IndraLab

Statements

ABRAXAS2 affects BRCC3
19 | 35
ABRAXAS2 binds BRCC3.
19 | 25
BRCC3 binds ABRAXAS2. 10 / 47
19 | 25
reach
"Moreover, besides interacting with CCDC98 within the BRCA1-A complex, BRCC36 also associates with another protein KIAA0157, which shares significant sequence homology with CCDC98."
20656690
reach
"The association between ABRAXAS2 and BRCC3 and NLRP3 depends on the phosphorylation of NLRP3 serine 194 and the NLRP3 interactor NIMA-related kinase 7 (NEK7), which acts as a scaffold for bridging adjacent NLRP3 subunits and requires proposed priming [124,125]."
36551253
reach
"Structural studies indicate that BRCC36 and ABRAXAS2 or ABRO1 form heterodimers, which ensure enzymatic activity and association with additional cofactors including RAP80 and BRCA1 (in the BRCA1-A complex) or the serine hydroxymethyltransferase 2 (SHMT2) (in the BRISC complex) (107, 108, 109)."
35764170
reach
"Finally, we also show that Abro1, another BRISC subunit, binds directly to Brcc36 and that the Brcc36 and Abro1 heterodimer includes a minimal complex with Lys (63)-specific DUB activity."
20032457
reach
"This mechanism is homologous to what has been observed in the ancestral BRCC36-KIAA0157 complex (Zeqiraj et al., 2015) but is distinct from that seen in the COP9 signalosome (CSN) and the proteasome lid, where the position of the scaffold MPN domain differs (Figure S3B) (Lingaraju et al., 2014, Pathare et al., 2014, Worden et al., 2014, Worden et al., 2017)."
31253574
reach
"Based on current reports, JAMM subunit interfaces are surprisingly diverse in structure and have a variety of roles including function in : i) the assembly of multisubunit complexes and ii) maintaining the JAMM and MPN+ domain in an active state, as in the BRCC36 and KIAA0157 heterodimer."
28479062
reach
"Furthermore, Abro1 binding to BRCC36 promotes the catalytic activity of the enzyme, although this heterodimer has minimal activity when compared to the complete four-subunit BRISC complex [XREF_BIBR, XREF_BIBR, XREF_BIBR]."
21195082
reach
"To understand the basis for BRCC36 regulation, we have solved the structure of an active BRCC36 and KIAA0157 heterodimer and an inactive BRCC36 homodimer."
26344097
reach
"Towards this end, we have characterized the binding architecture of BRISC and ARISC complexes and solved the X-ray crystal structures of the minimally active BRCC36 and KIAA0157 heterodimer subcomplex, and an inactive BRCC36-BRCC36 homodimer complex."
26344097
reach
"Comparison of the BRCC36 and KIAA0157 heterodimer structure with an inactive BRCC36 homodimer structure provides a model for understanding how this functional interplay is achieved."
26344097
ABRAXAS2 activates BRCC3.
| 9
ABRAXAS2 activates BRCC3. 9 / 11
| 9
reach
"Mechanism by which KIAA0157 supports BRCC36 catalytic function."
26344097
reach
"We pursued crystallization of BRCC36-KIAA0157 subcomplexes from different species (H. sapiens, G. gallus, X. tropicalis, D. rerio, C. floridanus and A. thaliana) to determine the structural basis for (1) how KIAA0157 supports the catalytic function of BRCC36, and (2) how super dimerization of the minimally active BRCC36 and KIAA0157 heterodimer is mediated."
26344097
reach
"To understand how KIAA0157 supports the catalytic function of BRCC36, we set out to solve an inactive-state structure of BRCC36 in isolation."
26344097
reach
"Abraxas brother 1 (ABRO1), a subunit of the BRCA1/BRCA2-containing complex subunit 36 (BRCC36) isopeptidase complex (BRISC), impedes WW domain-containing E3 ubiquitin-protein ligase 2 (WWP2)-mediated BRCC3 ubiquitination and increases BRCC3 stability [69]."
37047097
reach
"Interestingly, although CCDC98 functions as an adaptor of BRCC36 and regulates BRCC36 activity in the nucleus, KIAA0157 mainly localizes in cytosol and activates BRCC36 in the cytoplasm."
20656690
reach
"This likely reflects the fact that the mechanism by which KIAA0157 and Abraxas support BRCC36 will differ from how CSN6 and RPN8 support and regulate the function of CSN5 and RPN11."
26344097
reach
"BRCC36 is activated in the BRCA1-A complex by the MPN domain protein ABRAXAS and in BRISC particles by the MPN domain protein ABRO1 (Rabl, 2020)."
39600336
reach
"Many studies have shown that deficiency of ABRO1 substantially reduced the protein levels of the other components of BRISC, especially BRCC3 [23–25]."
37968261
reach
"Previous structural studies have clearly shown how the BRISC subunit Abro1 binds to and allosterically activates the DUB activity of BRCC36 and how this heterodimer further self-associates to form a " superdimeric " assembly."
28009280
ABRAXAS2 inhibits BRCC3.
| 1
ABRAXAS2 inhibits BRCC3. 1 / 1
| 1
reach
"Further investigations elucidated that ABRAXAS2 degradation triggered the subsequent degradation of adjacent BRCC3, which in turn, hindered TNIP1/ABIN1 degradation, ultimately inhibiting NFKB/NF-κB (nuclear factor kappa B)-mediated inflammatory responses."
40013521
BRCC3 affects ABRAXAS2
19 | 26
BRCC3 binds ABRAXAS2.
19 | 25
BRCC3 binds ABRAXAS2. 10 / 47
19 | 25
reach
"Moreover, besides interacting with CCDC98 within the BRCA1-A complex, BRCC36 also associates with another protein KIAA0157, which shares significant sequence homology with CCDC98."
20656690
reach
"The association between ABRAXAS2 and BRCC3 and NLRP3 depends on the phosphorylation of NLRP3 serine 194 and the NLRP3 interactor NIMA-related kinase 7 (NEK7), which acts as a scaffold for bridging adjacent NLRP3 subunits and requires proposed priming [124,125]."
36551253
reach
"Structural studies indicate that BRCC36 and ABRAXAS2 or ABRO1 form heterodimers, which ensure enzymatic activity and association with additional cofactors including RAP80 and BRCA1 (in the BRCA1-A complex) or the serine hydroxymethyltransferase 2 (SHMT2) (in the BRISC complex) (107, 108, 109)."
35764170
reach
"Finally, we also show that Abro1, another BRISC subunit, binds directly to Brcc36 and that the Brcc36 and Abro1 heterodimer includes a minimal complex with Lys (63)-specific DUB activity."
20032457
reach
"This mechanism is homologous to what has been observed in the ancestral BRCC36-KIAA0157 complex (Zeqiraj et al., 2015) but is distinct from that seen in the COP9 signalosome (CSN) and the proteasome lid, where the position of the scaffold MPN domain differs (Figure S3B) (Lingaraju et al., 2014, Pathare et al., 2014, Worden et al., 2014, Worden et al., 2017)."
31253574
reach
"Based on current reports, JAMM subunit interfaces are surprisingly diverse in structure and have a variety of roles including function in : i) the assembly of multisubunit complexes and ii) maintaining the JAMM and MPN+ domain in an active state, as in the BRCC36 and KIAA0157 heterodimer."
28479062
reach
"Furthermore, Abro1 binding to BRCC36 promotes the catalytic activity of the enzyme, although this heterodimer has minimal activity when compared to the complete four-subunit BRISC complex [XREF_BIBR, XREF_BIBR, XREF_BIBR]."
21195082
reach
"To understand the basis for BRCC36 regulation, we have solved the structure of an active BRCC36 and KIAA0157 heterodimer and an inactive BRCC36 homodimer."
26344097
reach
"Towards this end, we have characterized the binding architecture of BRISC and ARISC complexes and solved the X-ray crystal structures of the minimally active BRCC36 and KIAA0157 heterodimer subcomplex, and an inactive BRCC36-BRCC36 homodimer complex."
26344097
reach
"Comparison of the BRCC36 and KIAA0157 heterodimer structure with an inactive BRCC36 homodimer structure provides a model for understanding how this functional interplay is achieved."
26344097
BRCC3 activates ABRAXAS2.
| 1
BRCC3 activates ABRAXAS2. 1 / 1
| 1
reach
"Like many other members of this family, BRCC36 is activated though pairing with a partner protein containing an inactive MPN domain (MPN -), Abraxas in BRCA1-A, and Abro1 in BRISC."
28009280