scholarly journals Protein kinase A increases the binding affinity and the Ca2+ release activity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells

2007 ◽  
Vol 99 (7) ◽  
pp. 379-388 ◽  
Author(s):  
Benoit Chaloux ◽  
Annabelle Z. Caron ◽  
Gaétan Guillemette
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Binding Affinity ◽  
Receptor Type ◽  
Rinm5f Cells ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Type 3 ◽  
Kinase A

Protein kinase C decreases the apparent affinity of the inositol 1,4,5-trisphosphate receptor type 3 in RINm5F cells

Cell Calcium ◽  
2007 ◽  
Vol 42 (3) ◽  
pp. 323-331 ◽  
Author(s):  
Annabelle Z. Caron ◽  
Benoit Chaloux ◽  
Guillaume Arguin ◽  
Gaetan Guillemette
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Receptor Type ◽  
Rinm5f Cells ◽  
Apparent Affinity ◽  
Kinase C ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Type 3

scholarly journals Protein Kinase A Increases Type-2 Inositol 1,4,5-Trisphosphate Receptor Activity by Phosphorylation of Serine 937

2009 ◽  
Vol 284 (37) ◽  
pp. 25116-25125 ◽  
Author(s):  
Matthew J. Betzenhauser ◽  
Jenna L. Fike ◽  
Larry E. Wagner ◽  
David I. Yule
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Receptor Activity ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Kinase A

scholarly journals Association of Type 1 Inositol 1,4,5-Trisphosphate Receptor with AKAP9 (Yotiao) and Protein Kinase A

2004 ◽  
Vol 279 (18) ◽  
pp. 19375-19382 ◽  
Author(s):  
Huiping Tu ◽  
Tie-Shan Tang ◽  
Zhengnan Wang ◽  
Ilya Bezprozvanny
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Kinase A

Differential modulation of inositol 1,4,5-trisphosphate receptor type 1 and type 3 by ATP

Cell Calcium ◽  
2000 ◽  
Vol 27 (5) ◽  
pp. 257-267 ◽  
Author(s):  
K. Maes ◽  
L. Missiaen ◽  
P. De Smet ◽  
S. Vanlingen ◽  
G. Callewaert ◽  
...  
Keyword(s):  
Receptor Type ◽  
Differential Modulation ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Type 3

Thr90 phosphorylation of Hsp90α by protein kinase A regulates its chaperone machinery

2011 ◽  
Vol 441 (1) ◽  
pp. 387-397 ◽  
Author(s):  
Xiaofeng Wang ◽  
Xin-an Lu ◽  
Xiaomin Song ◽  
Wei Zhuo ◽  
Lin Jia ◽  
...  
Keyword(s):  
Heat Shock ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Binding Affinity ◽  
Heat Shock Protein 90 ◽  
Proliferating Cells ◽  
Interacting Protein ◽  
Fk506 Binding Protein ◽  
The Impact ◽  
Kinase A

Hsp90 (heat-shock protein 90) is one of the most important molecular chaperones in eukaryotes. Hsp90 facilitates the maturation, activation or degradation of its client proteins. It is now well accepted that both ATP binding and co-chaperone association are involved in regulating the Hsp90 chaperone machinery. However, other factors such as post-translational modifications are becoming increasingly recognized as being involved in this process. Recent studies have reported that phosphorylation of Hsp90 plays an unanticipated role in this process. In the present study, we systematically investigated the impact of phosphorylation of a single residue (Thr90) of Hsp90α (pThr90-Hsp90α) on its chaperone machinery. We demonstrate that protein kinase A specifically phosphorylates Hsp90α at Thr90, and that the pThr9090-Hsp90α level is significantly elevated in proliferating cells. Thr90 phosphorylation affects the binding affinity of Hsp90α to ATP. Subsequent examination of the interactions of Hsp90α with co-chaperones reveals that Thr90 phosphorylation specifically regulates the association of a subset of co-chaperones with Hsp90α. The Hsp90α T90E phosphor-mimic mutant exhibits increased association with Aha1 (activator of Hsp90 ATPase homologue 1), p23, PP5 (protein phosphatase 5) and CHIP (C-terminus of Hsp70-interacting protein), and decreased binding affinity with Hsp70, Cdc37 (cell division cycle 37) and Hop [Hsc70 (heat-shock cognate protein 70)/Hsp90-organizing protein], whereas its interaction with FKBP52 (FK506-binding protein 4) is only moderately affected. Moreover, we find that the ability of the T90E mutant to form complexes with its clients, such as Src, Akt or PKCγ (protein kinase Cγ), is dramatically impaired, suggesting that phosphorylation affects its chaperoning activity. Taken together, the results of the present study demonstrate that Thr90 phosphorylation is actively engaged in the regulation of the Hsp90α chaperone machinery and should be a generic determinant for the cycling of Hsp90α chaperone function.

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