کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8300730 | 1537470 | 2018 | 36 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Catalytic domain mutation in CYLD inactivates its enzyme function by structural perturbation and induces cell migration and proliferation
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Tumor suppressor cylindromatosis protein (CYLD), which specifically cleaves lysine 63-linked ubiquitin chain from its substrate molecules, contributes to myriad of important cellular events including cellular differentiation, oncogenesis, DNA repair and cell cycle control. It is a ubiquitously expressed protein, which negatively regulates NF-kB and JNK signaling pathways and mediates caspase dependent apoptosis through RIP1 deubiqutination. Germline mutations in CYLD are associated with a rare, hypertrophic skin cancer, termed Familial Cylindromatosis. Catalogue of Somatic Mutations in Cancer database ensembles accumulating CYLD point mutations in multiple benign and malignant tumors. However, the functional role of CYLD mutations and their association with cancer progression remains elusive. In the present report, we have shown that cancer associated mutations impose structural alteration in CYLD which impairs its binding to K63 ubiquitin chain. Here, we conclude that loss of CYLD catalytic activity potentiates its oncogenic gain of function through increased cell survival and migration.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1862, Issue 9, September 2018, Pages 2081-2089
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1862, Issue 9, September 2018, Pages 2081-2089
نویسندگان
Tanu Johari, Tushar Kanti Maiti,