Dissecting functions of the N-terminal domain and GAS-site recognition in STAT3 nuclear trafficking
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- 作者：Antons Martincuksa ; Dirk Fahrenkampa ; Serge Haana ; b ; c ; Andreas Herrmanna ; d ; Andrea Kü ; stera ; Gerhard Mü ; ller-Newena ; mueller-newen@rwth-aachen.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：CCD ; coiled-coil domain ; CFP ; cyan fluorescent protein ; FP ; fluorescent proteins ; IBB ; importin-β binding domain ; GAS ; gamma interferon activation site ; IL ; interleukin ; JAK ; Janus kinase ; LMB ; leptomycin B ; MEF ; murine embryonic fibroblasts ; NLS ; nuclear localization signal ; NPC ; nuclear pore complex ; NTD ; N-terminal domain ; PBS ; phosphate-buffered saline ; R ; receptor ; s ; soluble ; STAT ; signal transducer and activator of transcription ; TAD ; transactivation domain ; WT ; wild-type ; YFP ; yellow flu
- 刊名：Cellular Signalling
- 出版年：2016
- 出版时间：August 2016
- 年：2016
- 卷：28
- 期：8
- 页码：810-825
- 全文大小：2590 K
文摘
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GAS-element-specific DNA recognition is dispensable for nuclear accumulation of STAT3
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Upon activation STAT3 NTD deletion mutant remains in the cytoplasm in the form of phosphorylated dimers
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In contrast to STAT1, STAT3 NTD is not required for binding to various importin-α isoforms
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The importin-α5 mutant Y476G that does not bind STAT1 is still able to bind STAT3
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For latent nucleocytoplasmic shuttling of STAT3 GAS-element binding and functional N-terminal or SH2 domains are dispensable