBR]."
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"PIP3 promotes the membrane localization of PDK1 (NM_008960.2) and Akt1 (NM_011062.4), where PDK1 and PDK2 phosphorylate Akt1, resulting in glucose uptake and metabolism."
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"Activation of Akt1 is dependent on recruitment of the protein, through its PH domain [ xref ], to the inner side of the plasma membrane, which causes a conformational change [ xref ], allowing PDK1 to phosphorylate threonine 308 (T308) in Akt1’s catalytic domain and mTORC2 to phosphorylate serine 473 (S473) in Akt1’s regulatory domain [ xref , xref ]."
30355958
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"In contrast, the PIF-binding pocket of PDK1 is not required for the phosphorylation of PKBalpha by PDK1."
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"Phosphorylation of PI(4,5)P2 to PI(3,4,5)P3 by PI3K activates the PH-domain-containing kinase 3-phosphoinositide dependent protein kinase 1 (PDPK1), which in turn phosphorylates serine/threonine kinase AKT serine/threonine kinase 1 (AKT) [41]."
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"Phosphorylation of PI(4,5)P2 to PI(3,4,5)P3 by PI3K activates the PH-domain-containing kinase 3-phosphoinositide dependent protein kinase 1 (PDPK1), which in turn phosphorylates serine/threonine kinase AKT serine/threonine kinase 1 (AKT) [41]."
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"PI3K-independent AKT1 phosphorylation and activation by PDK1."
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"In the classical model of Akt1 regulation, phospholipid PIP3 recruits Akt1 to the plasma membrane ( xref ) where it is acted upon by two protein kinases, mTORC2 and PDK1, which phosphorylate Akt1 on its C-terminus (Ser473) and activation loop (Thr308), respectively ( xref ; xref ; xref )."
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"To install phosphorylation at Thr308, we co-expressed PDK1 and Akt1 while treating cells with phosphatase inhibitor (Fabbro et al., 1999; Kumar et al., 2001) or used recombinant PDK1 to phosphorylate [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"(8) Then PDK1 phosphorylates and activates protein kinase B (PKB), also referred to as Akt."
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"PIP3 generates membrane-docking sites for both Phosphotidylinositol-Dependent Kinase 1 (PDK1) and for the serine/threonine protein kinase AKT-1 through their pleckstrin homology domains, where PDK1 phosphorylates and activates AKT-1 ( xref – xref )."
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"Following its recruitment to the plasma membrane by PIP3, protein kinase B (Akt) is phosphorylated by 3-phosphoinositide-dependent protein kinase 1 (PDK1) [XREF_BIBR, XREF_BIBR]."
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"Therefore, after phosphorylation of Akt1 by the PDK1 at the membrane, a conformational change occurs, and Akt1 detaches from the membrane, leaving less Akt1 on the membrane at the time of observation."
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"Similarly, compared with full length protein, PKBalpha lacking its PH domain is phosphorylated at a 20-fold lower rate by full length PDK1 [40]."
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"Mechanistically, PDK1 phosphorylates AKT1 in a critical activation site at T308 (T309 in AKT2) in the activation loop of the kinase domain, while mTORC2 phosphorylates AKT on S473 (S474 in AKT2) in the C-terminal hydrophobic motif [ xref , xref ]."
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"Upon PI3K activation and/or PTEN inactivation, PDPK1 is recruited to the plasma membrane and phosphorylates AKT1 at threonine 308 (AKT1-T308), thus leading to its activation [XREF_BIBR]."
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"For instance, circ-AMOTL1 functions as a scaffold that facilitates the phosphorylation of AKT1 by PDK1 [ xref ]."
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"In contrast, the PIF-binding pocket of PDK1 is not required for the phosphorylation of PKBalpha by PDK1."
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"Interestingly, images of the co-location studies showed Akt1 and Hsp90 to be co-localized near the membrane-substrate interface when HAX-1 was expressed, in the region where it is known that Akt1 is phosphorylated by the PI3K and PDK1 axis."
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"After phosphoinositide dependent protein kinase (PDK) phosphorylating Akt-1, glycogen synthase kinase (Gsk) 3beta, a serine/threonine kinase, is inhibited."
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"Meanwhile, phosphorylation of C-terminal S477/T479 residues by CDK2/cyclin A2 or mTORC2, together with phosphorylation of S473, synergistically promotes the phosphorylation of Akt1 by PDK1 [81, 89]."
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"It is also known in other biological systems, that Akt1 and SGK can be phosphorylated and activated by the 3-phosphoinositide-dependent protein kinase 1 (PDK1)."
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"Ensemble activity measurements under matched conditions reveal that PDK1 activates AKT1 via a cis mechanism by phosphorylating an AKT1 molecule in the same PDK1:AKT1 heterodimer, while PKCα acts as a competitive inhibitor of this phosphoactivation reaction by displacing AKT1 from PDK1."
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"Akt1 is phosphorylated by PDK1, and thereby activated upon translocation to the membrane [22,23]."
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"In the classical model of Akt1 regulation, phospholipid PIP3 recruits Akt1 to the plasma membrane ( James et al., 1996 ) where it is acted upon by two protein kinases, mTORC2 and PDK1, which phosphory[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"This phosphorylation is quite different from PDK1 phosphorylation of Akt and PKBalpha and p70 S6K1."
10469565
rlimsp
"In summary, we have employed PCA as a novel tool to characterize AKT1 phosphorylation by PDK1 and provided direct evidence showing stabilized AKT1 association with PDK1 by the reconstituted IFP is sufficient for AKT1 phosphorylation by PDK1 independent of PI3K and membrane localization."
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