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Cot/Tpl2 and PKCzeta cooperate in the regulation of the transcriptional activity of NFATc2 through the phosphorylation of its amino-terminal domain.

Abstract：

:Nuclear factor of activated T cells (NFAT) plays a prominent role in gene transcription during the immune response. Growing evidence demonstrates the implication of inducible phosphorylation of the transactivation domain (TAD) of NFAT in transcriptional activation of genes. We have analyzed the regulation of NFATc2 activation by Cot/Tpl2 and protein kinase C zeta (PKCzeta) in T cells. Our results show that PKCzeta and Cot/Tpl2 cooperate in regulating the transactivation activity mediated by the amino-terminal domain of NFATc2. Neither Cot/Tpl2 kinase nor PKCzeta-mediated induction of the transactivation activity of NFATc2 was affected by cyclosporin-A treatment, supporting a calcineurin independent route in the signaling pathways mediating NFATc2 activation. Co-precipitation experiments showed physical interaction among Cot/Tpl2, PKCzeta and NFATc2. Analysis of the transactivation activity of deletions in the N-terminal region of NFATc2, suggested the involvement of amino acids 52-64 of NFATc2 in the induction of its transactivating function by PKCzeta. This kinase in vitro phosphorylates NFATc2 and deletion and mutational studies identified Ser53 and Ser56 (of the SPPS motif) as substrates for PKCzeta. Thus, our results suggest that PKCzeta phosphorylation of Ser53 and Ser56 in the N-terminal TAD from NFATc2 potentiates its transactivating function in human T cells.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Gómez-Casero E,San-Antonio B,Iñiguez MA,Fresno M

doi

10.1016/j.cellsig.2007.02.010

subject

Has Abstract

pub_date

2007-08-01 00:00:00

pages

1652-61

issue

8

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(07)00074-5

journal_volume

19

pub_type

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