Abstract:
: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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Srivastava S,Li Z,Ko K,Choudhury P,Albaqumi M,Johnson AK,Yan Y,Backer JM,Unutmaz D,Coetzee WA,Skolnik EYdoi
10.1016/j.molcel.2006.11.012subject
Has Abstractpub_date
2006-12-08 00:00:00pages
665-675issue
5eissn
1097-2765issn
1097-4164pii
S1097-2765(06)00783-0journal_volume
24pub_type
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