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RAP80 is a critical gatekeeper in impeding epithelial-mesenchymal transition-induced metastasis and malignant phenotypes of cancer as well as preserving DNA integrity.
Data suggest that RAP80 SIM (show SIM2 Proteins) (SUMO interacting motif) binds SUMO-2 (show SUMO2 Proteins); both specificity and affinity are enhanced through phosphorylation of canonical CK2 (show CSNK2A1 Proteins) (casein kinase 2) site within the SIM (show SIM2 Proteins).
Impaired TIP60 (show KAT5 Proteins)-mediated H4K16 acetylation accounts for the aberrant chromatin accumulation of 53BP1 (show TP53BP1 Proteins) and RAP80 in Fanconi anemia (show PALB2 Proteins) pathway-deficient cells.
TRAIP/RNF206 (show TRAIP Proteins) is required for recruitment of RAP80 to sites of DNA damage.(
A new role of FANCG in Homologous recombination repair of interstrand crosslinks through K63Ub-mediated interaction with the Rap80-BRCA1 complex.
patients with low RAP80 expression received gemcitabine/cisplatin, those with intermediate/high RAP80 expression and low/intermediate BRCA1 expression received docetaxel/cisplatin
Data indicate that a single point deletion (DeltaE81) in RAP80 abrogates multivalent interactions with polyubiquitin (show UBB Proteins).
connect ubiquitin- and SUMO-dependent DSB recognition, revealing that RNF4-synthesized hybrid SUMO-ubiquitin chains are recognized by RAP80 to promote BRCA1 recruitment and DNA repair.
post-translational phosphorylation of RAP80 by the Cdk1 (show CDK1 Proteins)-cyclin B(1) complex is important for RAP80 functional sensitivity to IR and G(2)/M checkpoint control.
Loss of RAP80 abolishes the recruitment of the BRCA1-A complex to DNA lesions in response to DNA damage.
Data indicate that RAP80-deficiency promotes genomic instability and causes an increase in cancer risk consistent with the concept that RAP80 exhibits a tumor suppressor function.
a model in which SUMO and Ub modification is coordinated to recruit Rap80 and BRCA1 to DNA damage sites.
Mechanistically, loss of RAP80 suppresses recruitment of the BRCA1-A complex to DNA damage sites and abrogates the DNA damage repair process at DNA damage sites.
Both ubiquitin-interacting motif 1(UIM1) and UIM2 of RAP80 recognize an Ile 44-centered hydrophobic patch on ubiquitin but neither UIM interacts with the Lys (show LYZ Proteins) 63-linked isopeptide bond. [RAP80]
Ubiquitin-binding protein that specifically recognizes and binds 'Lys-63'-linked ubiquitin. Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B\; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly Act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1 (By similarity).
ubiquitin interaction motif containing 1
, BRCA1-A complex subunit RAP80-like
, BRCA1-A complex subunit RAP80
, receptor-associated protein 80
, ubiquitin interaction motif-containing protein 1
, receptor associated protein 80
, retinoid X receptor-interacting protein 110
, retinoid x receptor interacting protein
, retinoid X receptor interacting protein 110