IndraLab

Statements

ABRAXAS2 affects BRCC3
10 | 27
ABRAXAS2 binds BRCC3.
10 | 21
BRCC3 binds ABRAXAS2. 10 / 34
10 | 21
reach
"These observations support the notion that the crystal structure of the BRCC36 and KIAA0157 heterodimer is reflective of both BRCC36-KIAA0157 and the BRCC36-Abraxas interactions in cells, and that perturbation of heterodimerization has far reaching consequences on the assembly of other subunits."
26344097
reach
"Structure of the BRCC36 and KIAA0157 heterodimer is functionally relevant in cells."
26344097
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
"However, and in contrast to insect Abro1 and BRCC36 complexes described previously, the human Abraxas and BRCC36 subcomplex behaved as a soluble aggregate that could not be further purified, but was, nonetheless, able to form a stable monodispersed and stoichiometric assembly when purified in combination with BRCC45 and MERIT40."
28009280
reach
"While the BRCC36 and KIAA0157 heterodimer structure was not determined in complex with K63-Ub 2, the K D for binding is 2 muM, the K M for K63-Ub 2 hydrolysis is 4 muM, and the substrate binding surfa[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28587922
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
biogrid
No evidence text available
22863883
biogrid
No evidence text available
19615732
reach
"Regardless, MALLS analysis of the reconstituted four-component BRCA1-A complex reported an apparent molecular mass of 280kDa (XREF_FIG B), suggestive of a dimer of Abraxas/BRCC36/BRCC45/MERIT40 heterotetramers and consonant with the " super-dimer " originally described for insect Abro1 and BRCC36 heterodimers."
28009280
reach
"To validate the BRCC36 and KIAA0157 heterodimer as being relevant in cells, we mutated direct contact residues and assessed interaction function of human BRCC36 and KIAA0157 by co-immunoprecipitation (see structure based sequence alignments in XREF_SUPPLEMENTARY and XREF_SUPPLEMENTARY for a list of equivalent residues mutated)."
26344097
ABRAXAS2 activates BRCC3.
| 6
ABRAXAS2 activates BRCC3. 6 / 8
| 6
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
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
"Mechanism by which KIAA0157 supports BRCC36 catalytic function."
26344097
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
"To understand how KIAA0157 supports the catalytic function of BRCC36, we set out to solve an inactive-state structure of BRCC36 in isolation."
26344097
BRCC3 affects ABRAXAS2
10 | 22
BRCC3 binds ABRAXAS2.
10 | 21
BRCC3 binds ABRAXAS2. 10 / 34
10 | 21
reach
"These observations support the notion that the crystal structure of the BRCC36 and KIAA0157 heterodimer is reflective of both BRCC36-KIAA0157 and the BRCC36-Abraxas interactions in cells, and that perturbation of heterodimerization has far reaching consequences on the assembly of other subunits."
26344097
reach
"Structure of the BRCC36 and KIAA0157 heterodimer is functionally relevant in cells."
26344097
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
"However, and in contrast to insect Abro1 and BRCC36 complexes described previously, the human Abraxas and BRCC36 subcomplex behaved as a soluble aggregate that could not be further purified, but was, nonetheless, able to form a stable monodispersed and stoichiometric assembly when purified in combination with BRCC45 and MERIT40."
28009280
reach
"While the BRCC36 and KIAA0157 heterodimer structure was not determined in complex with K63-Ub 2, the K D for binding is 2 muM, the K M for K63-Ub 2 hydrolysis is 4 muM, and the substrate binding surfa[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28587922
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
biogrid
No evidence text available
22863883
biogrid
No evidence text available
19615732
reach
"Regardless, MALLS analysis of the reconstituted four-component BRCA1-A complex reported an apparent molecular mass of 280kDa (XREF_FIG B), suggestive of a dimer of Abraxas/BRCC36/BRCC45/MERIT40 heterotetramers and consonant with the " super-dimer " originally described for insect Abro1 and BRCC36 heterodimers."
28009280
reach
"To validate the BRCC36 and KIAA0157 heterodimer as being relevant in cells, we mutated direct contact residues and assessed interaction function of human BRCC36 and KIAA0157 by co-immunoprecipitation (see structure based sequence alignments in XREF_SUPPLEMENTARY and XREF_SUPPLEMENTARY for a list of equivalent residues mutated)."
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