Concerted dephosphorylation of the transcription factor NFAT1 induces a conformational switch that regulates transcriptional activity (Q28140993)

ORCID Public Data File 2021

author name string

H Okamura

1

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J Aramburu

2

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C García-Rodríguez

3

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J P Viola

4

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A Raghavan

5

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M Tahiliani

6

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X Zhang

7

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J Qin

8

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P G Hogan

9

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A Rao

Selective inhibition of NFAT activation by a peptide spanning the calcineurin targeting site of NFAT

10

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language of work or name

English

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publication date

September 2000

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published in

Molecular Cell

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volume

6

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page(s)

539-50

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issue

3

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cites work

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Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA

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Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway

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Dimerization in MAP-kinase signaling

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Generic signals and specific outcomes: signaling through Ca2+, calcineurin, and NF-AT

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Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1

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Transcriptional control by protein phosphorylation: signal transmission from the cell surface to the nucleus

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Nucleocytoplasmic shuttling factors including Ran and CRM1 mediate nuclear export of NFAT In vitro

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Calcineurin binds the transcription factor NFAT1 and reversibly regulates its activity

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Interaction of calcineurin with a domain of the transcription factor NFAT1 that controls nuclear import

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Control of NFATx1 nuclear translocation by a calcineurin-regulated inhibitory domain

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Phosphorylation of the transcription factor NFATp inhibits its DNA binding activity in cyclosporin A-treated human B and T cells

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

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

113707

113707

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference