NF-AT activation requires suppression of Crm1-dependent export by calcineurin

Article Abstract:

NF-ATs are subject to a futile cycling across the nuclear envelope because of engagement with the exportin protein Crm1. This means that the nuclear import of NF-ATs is insufficient for the activation of NF-AT target genes. It has been established that nuclear-export signals (NESs) identified by functional analyses also mediate interactions between Crm1 and NT-AT4. Each of the NESs is sufficient for Crm1 binding and Crm1-mediated nuclear export. Suppression of the NF-AT nuclear export process through calcineurin binding is essential to the formation of effective NF-AT transcriptional complexes.

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Role of kinases and the phosphate calcineurin in the nuclear shuttling of transcription factor NF-AT4

Article Abstract:

The nuclear complex of transcription factor NF-AT4 and protein phosphatase calcineurin facilitates calcium signalling by attenuating a strong nuclear NF-AT kinase. Calcium signalling activates an interaction between NF-AT and calcineurin. These molecules are transported to the nucleus in the form of a complex. In the nucleus, calcineurin dephosphorylates NF-AT4. Calcineurin inhibitors, cyclosporin A and FK506, obstruct dephosphorylation and nuclear transfer of NF-AT.

Analysis, Enzymes, Proteins, Biological transport

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Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2

Article Abstract:

The mechanism behind suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2 was analyzed by coexpression of myc-epitope-tagged Bcl-2 with calcineurin (CnA) and immunoprecipitation with anti-myc antibodies in baby hamster kidneys. Results indicate that calcineurin is unable to promote the nuclear translocation of NF-AT, implicating the influence of Bcl-2 on the inhibition of NF-AT.

Cellular signal transduction, Growth factor receptors, Interleukin-2, Drug receptors

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