Gli1‐induced deubiquitinase USP 48 aids glioblastoma tumorigenesis by stabilizing Gli1
نویسندگان
چکیده
منابع مشابه
Wnt signaling stimulates transcriptional outcome of the Hedgehog pathway by stabilizing GLI1 mRNA.
Wnt and Hedgehog signaling pathways play central roles in embryogenesis, stem cell maintenance, and tumorigenesis. However, the mechanisms by which these two pathways interact are not well understood. Here, we identified a novel mechanism by which Wnt signaling pathway stimulates the transcriptional output of Hedgehog signaling. Wnt/beta-catenin signaling induces expression of an RNA-binding pr...
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Ribosome biogenesis dictates the translational capacity of cells. Several mechanisms establish and maintain transcriptional output from eukaryotic ribosomal DNA (rDNA) loci. rDNA silencing is one such mechanism that ensures the inactivity and hence the maintenance of a silenced state of a subset of rRNA gene copies. Whereas oncogenic agents stimulate rRNA gene transcription, tumor suppressors d...
متن کاملPolyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21 Supplementary Material
Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, UK Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 303222, USA Section of Structural Biology, The Institute of Cancer Research, 237 Fulham Road, London, UK $ Current address: Laboratory of Biochemistry and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20...
متن کاملE1-mediated recruitment of a UAF1-USP deubiquitinase complex facilitates human papillomavirus DNA replication.
UNLABELLED The human papillomavirus (HPV) E1 helicase promotes viral DNA replication through its DNA unwinding activity and association with host factors. The E1 proteins from anogenital HPV types interact with the cellular WD repeat-containing factor UAF1 (formerly known as p80). Specific amino acid substitutions in E1 that impair this interaction inhibit maintenance of the viral episome in im...
متن کاملPolyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21.
Modification of proteins by ubiquitin (Ub) and Ub-like (Ubl) modifiers regulates a variety of cellular functions. The ability of Ub to form chains of eight structurally and functionally distinct types adds further complexity to the system. Ub-specific proteases (USPs) hydrolyse polyUb chains, and some have been suggested to be cross-reactive with Ubl modifiers, such as neural precursor cell exp...
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ژورنال
عنوان ژورنال: EMBO reports
سال: 2017
ISSN: 1469-221X,1469-3178
DOI: 10.15252/embr.201643124