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PDBsum entry 1h10
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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High resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to ins(1,3,4,5)-tetrakisphophate
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Structure:
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Rac-alpha serine/threonine kinase. Chain: a. Fragment: pleckstrin homology domain, residues 1-123. Synonym: protein kinase b (alpha) pleckstrin homology, rac-pk-alpha, akt1, pkb, rac. Engineered: yes. Other_details: bound to ins(1,3,4,5)-tetrakisphophate, selenomethionine derivative
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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1.40Å
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R-factor:
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0.125
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R-free:
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0.176
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Authors:
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C.C.Thomas,M.Deak,D.R.Alessi,D.M.F.Van Aalten
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Key ref:
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C.C.Thomas
et al.
(2002).
High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol (3,4,5)-trisphosphate.
Curr Biol,
12,
1256-1262.
PubMed id:
DOI:
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Date:
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01-Jul-02
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Release date:
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27-Jun-03
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PROCHECK
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Headers
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References
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P31749
(AKT1_HUMAN) -
RAC-alpha serine/threonine-protein kinase from Homo sapiens
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Seq:
Struc:
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480 a.a.
117 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Curr Biol
12:1256-1262
(2002)
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PubMed id:
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High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol (3,4,5)-trisphosphate.
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C.C.Thomas,
M.Deak,
D.R.Alessi,
D.M.van Aalten.
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ABSTRACT
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The products of PI 3-kinase activation, PtdIns(3,4,5)P3 and its immediate
breakdown product PtdIns(3,4)P2, trigger physiological processes, by interacting
with proteins possessing pleckstrin homology (PH) domains. One of the best
characterized PtdIns(3,4,5)P3/PtdIns(3,4)P2 effector proteins is protein kinase
B (PKB), also known as Akt. PKB possesses a PH domain located at its N terminus,
and this domain binds specifically to PtdIns(3,4,5)P3 and PtdIns(3,4)P2 with
similar affinity. Following activation of PI 3-kinase, PKB is recruited to the
plasma membrane by virtue of its interaction with PtdIns(3,4,5)P3/PtdIns(3,4)P2.
PKB is then activated by the 3-phosphoinositide-dependent pro-tein kinase-1
(PDK1), which like PKB, possesses a PtdIns(3,4,5)P3/PtdIns(3,4)P2 binding PH
domain. Here, we describe the high-resolution crystal structure of the isolated
PH domain of PKB(alpha) in complex with the head group of PtdIns(3,4,5)P3. The
head group has a significantly different orientation and location compared to
other Ins(1,3,4,5)P4 binding PH domains. Mutagenesis of the basic residues that
form ionic interactions with the D3 and D4 phosphate groups reduces or abolishes
the ability of PKB to interact with PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The D5
phosphate faces the solvent and forms no significant interactions with any
residue on the PH domain, and this explains why PKB interacts with similar
affinity with both PtdIns(3,4,5)P3 and PtdIns(3,4)P2.
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Selected figure(s)
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Figure 1.
Figure 1. Structure of PKB[α]PH Complexed to
Ins(1,3,4,5)P[4](A) A ribbon drawing of the
PKB[α]PH-Ins(1,3,4,5)P[4] complex, with the seven β strands
(labeled β1–7) shown in blue and the α helices (labeled
α1–2) shown in red. Ins(1,3,4,5)P[4] is shown as purple
carbons. The side chains of residues interacting with this
molecule are shown as gray carbons. The basic residues thought
to interact with the membrane have their side chains shown as
sticks with green carbons. The negatively charged residues on
VL2 that are hypothesized to interact with the kinase domain are
shown as gray-blue carbons.(B) Ribbon diagrams of the
Ins(1,3,4,5)P[4] binding sites of PKB, GRP1, DAPP1, and BTK. The
Ins(1,3,4,5)P[4] is shown as purple carbons. For the
PKB-Ins(1,3,4,5)P[4] structure, the experimental electron
density map from SOLVE after density modification is shown in
orange (contoured at 2.25σ). Residues that are hydrogen bonding
the ligand are shown as sticks with gray carbons. Hydrogen bonds
are shown as black dotted lines.
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Figure 2.
Figure 2. Charge DistributionElectrostatic surface
potential of PKB[α]PH-Ins(1,3,4,5)P[4] (calculated with GRASP),
with the molecule in the same orientation as in Figure 1. Blue
areas (+6kT) represent highly positively charged residues, and
the red areas (−6kT) represent highly negatively charged
residues. Ins(1,3,4,5)P[4] is shown as a stick model.
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The above figures are
reprinted
by permission from Cell Press:
Curr Biol
(2002,
12,
1256-1262)
copyright 2002.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.F.Rowland,
D.J.Fazakerley,
and
D.E.James
(2011).
Mapping Insulin/GLUT4 Circuitry.
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Traffic,
12,
672-681.
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B.X.Huang,
M.Akbar,
K.Kevala,
and
H.Y.Kim
(2011).
Phosphatidylserine is a critical modulator for Akt activation.
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J Cell Biol,
192,
979-992.
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B.Miao,
I.Skidan,
J.Yang,
A.Lugovskoy,
M.Reibarkh,
K.Long,
T.Brazell,
K.A.Durugkar,
J.Maki,
C.V.Ramana,
B.Schaffhausen,
G.Wagner,
V.Torchilin,
J.Yuan,
and
A.Degterev
(2010).
Small molecule inhibition of phosphatidylinositol-3,4,5-triphosphate (PIP3) binding to pleckstrin homology domains.
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Proc Natl Acad Sci U S A,
107,
20126-20131.
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J.M.Askham,
F.Platt,
P.A.Chambers,
H.Snowden,
C.F.Taylor,
and
M.A.Knowles
(2010).
AKT1 mutations in bladder cancer: identification of a novel oncogenic mutation that can co-operate with E17K.
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Oncogene,
29,
150-155.
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M.Falasca,
D.Chiozzotto,
H.Y.Godage,
M.Mazzoletti,
A.M.Riley,
S.Previdi,
B.V.Potter,
M.Broggini,
and
T.Maffucci
(2010).
A novel inhibitor of the PI3K/Akt pathway based on the structure of inositol 1,3,4,5,6-pentakisphosphate.
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Br J Cancer,
102,
104-114.
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N.Berndt,
H.Yang,
B.Trinczek,
S.Betzi,
Z.Zhang,
B.Wu,
N.J.Lawrence,
M.Pellecchia,
E.Schönbrunn,
J.Q.Cheng,
and
S.M.Sebti
(2010).
The Akt activation inhibitor TCN-P inhibits Akt phosphorylation by binding to the PH domain of Akt and blocking its recruitment to the plasma membrane.
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Cell Death Differ,
17,
1795-1804.
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Q.L.Zhou,
Z.Y.Jiang,
A.S.Mabardy,
C.M.Del Campo,
D.G.Lambright,
J.Holik,
K.E.Fogarty,
J.Straubhaar,
S.Nicoloro,
A.Chawla,
and
M.P.Czech
(2010).
A novel pleckstrin homology domain-containing protein enhances insulin-stimulated Akt phosphorylation and GLUT4 translocation in adipocytes.
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J Biol Chem,
285,
27581-27589.
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T.G.Kutateladze
(2010).
Translation of the phosphoinositide code by PI effectors.
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Nat Chem Biol,
6,
507-513.
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Y.Sei,
Z.Li,
J.Song,
R.Ren-Patterson,
E.M.Tunbridge,
Y.Iizuka,
M.Inoue,
B.T.Alfonso,
S.Beltaifa,
Y.Nakai,
B.S.Kolachana,
J.Chen,
and
D.R.Weinberger
(2010).
Epistatic and functional interactions of catechol-o-methyltransferase (COMT) and AKT1 on neuregulin1-ErbB signaling in cell models.
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PLoS One,
5,
e10789.
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A.Denley,
M.Gymnopoulos,
S.Kang,
C.Mitchell,
and
P.K.Vogt
(2009).
Requirement of phosphatidylinositol(3,4,5)trisphosphate in phosphatidylinositol 3-kinase-induced oncogenic transformation.
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Mol Cancer Res,
7,
1132-1138.
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B.X.Huang,
and
H.Y.Kim
(2009).
Probing Akt-inhibitor interaction by chemical cross-linking and mass spectrometry.
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J Am Soc Mass Spectrom,
20,
1504-1513.
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D.F.Restuccia,
and
B.A.Hemmings
(2009).
Cell signaling. Blocking Akt-ivity.
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Science,
325,
1083-1084.
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I.Rodríguez-Escudero,
A.Andrés-Pons,
R.Pulido,
M.Molina,
and
V.J.Cid
(2009).
Phosphatidylinositol 3-Kinase-dependent Activation of Mammalian Protein Kinase B/Akt in Saccharomyces cerevisiae, an in Vivo Model for the Functional Study of Akt Mutations.
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J Biol Chem,
284,
13373-13383.
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J.Park,
J.Feng,
Y.Li,
O.Hammarsten,
D.P.Brazil,
and
B.A.Hemmings
(2009).
DNA-dependent Protein Kinase-mediated Phosphorylation of Protein Kinase B Requires a Specific Recognition Sequence in the C-terminal Hydrophobic Motif.
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J Biol Chem,
284,
6169-6174.
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L.Du-Cuny,
Z.Song,
S.Moses,
G.Powis,
E.A.Mash,
E.J.Meuillet,
and
S.Zhang
(2009).
Computational modeling of novel inhibitors targeting the Akt pleckstrin homology domain.
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Bioorg Med Chem,
17,
6983-6992.
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M.Guo,
B.X.Huang,
and
H.Y.Kim
(2009).
Conformational changes in Akt1 activation probed by amide hydrogen/deuterium exchange and nano-electrospray ionization mass spectrometry.
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Rapid Commun Mass Spectrom,
23,
1885-1891.
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R.S.Depetris,
J.Wu,
and
S.R.Hubbard
(2009).
Structural and functional studies of the Ras-associating and pleckstrin-homology domains of Grb10 and Grb14.
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Nat Struct Mol Biol,
16,
833-839.
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PDB code:
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S.A.Moses,
M.A.Ali,
S.Zuohe,
L.Du-Cuny,
L.L.Zhou,
R.Lemos,
N.Ihle,
A.G.Skillman,
S.Zhang,
E.A.Mash,
G.Powis,
and
E.J.Meuillet
(2009).
In vitro and in vivo activity of novel small-molecule inhibitors targeting the pleckstrin homology domain of protein kinase B/AKT.
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Cancer Res,
69,
5073-5081.
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V.Calleja,
M.Laguerre,
and
B.Larijani
(2009).
3-D structure and dynamics of protein kinase B-new mechanism for the allosteric regulation of an AGC kinase.
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J Chem Biol,
2,
11-25.
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V.Calleja,
M.Laguerre,
P.J.Parker,
and
B.Larijani
(2009).
Role of a novel PH-kinase domain interface in PKB/Akt regulation: structural mechanism for allosteric inhibition.
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PLoS Biol,
7,
e17.
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C.C.Hernandez,
O.Zaika,
and
M.S.Shapiro
(2008).
A carboxy-terminal inter-helix linker as the site of phosphatidylinositol 4,5-bisphosphate action on Kv7 (M-type) K+ channels.
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J Gen Physiol,
132,
361-381.
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C.Volonté,
N.D'Ambrosi,
and
S.Amadio
(2008).
Protein cooperation: from neurons to networks.
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Prog Neurobiol,
86,
61-71.
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D.Mahadevan,
G.Powis,
E.A.Mash,
B.George,
V.M.Gokhale,
S.Zhang,
K.Shakalya,
L.Du-Cuny,
M.Berggren,
M.A.Ali,
U.Jana,
N.Ihle,
S.Moses,
C.Franklin,
S.Narayan,
N.Shirahatti,
and
E.J.Meuillet
(2008).
Discovery of a novel class of AKT pleckstrin homology domain inhibitors.
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Mol Cancer Ther,
7,
2621-2632.
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G.Li,
A.Rajala,
A.F.Wiechmann,
R.E.Anderson,
and
R.V.Rajala
(2008).
Activation and membrane binding of retinal protein kinase Balpha/Akt1 is regulated through light-dependent generation of phosphoinositides.
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J Neurochem,
107,
1382-1397.
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H.Y.Kim
(2008).
Biochemical and biological functions of docosahexaenoic acid in the nervous system: modulation by ethanol.
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Chem Phys Lipids,
153,
34-46.
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K.D.Swanson,
Y.Tang,
D.F.Ceccarelli,
F.Poy,
J.P.Sliwa,
B.G.Neel,
and
M.J.Eck
(2008).
The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch.
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Mol Cell,
32,
564-575.
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PDB codes:
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N.Kannan,
A.F.Neuwald,
and
S.S.Taylor
(2008).
Analogous regulatory sites within the alphaC-beta4 loop regions of ZAP-70 tyrosine kinase and AGC kinases.
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Biochim Biophys Acta,
1784,
27-32.
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N.R.Leslie,
I.H.Batty,
H.Maccario,
L.Davidson,
and
C.P.Downes
(2008).
Understanding PTEN regulation: PIP2, polarity and protein stability.
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Oncogene,
27,
5464-5476.
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R.X.Guo,
Y.H.Qiao,
Y.Zhou,
L.X.Li,
H.R.Shi,
and
K.S.Chen
(2008).
Increased staining for phosphorylated AKT and nuclear factor-kappaB p65 and their relationship with prognosis in epithelial ovarian cancer.
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Pathol Int,
58,
749-756.
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S.J.Mills,
F.Vandeput,
M.N.Trusselle,
S.T.Safrany,
C.Erneux,
and
B.V.Potter
(2008).
Benzene polyphosphates as tools for cell signalling: inhibition of inositol 1,4,5-trisphosphate 5-phosphatase and interaction with the PH domain of protein kinase Balpha.
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Chembiochem,
9,
1757-1766.
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S.Wang,
and
M.D.Basson
(2008).
Identification of functional domains in AKT responsible for distinct roles of AKT isoforms in pressure-stimulated cancer cell adhesion.
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Exp Cell Res,
314,
286-296.
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W.S.Park,
W.D.Heo,
J.H.Whalen,
N.A.O'Rourke,
H.M.Bryan,
T.Meyer,
and
M.N.Teruel
(2008).
Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging.
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Mol Cell,
30,
381-392.
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W.Wen,
W.Liu,
J.Yan,
and
M.Zhang
(2008).
Structure basis and unconventional lipid membrane binding properties of the PH-C1 tandem of rho kinases.
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J Biol Chem,
283,
26263-26273.
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Y.K.Wang,
W.Chen,
D.Blair,
M.Pu,
Y.Xu,
S.J.Miller,
A.G.Redfield,
T.C.Chiles,
and
M.F.Roberts
(2008).
Insights into the structural specificity of the cytotoxicity of 3-deoxyphosphatidylinositols.
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J Am Chem Soc,
130,
7746-7755.
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B.Ananthanarayanan,
M.Fosbrink,
M.Rahdar,
and
J.Zhang
(2007).
Live-cell molecular analysis of Akt activation reveals roles for activation loop phosphorylation.
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J Biol Chem,
282,
36634-36641.
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B.Dong,
C.A.Valencia,
and
R.Liu
(2007).
Ca(2+)/calmodulin directly interacts with the pleckstrin homology domain of AKT1.
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J Biol Chem,
282,
25131-25140.
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D.F.Ceccarelli,
I.M.Blasutig,
M.Goudreault,
Z.Li,
J.Ruston,
T.Pawson,
and
F.Sicheri
(2007).
Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9.
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| |
J Biol Chem,
282,
13864-13874.
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PDB codes:
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D.Manna,
A.Albanese,
W.S.Park,
and
W.Cho
(2007).
Mechanistic basis of differential cellular responses of phosphatidylinositol 3,4-bisphosphate- and phosphatidylinositol 3,4,5-trisphosphate-binding pleckstrin homology domains.
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J Biol Chem,
282,
32093-32105.
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E.E.Kooijman,
D.P.Tieleman,
C.Testerink,
T.Munnik,
D.T.Rijkers,
K.N.Burger,
and
B.de Kruijff
(2007).
An electrostatic/hydrogen bond switch as the basis for the specific interaction of phosphatidic acid with proteins.
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J Biol Chem,
282,
11356-11364.
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H.Al-Ali,
T.J.Ragan,
X.Gao,
and
T.K.Harris
(2007).
Reconstitution of modular PDK1 functions on trans-splicing of the regulatory PH and catalytic kinase domains.
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Bioconjug Chem,
18,
1294-1302.
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J.D.Carpten,
A.L.Faber,
C.Horn,
G.P.Donoho,
S.L.Briggs,
C.M.Robbins,
G.Hostetter,
S.Boguslawski,
T.Y.Moses,
S.Savage,
M.Uhlik,
A.Lin,
J.Du,
Y.W.Qian,
D.J.Zeckner,
G.Tucker-Kellogg,
J.Touchman,
K.Patel,
S.Mousses,
M.Bittner,
R.Schevitz,
M.H.Lai,
K.L.Blanchard,
and
J.E.Thomas
(2007).
A transforming mutation in the pleckstrin homology domain of AKT1 in cancer.
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Nature,
448,
439-444.
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PDB codes:
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J.J.Falke
(2007).
Membrane Recruitment as a Cancer Mechanism: A Case Study of Akt PH Domain.
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| |
Cellscience,
4,
25-30.
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|
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J.J.Gills,
S.S.Castillo,
C.Zhang,
P.A.Petukhov,
R.M.Memmott,
M.Hollingshead,
N.Warfel,
J.Han,
A.P.Kozikowski,
and
P.A.Dennis
(2007).
Phosphatidylinositol ether lipid analogues that inhibit AKT also independently activate the stress kinase, p38alpha, through MKK3/6-independent and -dependent mechanisms.
|
| |
J Biol Chem,
282,
27020-27029.
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|
|
|
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|
N.Kannan,
N.Haste,
S.S.Taylor,
and
A.F.Neuwald
(2007).
The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module.
|
| |
Proc Natl Acad Sci U S A,
104,
1272-1277.
|
|
|
|
|
|
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V.Calleja,
D.Alcor,
M.Laguerre,
J.Park,
B.Vojnovic,
B.A.Hemmings,
J.Downward,
P.J.Parker,
and
B.Larijani
(2007).
Intramolecular and intermolecular interactions of protein kinase B define its activation in vivo.
|
| |
PLoS Biol,
5,
e95.
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|
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|
|
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|
V.Hietakangas,
and
S.M.Cohen
(2007).
Re-evaluating AKT regulation: role of TOR complex 2 in tissue growth.
|
| |
Genes Dev,
21,
632-637.
|
|
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|
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|
M.F.Arteaga,
L.Wang,
T.Ravid,
M.Hochstrasser,
and
C.M.Canessa
(2006).
An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery.
|
| |
Proc Natl Acad Sci U S A,
103,
11178-11183.
|
|
|
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W.Wen,
J.Yan,
and
M.Zhang
(2006).
Structural characterization of the split pleckstrin homology domain in phospholipase C-gamma1 and its interaction with TRPC3.
|
| |
J Biol Chem,
281,
12060-12068.
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PDB code:
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B.Ananthanarayanan,
Q.Ni,
and
J.Zhang
(2005).
Signal propagation from membrane messengers to nuclear effectors revealed by reporters of phosphoinositide dynamics and Akt activity.
|
| |
Proc Natl Acad Sci U S A,
102,
15081-15086.
|
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C.C.Kumar,
and
V.Madison
(2005).
AKT crystal structure and AKT-specific inhibitors.
|
| |
Oncogene,
24,
7493-7501.
|
|
|
|
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|
C.Edlich,
G.Stier,
B.Simon,
M.Sattler,
and
C.Muhle-Goll
(2005).
Structure and phosphatidylinositol-(3,4)-bisphosphate binding of the C-terminal PH domain of human pleckstrin.
|
| |
Structure,
13,
277-286.
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PDB code:
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G.Song,
G.Ouyang,
and
S.Bao
(2005).
The activation of Akt/PKB signaling pathway and cell survival.
|
| |
J Cell Mol Med,
9,
59-71.
|
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|
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J.Yan,
W.Wen,
W.Xu,
J.F.Long,
M.E.Adams,
S.C.Froehner,
and
M.Zhang
(2005).
Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin.
|
| |
EMBO J,
24,
3985-3995.
|
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PDB codes:
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L.Li,
M.M.Ittmann,
G.Ayala,
M.J.Tsai,
R.J.Amato,
T.M.Wheeler,
B.J.Miles,
D.Kadmon,
and
T.C.Thompson
(2005).
The emerging role of the PI3-K-Akt pathway in prostate cancer progression.
|
| |
Prostate Cancer Prostatic Dis,
8,
108-118.
|
|
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|
|
M.A.Teitell
(2005).
The TCL1 family of oncoproteins: co-activators of transformation.
|
| |
Nat Rev Cancer,
5,
640-648.
|
|
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|
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|
|
M.Akbar,
F.Calderon,
Z.Wen,
and
H.Y.Kim
(2005).
Docosahexaenoic acid: a positive modulator of Akt signaling in neuronal survival.
|
| |
Proc Natl Acad Sci U S A,
102,
10858-10863.
|
|
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M.P.Scheid,
M.Parsons,
and
J.R.Woodgett
(2005).
Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation.
|
| |
Mol Cell Biol,
25,
2347-2363.
|
|
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|
Z.Z.Chong,
F.Li,
and
K.Maiese
(2005).
Oxidative stress in the brain: novel cellular targets that govern survival during neurodegenerative disease.
|
| |
Prog Neurobiol,
75,
207-246.
|
|
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A.Mora,
D.Komander,
D.M.van Aalten,
and
D.R.Alessi
(2004).
PDK1, the master regulator of AGC kinase signal transduction.
|
| |
Semin Cell Dev Biol,
15,
161-170.
|
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|
A.Roy,
and
T.P.Levine
(2004).
Multiple pools of phosphatidylinositol 4-phosphate detected using the pleckstrin homology domain of Osh2p.
|
| |
J Biol Chem,
279,
44683-44689.
|
|
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|
|
D.Auguin,
P.Barthe,
C.Royer,
M.H.Stern,
M.Noguchi,
S.T.Arold,
and
C.Roumestand
(2004).
Structural basis for the co-activation of protein kinase B by T-cell leukemia-1 (TCL1) family proto-oncoproteins.
|
| |
J Biol Chem,
279,
35890-35902.
|
|
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|
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|
|
D.Komander,
A.Fairservice,
M.Deak,
G.S.Kular,
A.R.Prescott,
C.Peter Downes,
S.T.Safrany,
D.R.Alessi,
and
D.M.van Aalten
(2004).
Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates.
|
| |
EMBO J,
23,
3918-3928.
|
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|
PDB codes:
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D.Komander,
M.Deak,
N.Morrice,
and
D.M.van Aalten
(2004).
Purification, crystallization and preliminary X-ray diffraction of a proteolytic fragment of PDK1 containing the pleckstrin homology domain.
|
| |
Acta Crystallogr D Biol Crystallogr,
60,
314-316.
|
|
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|
|
M.Hiromura,
F.Okada,
T.Obata,
D.Auguin,
T.Shibata,
C.Roumestand,
and
M.Noguchi
(2004).
Inhibition of Akt kinase activity by a peptide spanning the betaA strand of the proto-oncogene TCL1.
|
| |
J Biol Chem,
279,
53407-53418.
|
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|
T.C.Cronin,
J.P.DiNitto,
M.P.Czech,
and
D.G.Lambright
(2004).
Structural determinants of phosphoinositide selectivity in splice variants of Grp1 family PH domains.
|
| |
EMBO J,
23,
3711-3720.
|
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PDB codes:
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C.Figueroa,
S.Tarras,
J.Taylor,
and
A.B.Vojtek
(2003).
Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex.
|
| |
J Biol Chem,
278,
47922-47927.
|
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D.J.Powell,
E.Hajduch,
G.Kular,
and
H.S.Hundal
(2003).
Ceramide disables 3-phosphoinositide binding to the pleckstrin homology domain of protein kinase B (PKB)/Akt by a PKCzeta-dependent mechanism.
|
| |
Mol Cell Biol,
23,
7794-7808.
|
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|
|
G.E.Cozier,
D.Bouyoucef,
and
P.J.Cullen
(2003).
Engineering the phosphoinositide-binding profile of a class I pleckstrin homology domain.
|
| |
J Biol Chem,
278,
39489-39496.
|
|
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|
J.Luo,
B.D.Manning,
and
L.C.Cantley
(2003).
Targeting the PI3K-Akt pathway in human cancer: rationale and promise.
|
| |
Cancer Cell,
4,
257-262.
|
|
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|
M.A.Lemmon
(2003).
Phosphoinositide recognition domains.
|
| |
Traffic,
4,
201-213.
|
|
|
|
|
|
|
D.P.Brazil,
J.Park,
and
B.A.Hemmings
(2002).
PKB binding proteins. Getting in on the Akt.
|
| |
Cell,
111,
293-303.
|
|
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|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
