IndraLab

Statements

PDPK1 is active.
3 14 |
PDPK1 phosphorylated on S241 is active. 5 / 5
3 2 |
biopax:pid
No evidence text available
signor
"In terms of the modulation of PDK1 activity by reversible phosphorylation, five pS sites have been identified on PDK1 in vivo, but only one of these sites, Ser-241 in the activation loop of PDK1, is essential for activity. It seems likely that PDK1 autophosphorylates itself on this residue."
11481331
biopax:pid
No evidence text available
10856237
biopax:pid
No evidence text available
10480933
signor
"Pdk1 is itself phosphorylated in vivo and whether phosphorylation plays a role in regulating its activity/ phosphorylation of ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1"
10455013
PDPK1 phosphorylated on Y373 is active. 3 / 3
3 |
signor
"IGF-1R Directly Interacts with and Phosphorylates PDK1 in Vitro"
20044479
signor
"Src-dependent pdk1 tyr373/376 tyrosine phosphorylation. / optimal activation of pdk1 requires phosphorylation of tyr373/376"
20643654
signor
"Previous studies indicate that optimal activation of PDK1 requires phosphorylation of Tyr373/376 (11, 12, 14, 17), and growth factor receptor activation leads to PDK1 recruitment to the plasma membrane, followed by sequential phosphorylation of Tyr9 and then Tyr373/376"
20643654
PDPK1 phosphorylated on Y376 is active. 3 / 3
3 |
signor
"Src-dependent pdk1 tyr373/376 tyrosine phosphorylation. / optimal activation of pdk1 requires phosphorylation of tyr373/376"
20643654
signor
"We have described that upon ligand binding, igf-1r directly interacts with and phosphorylates pdk1 at tyr373/376"
20044479
signor
"Previous studies indicate that optimal activation of PDK1 requires phosphorylation of Tyr373/376, and growth factor receptor activation leads to PDK1 recruitment to the plasma membrane, followed by sequential phosphorylation of Tyr9 and then Tyr373/376"
20643654
PDPK1 phosphorylated on Y9 is active. 2 / 2
2 |
signor
"Using site-directed mutants, we show that, although phosphorylation on tyr-373/376 is important for pdk1 activity, phosphorylation on tyr-9 has no effect on the activity of the kinase. Both of these residues can be phosphorylated by v-src tyrosine kinase in vitro, and co-expression of v-src leads to tyrosine phosphorylation and activation of pdk1."
11481331
signor
"Ret/ptc (rearranged in transformation/papillary thyroid carcinomas) tyrosine kinase phosphorylates and activates phosphoinositide-dependent kinase 1 (pdk1) ret/ptc phosphorylates a specific tyrosine (y9) residue located in the n-terminal region of pdk1."
12738763
PDPK1 bound to PtsIns(3,4,5)P3 is active. 2 / 2
2 |
signor
"PIP3 recruits PDK1 and AKT to the plasma membrane, where PDK1 phosphorylates AKT on Thr308 in the activation loop of the kinase domain."
19951971
signor
"We tested the kinase in the presence of several inositol phospholipids and found that only low micromolar concentrations of the D enantiomers of either phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) or PtdIns(3,4)P2 were effective in potently activating the kinase, which has been named PtdIns(3,4,5)P3-dependent protein kinase-1 (PDK1)"
9094314
PDPK1 bound to PIK3CG is active. 1 / 1
1 |
signor
"Recent reports have also shown that the phosphoinositide-dependent protein kinase-1 (pdk-1), which binds with high affinity to the pi 3-kinase lipid product phosphatidylinositol-3,4,5-trisphosphate (ptdins-3,4,5-p), phosphorylates and potently activates two other pi 3-kinase targets, the protein kinases akt/pkb and p70s6k."
9768361
Phosphorylated PDPK1 is active. 1 / 1
1 |
signor
"Here, we show that PPP2R2B, encoding the B55² regulatory subunit of the PP2A complex, is epigenetically inactivated by DNA hypermethylation in colorectal cancer. B55²-associated PP2A interacts with PDK1 and modulates its activity toward Myc phosphorylation."
21075311
PDPK1 is inactive.
2 |
PDPK1 bound to PPP2R2B is inactive. 1 / 1
1 |
signor
"Here, we show that PPP2R2B, encoding the B55² regulatory subunit of the PP2A complex, is epigenetically inactivated by DNA hypermethylation in colorectal cancer. B55²-associated PP2A interacts with PDK1 and modulates its activity toward Myc phosphorylation."
21075311
PDPK1 phosphorylated on S241 is inactive. 1 / 1
1 |
signor
"PDK1 kinase activity is negatively regulated by binding to 14-3-3 through the PDK1 autophosphorylation site Ser-241. PDK1 binds to 14-3-3 in vivo and in vitro through the residues surrounding the autophosphorylation site Ser-241 and that the association is achieved only when Ser-241 has been phosphorylated"
12177059