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PDPK1 phosphorylates AKT1 on T308. 54 / 110
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"The results also show that PI3K phosphorylates Akt1 both at Thr308 and Ser473 and Akt2 at Ser474 and that PDK1, a downstream effector of PI3K, phosphorylates Akt1 and Akt2 at Thr308 and Thr309 respectively."

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"Inactivation of GSK-3β Y216 was followed by the phosphorylation of Akt1 T308 by PDK1."

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"PDK1 phosphorylates Akt1 and Akt2 at residues Thr308 and Thr309, respectively."

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"PDK1 phosphorylates Akt1 and Akt2 at residues Thr308 and Thr309, respectively."

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"A straightforward scaffold model predicted the dependence of AKT1 interaction with LASP1 at the cell membrane, potentially in combination with mTORC2, as AKT1 phosphorylation at T308 by PDK1 was not affected ( 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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"PI3k activates phosphatidylinositol 3, 4, 5-triphosphate (PIP3), which triggers phosphoinositide-dependent protein kinase (PDK), promoting protein kinase B (Akt) phosphorylation in threonine 308 and serine 473 residues."

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"AKT1 is usually activated by two different upstream kinases : PDPK1 phosphorylates AKT1 at the T308 residue, while the mTORC2 kinase complex phosphorylates the AKT1-S473 and AKT1-T450 sites."

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"The results show that the physical association of PDK1 with AKT1 induced by reconstituted IFP is sufficient to produce T308 phosphorylation and activation of AKT1 independent of PI3K activation or membrane localization."

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"PDK1 activates Akt by phosphorylating its activation loop (e.g., on residue Thr 308 of AKT1), which initiates a conformational change to the active protein."

sparser
"The phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates AKT1 on Thr308, which is required for AKT activity, but maximal activation of AKT also requires phosphorylation of Ser473 ( xref )."

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"Two phosphorylation events are necessary for maximal activation of Akt, namely phosphorylation at Thr308 and Ser473 in Akt1 (Thr309/Ser474 in Akt2 and Thr305/Ser472 in Akt3) by phosphoinositide-dependent protein kinase 1 (PDK1) and the mechanistic target of rapamycin (mTOR) complex 2 (mTORC2), respectively [ xref , xref ]."

sparser
"AKT1 T308 is phosphorylated by the upstream kinase PDK1."

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"Phosphoinositide-dependent-protein kinase 1 (PDK1) phosphorylates AKT1 at threonine 308, and the second phosphorylation takes place at serine 473 by mTOR complex 2."

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"Akt1 is phosphorylated by PDK1 at T308, and additionally at S473 by the Pl3K related kinases, mammalian target of rapamycin complex 2 (mTORC2) or DNA-PK to achieve its full kinase activity, depending on the stimulus and the cellular context."

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"In contrast, PDK1 phosphorylates Akt1 at Thr308 and Akt2 at Thr309."

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"PDK1 phosphorylates Thr 308 of PKBalpha (homologous phosphorylation sites are Thr 309 in PKBbeta and Thr 305 in PKBgamma), although full activation requires additional phosphorylation of Ser 473 (Ser [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"In contrast, PDK1 phosphorylates Akt1 at Thr308 and Akt2 at Thr309."

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"In contrast, PDK1 (1mug/ml) phosphorylated Akt1 only at Thr308, which was abolished by BX912 (100nM) (XREF_FIG B)."

sparser
"In contrast, PDK1 (1 μg/ml) phosphorylated Akt1 only at Thr308, which was abolished by BX912 (100 nM) ( xref B)."

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"The results also show that PI3K phosphorylates Akt1 both at Thr308 and Ser473 and Akt2 at Ser474 and that PDK1, a downstream effector of PI3K, phosphorylates Akt1 and Akt2 at Thr308 and Thr309 respectively."

sparser
"AKT1 is usually activated by two different upstream kinases: PDPK1 phosphorylates AKT1 at the T308 residue, while the mTORC2 kinase complex phosphorylates the AKT1-S473 and AKT1-T450 sites ( xref , xref )."

sparser
"In the cell-free assay, PI3K phosphorylated Akt1 both at Thr308 and Ser473, but PDK1 phosphorylated Akt1 only at Thr308."

sparser
"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 ]."

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"Membrane-associated Akt1 is phosphorylated by phosphoinositide-dependent kinase-1 (PDK1) and phosphoinositide-dependent kinase-2 (PDK2) at serine 473 and threonine 308, respectively, leading to its ac[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Thr 308 of PKBalpha and Thr 252 of p70 S6 kinase are phosphorylated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) in vitro."

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"The phosphorylation of Akt-1 on Thr 308 and Ser 473 by the PI-dependent kinases PDK1 and PDK2 is also important for the activation of Akt-1 ( Marte and Downward 1997 )."

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"Although both IRS are required for insulin-stimulated PDK1 phosphorylation of AKT1 at Thr308/Thr309 (AKT2), phosphorylation of both Thr308/Thr309 and Ser473 (AKT1)/Ser474 (AKT2) is required for maximal activity of AKT (Figure 1) (13, 76)."

sparser
"Akt1 is phosphorylated by PDK1 at T308, and additionally at S473 by the Pl3K-related kinases, mammalian target of rapamycin complex 2 (mTORC2) or DNA-PK to achieve its full kinase activity, depending on the stimulus and the cellular context ( xref )."

sparser
"PDK1 phosphorylates Akt1 Thr308, activating mTORC1 for protein synthesis, and Akt1 Ser473 phosphorylation by mTORC2 or DNA-PK completes its activation (Akt2, Thr309 and Ser474; Akt3, Thr305 and Ser472) [ xref , xref , xref , xref , xref , xref ]."

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"PDK1 phosphorylates Protein Kinase B (AKT) at residue T308 in the kinase domain, leading to AKT activation."

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"Expressed PDK1 and DSTPK61 phosphorylated Thr308 of PKB alpha only in the presence of Ptdlns (3,4,5) P3 or Ptdlns (3,4) P2."

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"AKT1 is a signaling protein downstream of PI3K; AKT1 is phosphorylated by PDK1 on Thr308 (25) and on Ser473 by MTORC2 (26) (Fig. S3)."

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"In the case of AKT, activated PI3 kinase phosphorylates (activating) the downstream protein PIP 3 -dependent kinase 1 (PDK1), which in turn phosphorylates protein kinase B (AKT) at a threonine 308 residue."

sparser
"Another example of a scaffolding circRNA is circAMOTL1, which binds to pyruvate dehydrogenase kinase 1 (PDK1) and AKT serine/threonine kinase 1 (AKT1), leading to AKT1 phosphorylation at T308 by PDK1 and nuclear translocation, where it exerts antiapoptotic and differentiation functions xref ."

sparser
"This pathway is initiated by receptor tyrosine kinase (RTK) or G-protein coupled receptor activation, like CXCR4, thus inducing phosphorylation of PIP2 to PIP3 by PI3K, thereby recruiting AKT1 and phosphoinositide-dependent kinase (PDK1) to the plasma membrane, where AKT1 is phosphorylated by PDK1 at T308."

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"PDK1 plays a key role in AKT activation by phosphorylating AKT1 at T308 (Alessi et al., 1997; Stokoe et al., 1997)."

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"Active PDPK1 phosphorylates AKT1 (also known as Protein Kinase B) at Thr308."

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"PDK1 (0.5 nM) and AKT1 (60 nM, not yet activated by PDK1 phosphorylation at AKT1 position T308) enzymes were combined in assay buffer supplemented with 6 μ M sonicated lipids (standard lipids, 73.5:24[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"This pathway is initiated by receptor tyrosine kinase (RTK) or G-protein coupled receptor activation, like CXCR4, thus inducing phosphorylation of PIP2 to PIP3 by PI3K, thereby recruiting AKT1 and phosphoinositide-dependent kinase (PDK1) to the plasma membrane, where AKT1 is phosphorylated by PDK1 at T308."

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"This brings both kinases in close vicinity and thereby promotes PDK1 dependent phosphorylation of Akt1 at T308 in the activation loop of the catalytic domain [XREF_BIBR, XREF_BIBR]."

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"PDK1, on the other hand, increased phosphorylation of Akt1 only at Thr308 without affecting Ser473 phosphorylation ( Fig. 1 B)."

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"In this autoinhibited conformation, PDK1 in unable to phosphorylate Thr308 or Ser473 of Akt1."

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"Of note, the detection of macrophages in mouse mammary tumor tissues by flow cytometry revealed that PDK1 deletion significantly inhibited the phosphorylation of protein kinase B (AKT) T308 and S6 in macrophages and suppressed the activation of AKT/mTOR signaling in TAMs."

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"In the canonical PI3K/Akt pathway, phosphoinositide-dependent kinase 1 (PDK1) and Akt are recruited to the inner surface of the cell membrane via the pleckstrin homology (PH) domain where PDK1 initiat[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Active PDPK1 phosphorylates AKT1 (also known as Protein Kinase B) at Thr308."

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"Given that PDK1 specifically phosphorylates Akt1 at the Thr308 residue, and that Thr308 phosphorylation is lower in suicide brain, there is a strong possibility that decreased phosphorylation of Thr308 is due to diminished phosphorylation and activation of PDK1."

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"In general, receptor- or non-receptor tyrosine kinases, PI3K, the 3-phosphoinositide-dependent protein kinase 1 (PDK1) and mTOR complex 2 (mTORC2) can activate Akt by promoting the phosphorylation of Akt1, Akt2 and Akt3 at residues T308/S473, T309/S474 and T305/S472, respectively [83]."

sparser
"In the canonical PI3K/Akt pathway, phosphoinositide-dependent kinase 1 (PDK1) and Akt are recruited to the inner surface of the cell membrane via the pleckstrin homology (PH) domain where PDK1 initiat[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"It has been shown that PI3,4P2 and PI3,4,5P3, interacting with the PH domain of AKT-1/PKB, promote its translocation to the plasma membrane inducing conformational changes and, in parallel, activate P[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"PDK1 phosphorylates Akt1 Thr308, activating mTORC1 for protein synthesis, and Akt1 Ser473 phosphorylation by mTORC2 or DNA-PK completes its activation (Akt2, Thr309 and Ser474; Akt3, Thr305 and Ser472) [[144], [145], [146], [147], [148], [149]]."

sparser
"AKT1 is a signaling protein downstream of PI3K; AKT1 is phosphorylated by PDK1 on Thr308 ( xref ) and on Ser473 by MTORC2 ( xref ) ( xref )."

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"PDK1 phosphorylates Akt1 at T308 in its activation loop (6), while mTORC2 is widely believed to phosphorylate S473 in its hydrophobic motif (7)."

sparser
"AKT1 is recruited to the plasma membrane through the interaction between its pleckstrin homology (PH) domain and PIP3, which leads to AKT1 phosphorylation at T308 by phosphoinositide-dependent protein kinase 1 (PDK1) [ xref ]."