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rdf:type |
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lifeskim:mentions |
umls-concept:C0019602,
umls-concept:C0031715,
umls-concept:C0032824,
umls-concept:C0039194,
umls-concept:C1332714,
umls-concept:C1416611,
umls-concept:C1506309,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1879547
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pubmed:issue |
5
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pubmed:dateCreated |
2006-12-12
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pubmed:abstractText |
The Ca2+ -activated K+ channel KCa3.1 is required for Ca2+ influx and the subsequent activation of B and T cells. Inhibitors of KCa3.1 are in development to treat autoimmune diseases and transplant rejection, underscoring the importance in understanding how these channels are regulated. We show that nucleoside diphosphate kinase B (NDPK-B), a mammalian histidine kinase, functions downstream of PI(3)P to activate KCa3.1. NDPK-B directly binds and activates KCa3.1 by phosphorylating histidine 358 in the carboxyl terminus of KCa3.1. Endogenous NDPK-B is also critical for KCa3.1 channel activity and the subsequent activation of CD4 T cells. These findings provide one of the best examples whereby histidine phosphorylation regulates a biological process in mammals, and provide an example whereby a channel is regulated by histidine phosphorylation. The critical role for NDPK-B in the reactivation of CD4 T cells indicates that understanding NDPK-B regulation should uncover novel pathways required for T cell activation.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1097-2765
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pubmed:author |
pubmed-author:AlbaqumiMamdouhM,
pubmed-author:BackerJonathan MJM,
pubmed-author:ChoudhuryPapiyaP,
pubmed-author:CoetzeeWilliam AWA,
pubmed-author:JohnsonAmanda KAK,
pubmed-author:KoKyungK,
pubmed-author:SkolnikEdward YEY,
pubmed-author:SrivastavaShekharS,
pubmed-author:UnutmazDeryaD,
pubmed-author:YanYingY,
pubmed-author:ZempEE
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
665-75
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:17157250-Amino Acid Sequence,
pubmed-meshheading:17157250-Androstadienes,
pubmed-meshheading:17157250-Animals,
pubmed-meshheading:17157250-CD4-Positive T-Lymphocytes,
pubmed-meshheading:17157250-CHO Cells,
pubmed-meshheading:17157250-Cells, Cultured,
pubmed-meshheading:17157250-Cricetinae,
pubmed-meshheading:17157250-Histidine,
pubmed-meshheading:17157250-Humans,
pubmed-meshheading:17157250-Intermediate-Conductance Calcium-Activated Potassium...,
pubmed-meshheading:17157250-Lymphocyte Activation,
pubmed-meshheading:17157250-Molecular Sequence Data,
pubmed-meshheading:17157250-NM23 Nucleoside Diphosphate Kinases,
pubmed-meshheading:17157250-Nucleoside-Diphosphate Kinase,
pubmed-meshheading:17157250-Phosphorylation,
pubmed-meshheading:17157250-Protein Binding,
pubmed-meshheading:17157250-Time Factors
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pubmed:year |
2006
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pubmed:articleTitle |
Histidine phosphorylation of the potassium channel KCa3.1 by nucleoside diphosphate kinase B is required for activation of KCa3.1 and CD4 T cells.
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pubmed:affiliation |
Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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