WebSep 15, 2024 · Here, we show that a Spata2-like protein, Spata2L, can also form a complex with CYLD to inhibit the TLR4-dependent inflammatory response. We found that Spata2L … WebJun 17, 2024 · The deubiquitinase CYLD in complex with SPATA2 is recruited to receptor signaling complexes by the ubiquitin ligase LUBAC and regulates Met1- and Lys63-linked polyubiquitin and receptor signaling outcomes ... Macromolecules Find similar proteins by: (by identity cutoff) 3D Structure Find similar proteins by: (by identity cutoff) 3D Structure
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WebAug 30, 2016 · Here, we identify SPATA2 as a constitutive direct binding partner of HOIP that bridges the interaction between CYLD and HOIP. SPATA2 recruitment to TNFR1- … WebNov 19, 2024 · Since SPATA2 enhances the deubiquitination activity of CYLD [9, 10], and CYLD had been shown to deubiquitinate RIPK1 , the presence of SPATA2 can promote …
WebJun 17, 2024 · The deubiquitinase CYLD in complex with SPATA2 is recruited to receptor signaling complexes by the ubiquitin ligase LUBAC and regulates Met1- and Lys63-linked polyubiquitin and receptor signaling outcomes. Here, we investigate the molecular determinants of CYLD activity. We reveal that two CAP-Gly domains in CYLD are … WebJul 18, 2016 · SPATA2 Links CYLD to LUBAC, Activates CYLD, and Controls LUBAC Signaling. Elliott, P.R. , Leske, D. , Hrdinka, M. , Bagola, K. , Fiil, B.K. , McLaughlin, S.H. , Wagstaff, J. , Volkmar, N. , Christianson, J.C. , Kessler, B.M. , Freund, S.M. , Komander, D. , Gyrd-Hansen, M. (2016) Mol Cell 63: 990-1005
WebIn cells, SPATA2 is recruited to the TNF receptor 1 signaling complex and is required for CYLD recruitment. Loss of SPATA2 increases ubiquitination … WebAug 30, 2016 · We here show that CYLD interacts with HOIP via spermatogenesis-associated protein 2 (SPATA2). SPATA2 interacts with CYLD through its non-canonical PUB domain, which binds the catalytic CYLD USP domain in a CYLD B-box-dependent manner. Significantly, SPATA2 binding activates CYLD-mediated hydrolysis of ubiquitin …
WebAug 17, 2016 · Specifically, the ability of SPATA2 to interact with CYLD promotes the assembly of a complex consisting of a hetero-tetramer which then interacts with two LUBAC complexes by means of HOIP [9,10,12].
http://genesdev.cshlp.org/content/early/2024/07/12/gad.299776.117.full.pdf ctrl f search div scrollbarWebDec 1, 2024 · There are reports that spermatogenesis-associated protein 2 (SPATA2) acts as an allosteric activator for CYLD. SPATA2 interacts via its PUB domain with CYLD, which activates the deubiquitinase activity of CYLD [18]. Thus, it is likely that the SPATA2/CYLD pathway plays an important role in regulation of doxorubicin-induced ferritinophagy. earth\\u0027s climate past and future pdfWebLoss of SPATA2 impairs the recruitment of CYLD to com- plex I and preserves the M1-Ubi of RIPK1; as a conse- quence, RIPK1 activation is impaired ( Hitomi et al. 2008;Moquin et al. 2013;Draber et ... ctrl f search wildcardWebJun 15, 2016 · SPATA2 binds CYLD and HOIP, and SPATA2 knockdown abolishes the TNF-α-dependent recruitment of CYLD. The PUB domain in the N-terminus of SPATA2 interacts with the C-terminal USP domain of CYLD. SPATA2 knockdown increases TNF-α-induced NF-κB activation and impairs necroptosis. Introduction ctrl f searchWebMar 31, 2024 · CYLD contains three cytoskeleton-associated protein glycine-rich (CAP-Gly) domains that mediate microtubule binding, two proline-rich (PR) motifs and the USP domain harboring its DUB activity.... ctrl f search exact matchWebAug 14, 2003 · CYLD, a tumour suppressor that is mutated in familial cylindromatosis, interacts with NEMO, the regulatory subunit of IKK, strengthening the notion that ubiquitination is involved in IKK activation by TRAFs and suggesting that CYLD functions in this process. NF-κB transcription factors have key roles in inflammation, immune … earth\u0027s climate past and future pdfWebOct 5, 2024 · CYLD is a comparably well-studied DUB in terms of its activity, specificity, and regulation. It is an unusual and divergent member of the Ub-specific protease (USP) family of DUBs, since its structurally distinct USP domain preferentially hydrolyses Met1- and Lys63-Ub ( Komander et al., 2008, 2009; Sato et al., 2015 ). ctrl f smartphone