Actin binding of human LIM and SH3 Protein (LASP) is regulated by cGMP-and cAMP-dependent protein kinase phosphorylation on serine 146

2003 ◽  
Vol 3 (S2) ◽  
Author(s):  
Elke Butt ◽  
Christian Kaicher ◽  
Stepan Gambaryan ◽  
Nina Göttfert ◽  
Annette Galler ◽  
...  

2003 ◽  
Vol 278 (18) ◽  
pp. 15601-15607 ◽  
Author(s):  
Elke Butt ◽  
Stepan Gambaryan ◽  
Nina Göttfert ◽  
Annette Galler ◽  
Katrin Marcus ◽  
...  






2001 ◽  
Vol 280 (6) ◽  
pp. L1282-L1289 ◽  
Author(s):  
Stephanie E. Porter ◽  
Lori D. Dwyer-Nield ◽  
Alvin M. Malkinson

Cell shape is mediated in part by the actin cytoskeleton and the actin-binding protein vinculin. These proteins in turn are regulated by protein phosphorylation. We assessed the contribution of cAMP-dependent protein kinase A isozyme I (PKA I) to lung epithelial morphology using the E10/E9 sibling cell lines. PKA I concentration is high in flattened, nontumorigenic E10 cells but low in their round E9 transformants. PKA I activity was lowered in E10 cells by stable transfection with a dominant negative RIα mutant of the PKA I regulatory subunit and was raised in E9 cells by stable transfection with a wild-type Cα catalytic subunit construct. Reciprocal changes in morphology ensued. E10 cells became rounder and grew in colonies, their actin microfilaments were disrupted, and vinculin localization at cell-cell junctions was diminished. The converse occurred in E9 cells on elevating their PKA I content. Demonstration that PKA I is responsible for the dichotomy in these cellular behaviors suggests that manipulating PKA I concentrations in lung cancer would provide useful adjuvant therapy.



1975 ◽  
Author(s):  
F. M. Booyse ◽  
J. Marr ◽  
D. Tomlinson ◽  
D. G. Yang ◽  
M. E. Rafelson

Analysis of intact 32P-labeled platelets by SDS-polyacrylamidegel electrophoresis shows the presence of only a single phosphorylated protein. This phosphoprotein has been isolated, has a subunit molecular weight of 11,100, is surface localized (lactoperoxidase-125 Iodine labeling) and binds 1 mole of Ca2+ per mole of phosphorylated subunit. The γ-32ऩ from (γ-32P) ATP is specifically incorporated as 0-phosphoserine by a cAMP-dependent protein kinase.The phosphorylated state and hence the Ca-binding of this protein is maintained by membrane associated cAMP-dependent protein kinase phosphorylation and phosphoprotein phosphatase dephosphorylation. Thrombin, collagen, histone and ADP competitively inhibit phosphorylation and Ca-binding by serving as protein kinase acceptors. Epinephrine, serotonin and ristosetin induce dephosphorylation and abolish Ca-binding by activating the phosphoprotein phosphatase. PGEl5 ATP, cAMP increase phosphorylation and Ca-binding by activating the protein kinase ; aspirin and EDTA increase phosphorylation and Ca-binding by inhibiting the phosphoprotein phosphatase. In 3 cases of Glanzmann’s thrombasthenia, increased phosphorylation and Ca-binding was due to decreased phosphoprotein phosphatase activity-activity was restored the addition of ristosetin. A common phosphorylation-dephosphorylation mechanism for the action of inducers and inhibitors on Ca-mobilization and platelet activation will be presented.





2008 ◽  
Vol 283 (12) ◽  
pp. 7523-7530 ◽  
Author(s):  
Yun Shi ◽  
Xianfeng Chen ◽  
Zhongying Wu ◽  
Weiwei Shi ◽  
Yang Yang ◽  
...  


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