Possible involvement of protein phosphorylation in the regulation of cytoplasmic organization and streaming in root hair cells as revealed by a protein phosphatase inhibitor, calyculin A

PROTOPLASMA ◽  
2000 ◽  
Vol 211 (1-2) ◽  
pp. 29-38 ◽  
Author(s):  
E. Yokota ◽  
K. Hibara ◽  
N. Imamichi ◽  
T. Shimmen
2010 ◽  
Vol 58 (3) ◽  
pp. 147-156 ◽  
Author(s):  
Mercedes Pozuelo-Rubio ◽  
Nick R. Leslie ◽  
Jane Murphy ◽  
Carol MacKintosh

Platelets ◽  
2010 ◽  
Vol 21 (7) ◽  
pp. 555-562 ◽  
Author(s):  
Zsuzsa Simon ◽  
Andrea Kiss ◽  
Ferenc Erdödi ◽  
Hendra Setiadi ◽  
Ildikó Beke Debreceni ◽  
...  

2004 ◽  
Vol 14 (3) ◽  
pp. 287-296 ◽  
Author(s):  
Ryan L. Wagner ◽  
M.K. Walker-Simmons

An early difference in net protein phosphorylation activity occurred in dormant and after-ripened wheat (Triticum aestivum L.) grains within the first hour of imbibition at 30°C. Embryos from dry, dormant and after-ripened caryopses exhibited a high degree of protein phosphorylation, particularly of four proteins (68, 54, 51 and 42 kDa). Upon hydration, protein phosphorylation activity in dormant embryos decreased within 1 h and reached minimal phosphorylation activity by 5 h. Protein phosphorylation activity in after-ripened (germinable) embryos was not suppressed and remained high during germination. If the hydrated dormant embryos were dried, protein phosphorylation activity was restored. Application of the protein phosphatase inhibitor, okadaic acid, partially overcame dormancy and slowed the decrease in phosphorylation activity. These results suggested that reduction of protein phosphorylation activity slowed the rate of germination.


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