Mutation of the regulatory phosphorylation site of tobacco nitrate reductase results in high nitrite excretion and NO emission from leaf and root tissue

Planta ◽  
2004 ◽  
Vol 219 (1) ◽  
pp. 59-65 ◽  
Author(s):  
Unni S. Lea ◽  
Floor ten Hoopen ◽  
Fiona Provan ◽  
Werner M. Kaiser ◽  
Christian Meyer ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Phosphorylation Site ◽  
Root Tissue ◽  
No Emission ◽  
Regulatory Phosphorylation

Identification of Ser-543 as the Major Regulatory Phosphorylation Site in Spinach Leaf Nitrate Reductase

1996 ◽  
Vol 8 (3) ◽  
pp. 505 ◽  
Author(s):  
Markus Bachmann ◽  
Naomasa Shiraishi ◽  
Wilbur H. Campbell ◽  
Byung-Chun Yoo ◽  
Alice C. Harmon ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Phosphorylation Site ◽  
Regulatory Phosphorylation ◽  
Spinach Leaf ◽  
Leaf Nitrate

scholarly journals Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase.

1996 ◽  
Vol 8 (3) ◽  
pp. 505-517 ◽  
Author(s):  
M Bachmann ◽  
N Shiraishi ◽  
W H Campbell ◽  
B C Yoo ◽  
A C Harmon ◽  
...  
Keyword(s):  
Nitrate Reductase ◽  
Phosphorylation Site ◽  
Regulatory Phosphorylation ◽  
Spinach Leaf ◽  
Leaf Nitrate

scholarly journals Histidine phosphorylation relieves copper inhibition in the mammalian potassium channel KCa3.1

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Shekhar Srivastava ◽  
Saswati Panda ◽  
Zhai Li ◽  
Stephen R Fuhs ◽  
Tony Hunter ◽  
...  
Keyword(s):  
Potassium Channel ◽  
T Cell Activation ◽  
Cell Activation ◽  
Phosphorylation Site ◽  
Nucleoside Diphosphate Kinase ◽  
Calcium Flux ◽  
Channel Activity ◽  
Nucleoside Diphosphate Kinase B ◽  
Regulatory Phosphorylation ◽  
Histidine Phosphorylation

KCa2.1, KCa2.2, KCa2.3 and KCa3.1 constitute a family of mammalian small- to intermediate-conductance potassium channels that are activated by calcium-calmodulin. KCa3.1 is unique among these four channels in that activation requires, in addition to calcium, phosphorylation of a single histidine residue (His358) in the cytoplasmic region, by nucleoside diphosphate kinase-B (NDPK-B). The mechanism by which KCa3.1 is activated by histidine phosphorylation is unknown. Histidine phosphorylation is well characterized in prokaryotes but poorly understood in eukaryotes. Here, we demonstrate that phosphorylation of His358 activates KCa3.1 by antagonizing copper-mediated inhibition of the channel. Furthermore, we show that activated CD4+ T cells deficient in intracellular copper exhibit increased KCa3.1 histidine phosphorylation and channel activity, leading to increased calcium flux and cytokine production. These findings reveal a novel regulatory mechanism for a mammalian potassium channel and for T-cell activation, and highlight a unique feature of histidine versus serine/threonine and tyrosine as a regulatory phosphorylation site.

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