scholarly journals Posttranslational Modification of Maize Chloroplast Pyruvate Orthophosphate Dikinase Reveals the Precise Regulatory Mechanism of Its Enzymatic Activity

2014 ◽  
Vol 165 (2) ◽  
pp. 534-549 ◽  
Author(s):  
Yi-Bo Chen ◽  
Tian-Cong Lu ◽  
Hong-Xia Wang ◽  
Jie Shen ◽  
Tian-Tian Bu ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Posttranslational Modification ◽  
Regulatory Mechanism ◽  
Pyruvate Orthophosphate Dikinase ◽  
Orthophosphate Dikinase ◽  
Maize Chloroplast

scholarly journals Tubulin Acetyltransferase αTAT1 Destabilizes Microtubules Independently of Its Acetylation Activity

2012 ◽  
Vol 33 (6) ◽  
pp. 1114-1123 ◽  
Author(s):  
Nereo Kalebic ◽  
Concepcion Martinez ◽  
Emerald Perlas ◽  
Philip Hublitz ◽  
Daniel Bilbao-Cortes ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Posttranslational Modification ◽  
Functional Significance ◽  
Mammalian Cells ◽  
Regulatory Mechanism ◽  
Critical Factor ◽  
Cellular Functions ◽  
Microtubule Stability ◽  
Per Se ◽  
Major Target

Acetylation of α-tubulin at lysine 40 (K40) is a well-conserved posttranslational modification that marks long-lived microtubules but has poorly understood functional significance. Recently, αTAT1, a member of the Gcn5-relatedN-acetyltransferase superfamily, has been identified as an α-tubulin acetyltransferase in ciliated organisms. Here, we explored the function of αTAT1 with the aim of understanding the consequences of αTAT1-mediated microtubule acetylation. We demonstrate that α-tubulin is the major target of αTAT1 but that αTAT1 also acetylates itself in a regulatory mechanism that is required for effective modification of tubulin. We further show that in mammalian cells, αTAT1 promotes microtubule destabilization and accelerates microtubule dynamics. Intriguingly, this effect persists in an αTAT1 mutant with no acetyltransferase activity, suggesting that interaction of αTAT1 with microtubules, rather than acetylationper se, is the critical factor regulating microtubule stability. Our data demonstrate that αTAT1 has cellular functions that extend beyond its classical enzymatic activity as an α-tubulin acetyltransferase.

scholarly journals Pyruvate Orthophosphate Dikinase

1984 ◽  
Vol 74 (1) ◽  
pp. 189-191 ◽  
Author(s):  
Sherry L. Gee ◽  
Steven Ruzin ◽  
James A. Bassham
Keyword(s):  
Pyruvate Orthophosphate Dikinase ◽  
Orthophosphate Dikinase
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