کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5508840 | 1400401 | 2017 | 48 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The E3 ubiquitin ligase MID1/TRIM18 promotes atypical ubiquitination of the BRCA2-associated factor 35, BRAF35
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کلمات کلیدی
PTMFN3HmgHECTTRIMBHCRFPRBRMid2HMWRBCCPP2AHDACRET finger proteinSUMOOpitz G/BBB syndromeMid1 - mid1post-translational modification - اصلاح post-translationalsmall ubiquitin-related modifier - اصلاح کننده کوچک کوچک ubiquitintripartite motif - الگوی سه گانهRing - حلقهfibronectin type III - فیبرنکتین نوع IIIhistone deacetylase - هیستون داستیلازhigh molecular weight - وزن مولکولی بالاprotein phosphatase 2A - پروتئین فسفاتاز 2Areally interesting new gene - ژن جدید واقعا جالبSpry - کشیدنCoiled-coil - کویل کویلhigh-mobility-group - گروه تحرک بالاubiquitination - یوبی کوئیتینه شدن Ubiquitin - یوبیکویتین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
MID1/TRIM18 is a member of the TRIM family of ubiquitin E3 ligases characterized by the presence of a conserved RING-containing N-terminal tripartite motif. Mutations in the MID1 gene have been associated with the X-linked form of Opitz Syndrome, a developmental disorder characterized by midline defects and intellectual disability. The effect of MID1 E3 ligase activity within the cell and the role in the pathogenesis of the disease is still not completely unraveled. Here, we report BRAF35, a non-canonical HMG nuclear factor, as a novel MID1 substrate. MID1 is implicated in BRAF35 ubiquitination promoting atypical poly-ubiquitination via K6-, K27- and K29-linkages. We observed a partial co-localization of the two proteins within cytoplasmic bodies. We found that MID1 depletion alters BRAF35 localization in these structures and increases BRAF35 stability affecting its cytoplasmic abundance. Our data reveal a novel role for MID1 and for atypical ubiquitination in balancing BRAF35 presence, and likely its activity, within nuclear and cytoplasmic compartments.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1864, Issue 10, October 2017, Pages 1844-1854
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1864, Issue 10, October 2017, Pages 1844-1854
نویسندگان
Melania E. Zanchetta, Luisa M.R. Napolitano, Danilo Maddalo, Germana Meroni,