scholarly journals High Affinity Binding of Inositol Phosphates and Phosphoinositides to the Pleckstrin Homology Domain of RAC/Protein Kinase B and Their Influence on Kinase Activity

1997 ◽  
Vol 272 (13) ◽  
pp. 8474-8481 ◽  
Author(s):  
Matthias Frech ◽  
Mirjana Andjelkovic ◽  
Evan Ingley ◽  
K. Kishta Reddy ◽  
John R. Falck ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Inositol Phosphates ◽  
Protein Kinase B ◽  
Pleckstrin Homology Domain ◽  
Affinity Binding ◽  
Pleckstrin Homology ◽  
High Affinity Binding ◽  
High Affinity

scholarly journals High Affinity Binding of the Pleckstrin Homology Domain of mSos1 to Phosphatidylinositol (4,5)-Bisphosphate

1997 ◽  
Vol 272 (3) ◽  
pp. 1799-1804 ◽  
Author(s):  
Terry J. Kubiseski ◽  
Yuh Min Chook ◽  
Wendy E. Parris ◽  
Maria Rozakis-Adcock ◽  
Tony Pawson
Keyword(s):  
Pleckstrin Homology Domain ◽  
Affinity Binding ◽  
Pleckstrin Homology ◽  
High Affinity Binding ◽  
High Affinity

scholarly journals Analysis of High-Affinity Binding of Protein Kinase R to Double-Stranded RNA

Biochemistry ◽  
2012 ◽  
Vol 51 (44) ◽  
pp. 8764-8770 ◽  
Author(s):  
Bushra Husain ◽  
Ishita Mukerji ◽  
James L. Cole
Keyword(s):  
Protein Kinase ◽  
Affinity Binding ◽  
Protein Kinase R ◽  
High Affinity Binding ◽  
Double Stranded Rna ◽  
High Affinity

scholarly journals A Cell Number Counting Factor Regulates Akt/Protein Kinase B To Regulate Dictyostelium discoideum Group Size

2004 ◽  
Vol 3 (5) ◽  
pp. 1176-1184 ◽  
Author(s):  
Tong Gao ◽  
David Knecht ◽  
Lei Tang ◽  
R. Diane Hatton ◽  
Richard H. Gomer
Keyword(s):  
Protein Kinase ◽  
Dictyostelium Discoideum ◽  
Group Size ◽  
Kinase Activity ◽  
Fluorescent Protein ◽  
Protein Kinase B ◽  
Cell Number ◽  
Pleckstrin Homology Domain ◽  
Wild Type ◽  
High Concentration

ABSTRACT Little is known about how individual cells can organize themselves to form structures of a given size. During development, Dictyostelium discoideum aggregates in dendritic streams and forms groups of ∼20,000 cells. D. discoideum regulates group size by secreting and simultaneously sensing a multiprotein complex called counting factor (CF). If there are too many cells in a stream, the associated high concentration of CF will decrease cell-cell adhesion and increase cell motility, causing aggregation streams to break up. The pulses of cyclic AMP (cAMP) that mediate aggregation cause a transient translocation of Akt/protein kinase B (Akt/PKB) to the leading edge of the plasma membrane and a concomitant activation of the kinase activity, which in turn stimulates motility. We found that countin− cells (which lack bioactive CF) and wild-type cells starved in the presence of anticountin antibodies (which block CF activity) showed a decreased level of cAMP-stimulated Akt/PKB membrane translocation and kinase activity compared to parental wild-type cells. Recombinant countin has the bioactivity of CF, and a 1-min treatment of cells with recombinant countin potentiated Akt/PKB translocation to membranes and Akt/PKB activity. Western blotting of total cell lysates indicated that countin does not affect the total level of Akt/PKB. Fluorescence microscopy of cells expressing an Akt/PKB pleckstrin homology domain-green fluorescent protein (PH-GFP) fusion protein indicated that recombinant countin and anti-countin antibodies do not obviously alter the distribution of Akt/PKB PH-GFP when it translocates to the membrane. Our data indicate that CF increases motility by potentiating the cAMP-stimulated activation and translocation of Akt/PKB.

Sign in / Sign up

Export Citation Format

Share Document