کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10802204 | 1055668 | 2014 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Intracellular mobility and nuclear trafficking of the stress-activated kinase JNK1 are impeded by hyperosmotic stress
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کلمات کلیدی
JnkTAGP45NLSIAFIMPNTSMEFsERKFRAPGSTGFPCLSM5-Iodoacetamidofluorescein - 5-یووداکتامید فلوئورسینc-Jun N-terminal kinase - C-Jun N-terminal kinaseMAPK - MAPKMAPK kinase - MAPK کینازMKK - MCCt1/2 - t1 / 2Live-imaging - تصویربرداری زندهstandard error of the mean - خطای استاندارد میانگینnuclear localization sequence - دنباله محلی سازی هسته ایHTC cells - سلول های HTCSorbitol - سوربیتولfluorescence recovery after photobleaching - فلوئورسانس پس از فوتوبلاسیکmurine embryonic fibroblasts - فیبروبلاست های جنینی جنینیSEM - مدل معادلات ساختاری / میکروسکوپ الکترونی روبشیconfocal laser scanning microscopy - میکروسکوپهای اسکن لیزری کانفوکالImportin - وارداتNuclear import - واردات هسته ایgreen fluorescent protein - پروتئین فلورسنت سبزmitogen-activated protein kinase - پروتئین کیناز فعال با mitogenextracellular signal-regulated kinase - کیناز تنظیم شده سیگنال خارج سلولیglutathione S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Intracellular mobility and nuclear trafficking of the stress-activated kinase JNK1 are impeded by hyperosmotic stress Intracellular mobility and nuclear trafficking of the stress-activated kinase JNK1 are impeded by hyperosmotic stress](/preview/png/10802204.png)
چکیده انگلیسی
The c-Jun N-terminal kinases (JNKs) are a group of stress-activated protein kinases that regulate gene expression changes through specific phosphorylation of nuclear transcription factor substrates. To address the mechanisms underlying JNK nuclear entry, we employed a semi-intact cell system to demonstrate for the first time that JNK1 nuclear entry is dependent on the importin α2/β1 heterodimer and independent of importins α3, α4, β2, β3, 7 and 13. However, quantitative image analysis of JNK1 localization following exposure of cells to either arsenite or hyperosmotic stress did not indicate its nuclear accumulation. Extending our analyses to define the dynamics of nuclear trafficking of JNK1, we combined live cell imaging analyses with fluorescence recovery after photobleaching (FRAP) protocols. Subnuclear and subcytoplasmic bleaching protocols revealed the slowed movement of JNK1 in both regions in response to hyperosmotic stress. Strikingly, while movement into the nucleus of green fluorescent protein (GFP) or transport of a GFP-T-antigen fusion protein as estimated by initial rates and time to reach half-maximal recovery (t1/2) measures remained unaltered, hyperosmotic stress slowed the nuclear entry of GFP-JNK1. In contrast, arsenite exposure which did not alter the initial rates of nuclear accumulation of GFP, GFP-T-antigen or GFP-JNK1, decreased the t1/2 for nuclear accumulation of both GFP and GFP-JNK1. Thus, our results challenge the paradigm of increased nuclear localization of JNK broadly in response to all forms of stress-activation and are consistent with enhanced interactions of stress-activated JNK1 with scaffold and substrate proteins throughout the nucleus and the cytosol under conditions of hyperosmotic stress.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1843, Issue 2, February 2014, Pages 253-264
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1843, Issue 2, February 2014, Pages 253-264
نویسندگان
Mariya Misheva, Gurpreet Kaur, Kevin R.W. Ngoei, Yvonne Y. Yeap, Ivan H.W. Ng, Kylie M. Wagstaff, Dominic C.H. Ng, David A. Jans, Marie A. Bogoyevitch,