کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10802104 | 1055658 | 2014 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Histone H3K4 methyltransferase Mll1 regulates protein glycosylation and tunicamycin-induced apoptosis through transcriptional regulation
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کلمات کلیدی
2-deoxy-d-glucoseinositol-requiring protein-1protein kinase RNA (PKR)-like ER kinaseLAMP2DPAGT1MLL1tunicamycinH6PDBFAATF6ThapsigarginIRE1UPR2-DG - 2 DGbrefeldin A - برفلدین AApoptosis - خزان یاختهایactivating transcription factor-6 - فعال کردن عامل رونویسی 6Hexose-6-phosphate dehydrogenase - هگزوز 6-فسفات دهیدروژنازlysosomal-associated membrane protein 2 - پروتئین غشای مرتبط با لیزوزوم 2PERK - پرکProtein glycosylation - گلیکوزیلت پروتئین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Histone H3K4 methyltransferase Mll1 regulates protein glycosylation and tunicamycin-induced apoptosis through transcriptional regulation Histone H3K4 methyltransferase Mll1 regulates protein glycosylation and tunicamycin-induced apoptosis through transcriptional regulation](/preview/png/10802104.png)
چکیده انگلیسی
Disrupting protein glycosylation induces ER (endoplasmic reticulum) stress, resulting in the activation of UPR (unfolded protein response) pathways. A key function of the UPR is to restore ER homeostasis, but prolonged or unsolved ER stress can lead to apoptosis. MLL1 (Mixed Lineage Leukemia 1, also named ALL-1 or HRX), a histone H3K4 methyltransferase in mammals, plays important roles in leukemogenesis, transcriptional regulation, cell cycle and development. Here, we find that Mll1 deficiency enhances UPR and apoptosis induced by the glycosylation inhibitor TM (tunicamycin). The abnormal regulation of the UPR appears to be caused by a defect in protein glycosylation. Furthermore, Mll1 directly binds to the promoters of H6pd, Galnt12 and Ugp2, which regulates H3K4 trimethylation and the subsequent expression of these genes. The knockdown of H6pd, Galnt12 or Ugp2 enhances TM-induced apoptosis in Mll1+/+Â MEF cells, whereas the ectopic expression of these proteins inhibits TM-induced apoptosis in Mll1â/â MEF cells. Together, our data suggest that the maturation of glycoproteins in the ER is subject to regulation at the epigenetic level by a histone methyltransferase whose abnormality can lead to cancer and developmental defects.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1843, Issue 11, November 2014, Pages 2592-2602
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1843, Issue 11, November 2014, Pages 2592-2602
نویسندگان
Xiang Wang, Lingao Ju, Jiadong Fan, Yuan Zhu, Xiaolan Liu, Kun Zhu, Min Wu, Lianyun Li,