کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8322197 | 1539864 | 2016 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
TRIM32 ubiquitin E3 ligase, one enzyme for several pathologies: From muscular dystrophy to tumours
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کلمات کلیدی
TNFαRetinoic acid receptor alphaPIASSUMOHEKLGMDSTMNDRG2N-myc downstream regulated gene 2MuRF1TRIMRARαXIAPNFκB - NFKBtripartite motif - الگوی سه گانهmuscle RING finger 1 - انگشت رینگ عضلانی 1tumor necrosis factor alpha - تومور نکروز عامل آلفاRing - حلقهLimb-girdle muscular dystrophy - دیستروفی عضلانی کمربند کمربندCancer - سرطانnuclear factor kappa B - فاکتور هسته ای کاپا BX-linked inhibitor of apoptosis - مهارکننده آپوپتوز X مرتبط با آنprotein inhibitor of activated Stat - مهارکننده پروتئین فعال شدهProteasome - پروتئازومreally interesting new gene - ژن جدید واقعا جالبhuman embryonic kidney - کلیه جنین انسان
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
TRIM32 is a member of the TRIpartite Motif family characterised by the presence of an N-terminal three-domain-module that includes a RING domain, which confers E3 ubiquitin ligase activity, one or two B-box domains and a Coiled-Coil region that mediates oligomerisation. Several TRIM32 substrates were identified including muscular proteins and proteins involved in cell cycle regulation and cell motility. As ubiquitination is a versatile post-translational modification that can affect target turnover, sub-cellular localisation or activity, it is likely that diverse substrates may be differentially affected by TRIM32-mediated ubiquitination, reflecting its multi-faceted roles in muscle physiology, cancer and immunity. With particular relevance for muscle physiology, mutations in TRIM32 are associated with autosomal recessive Limb-Girdle Muscular Dystrophy 2H, a muscle-wasting disease with variable clinical spectrum ranging from almost asymptomatic to wheelchair-bound patients. In this review, we will focus on the ability of TRIM32 to mark specific substrates for proteasomal degradation discussing how the TRIM32-proteasome axis may (i) be important for muscle homeostasis and for the pathogenesis of muscular dystrophy; and (ii) define either an oncogenic or tumour suppressive role for TRIM32 in the context of different types of cancer.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 79, October 2016, Pages 469-477
Journal: The International Journal of Biochemistry & Cell Biology - Volume 79, October 2016, Pages 469-477
نویسندگان
Elisa Lazzari, Germana Meroni,