IndraLab

Statements


CYLD binds USP. 9 / 9
| 9

sparser
"Strikingly, the SPATA2 PUB domain (aa 1–241, 27.6 kDa), a monomer on its own (26.6 kDa), formed a 2:2 complex with dimeric CYLD USP domain of 136 kDa (calculated 140 kDa) in SEC-MALS ( xref A)."

sparser
"Although the conserved CAP-GLY domains provide structural basis for the interactions of CYLD with microtubules and many other proteins, an interesting finding is that EB1 containing a known CAP-GLY domain-interacting motif interacts with the C-terminal USP domain of CYLD other than the CAP-GLY domains, implicating a previously unknown role for the USP domain in mediating protein-protein interactions."

sparser
"The interaction with CYLD is mediated by the adaptor protein Spermatogenesisassociated 2 (SPATA2) [31, [33] [34] [35] , which interacts with the CYLD USP domain and contains a PIM that facilitates binding to the HOIP PUB domain [31] (Fig. 1 )."

sparser
"The interaction with CYLD is mediated by the adaptor protein Spermatogenesis-associated 2 (SPATA2) [31, 33–35], which interacts with the CYLD USP domain and contains a PIM that facilitates binding to the HOIP PUB domain [31] (Fig. 1)."

sparser
"The interaction with CYLD is mediated by the adaptor protein Spermatogenesis-associated 2 (SPATA2) [ xref , xref – xref ], which interacts with the CYLD USP domain and contains a PIM that facilitates binding to the HOIP PUB domain [ xref ] (Fig.  xref )."

sparser
"It has been shown that the USP domain of CYLD binds the PUB domain of spermatogenesis-associated protein 2 (Spata2) ( xref ), leading to recruitment of CYLD to the centrosome and de-ubiquitination of Plk4."

sparser
"SPATA2 contains both a PIM sequence, which is tightly bound by HOIP-PUB, and also a PUB domain on its own, which cannot bind a canonical PIM sequence but was found to interact with the ubiquitin-specific protease (USP) domain of CYLD [ xref , xref ]."

sparser
"TNF-α stimulation also induces rapid ubiquitylation of components of the TNF-RSC Temporal analysis of the TNF-RSC composition identified SPATA2 as a novel component of the TNF-RSC The predicted PUB domain in the N-terminus of SPATA2 interacts with the USP domain of CYLD, whereas the C-terminus of SPATA2 interacts with HOIP SPATA2 is required for recruitment of CYLD to the TNF-RSC Downregulation of SPATA2 augments transcriptional activation of NF-κB and inhibits TNF-α-induced necroptosis, pointing to an important function of SPATA2 in modulating the outcomes of TNF-α signaling."

sparser
"Moreover, Nox4 was deubiquitinated via a direct interaction with the ubiquitin-specific protease domain of CYLD."