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Keywords: pleckstrin homology domain
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Articles

Identification and characterization of pleckstrin-homology-domain-dependent and isoenzyme-specific Akt inhibitors

Stanley F. BARNETT, Deborah DEFEO-JONES, Sheng FU, Paula J. HANCOCK, Kathleen M. HASKELL, Raymond E. JONES, Jason A. KAHANA, Astrid M. KRAL, Karen LEANDER, Ling L. LEE, John MALINOWSKI, Elizabeth M. McAVOY, Debbie D. NAHAS, Ronald G. ROBINSON, Hans E. HUBER
Journal: Biochemical Journal
Biochem J (2005) 385 (2): 399–408.
https://doi.org/10.1042/BJ20041140
Published: 07 January 2005
... the second compound (Akt-I-1,2) inhibited both Akt1 and Akt2 with IC 50 values of 2.7 and 21 μM respectively. Neither compound inhibited Akt3 nor mutants lacking the PH (pleckstrin homology) domain at concentrations up to 250 μM. These compounds were reversible inhibitors, and exhibited a linear mixed-type...
View articletitled, Identification and characterization of pleckstrin-homology-domain-dependent and isoenzyme-specific Akt inhibitors
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Articles

Inositol phospholipids regulate the guanine-nucleotide-exchange factor Tiam1 by facilitating its binding to the plasma membrane and regulating GDP/GTP exchange on Rac1

Ian N. FLEMING, Ian H. BATTY, Alan R. PRESCOTT, Alex GRAY, Gursant S. KULAR, Hazel STEWART, C. Peter DOWNES
Journal: Biochemical Journal
Biochem J (2004) 382 (3): 857–865.
https://doi.org/10.1042/BJ20040916
Published: 07 September 2004
...Ian N. FLEMING; Ian H. BATTY; Alan R. PRESCOTT; Alex GRAY; Gursant S. KULAR; Hazel STEWART; C. Peter DOWNES Binding of the Rac1-specific guanine-nucleotide-exchange factor, Tiam1, to the plasma membrane requires the N-terminal pleckstrin homology domain. In the present study, we show that membrane...
View articletitled, Inositol phospholipids regulate the guanine-nucleotide-exchange factor Tiam1 by facilitating its binding to the plasma membrane and regulating GDP/GTP exchange on Rac1
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Articles

The plasma membrane translocation of diacylglycerol kinase δ1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain

Shin-ichi IMAI, Masahiro KAI, Keiko YAMADA, Hideo KANOH, Fumio SAKANE
Journal: Biochemical Journal
Biochem J (2004) 382 (3): 957–966.
https://doi.org/10.1042/BJ20040681
Published: 07 September 2004
...Shin-ichi IMAI; Masahiro KAI; Keiko YAMADA; Hideo KANOH; Fumio SAKANE DGK (diacylglycerol kinase) regulates the concentration of two bioactive lipids, diacylglycerol and phosphatidic acid. DGKδ1 or its PH (pleckstrin homology) domain alone has been shown to be translocated to the plasma membrane...
View articletitled, The plasma membrane translocation of diacylglycerol kinase δ1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain
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Articles

Single-cell imaging of graded Ins(1,4,5)P3 production following G-protein-coupled-receptor activation

Mark S. NASH, Kenneth W. YOUNG, Gary B. WILLARS, R. A. John CHALLISS, Stefan R. NAHORSKI
Journal: Biochemical Journal
Biochem J (2001) 356 (1): 137–142.
https://doi.org/10.1042/bj3560137
Published: 08 May 2001
...Mark S. NASH; Kenneth W. YOUNG; Gary B. WILLARS; R. A. John CHALLISS; Stefan R. NAHORSKI The pleckstrin homology domain of phospholipase Cδ1 (PH PLCδ ) binds Ins(1,4,5) P 3 and PtdIns(4,5) P 2 specifically, and can be used to detect changes in Ins(1,4,5) P 3 in single cells. A fusion construct...
View articletitled, Single-cell imaging of graded Ins(1,4,5)P3 production following G-protein-coupled-receptor activation
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Articles

Phosphatidylinositol transfer proteins and protein kinase C make separate but non-interacting contributions to the phosphorylation state necessary for secretory competence in rat mast cells

Jef A. PINXTEREN, Bastien D. GOMPERTS, Danise ROGERS, Scott E. PHILLIPS, Peter E. R. TATHAM, Geraint M. H. THOMAS
Journal: Biochemical Journal
Biochem J (2001) 356 (1): 287–296.
https://doi.org/10.1042/bj3560287
Published: 08 May 2001
... to phosphoinositide headgroups, and by a PH (pleckstrin homology) domain polypeptide that binds phosphoinositides. The apparent displacement of neomycin by exogenous PITPs suggests that these proteins screen essential lipids. Secretion from run-down cells is also inhibited by 1- O -hexadecyl-2- O -methyl- rac...
View articletitled, Phosphatidylinositol transfer proteins and protein kinase C make separate but non-interacting contributions to the phosphorylation state necessary for secretory competence in rat mast cells
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Articles

Membrane recruitment of DOCK180 by binding to PtdIns(3,4,5)P3

Shin KOBAYASHI, Toshiyuki SHIRAI, Etsuko KIYOKAWA, Naoki MOCHIZUKI, Michiyuki MATSUDA, Yasuhisa FUKUI
Journal: Biochemical Journal
Biochem J (2001) 354 (1): 73–78.
https://doi.org/10.1042/bj3540073
Published: 08 February 2001
... on the activation of PI-3K. 1 To whom correspondence should be addressed (e-mail [email protected] ). 9 2 2000 27 9 2000 20 11 2000 The Biochemical Society, London © 2001 2001 CDM family proteins pleckstrin homology domain Rac Biochem. J. (2001) 354, 73 78 (Printed...
View articletitled, Membrane recruitment of DOCK180 by binding to PtdIns(3,4,5)P3
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Articles

Identification of centaurin-α1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1

Kanamarlapudi VENKATESWARLU, Paru B. OATEY, Jeremy M. TAVARÉ, Trevor R. JACKSON, Peter J. CULLEN
Journal: Biochemical Journal
Biochem J (1999) 340 (2): 359–363.
https://doi.org/10.1042/bj3400359
Published: 25 May 1999
... demonstrated the rapid plasma membrane recruitment of cytosolic GFP-centaurin-α 1 following stimulation with either nerve growth factor or epidermal growth factor. This recruitment was dependent on the centaurin-α 1 pleckstrin homology domains and was blocked by the PtdIns(4,5) P 2 3-kinase (PI 3-kinase...
View articletitled, Identification of centaurin-α1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1
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Includes: Supplementary data