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Data indicate that HR23A protein-depleted cells exhibit enhanced autophagy when treated with DNA-damaging agents.
HR23A role in DNA reapair, in protein degradation and stability, tumorigenesis and neurodegenerative disorders [review]
hHR23A associates with Chk1 through its ubiquitin-associated domains, and knockdown of hHR23A increases and stabilizes the protein level of Chk1 and its phosphorylation at S347.
Data indicate that phosphorylation provides a mechanism to regulate Rad23/proteasome interaction.
Here, we show that hHR23A utilizes both the UBA2 and XPCB domains to form a stable complex with Vpr, linking Vpr directly to cellular DNA repair pathways and their probable exploitation by the virus.
this study identified RAD23A as a novel negative regulator of RIG-I/MDA5 mediated anti-virus response.
Determined is the three-dimensional structure of its ubiquitin-like (UbL) domain by X-ray crystallography.
Vpr promotes hHR23A-mediated protein-ubiquitination, and down-regulation of hHR23A using RNAi significantly reduced viral replication in non-proliferating MAGI-CCR5 cells and primary macrophages
involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination
structures of the UBA domains of HHR23A reveal a conserved hydrophobic surface for protein-protein interactions
the solution structures of the HHR23A Ubl domain
Adopts a closed conformation and binds to the proteasomal subunit S5a thereby changing its own conformation.
hHR23 binds to polyubiquitylated p53 via its carboxyl-terminal ubiquitin-associated (Uba) domain shielding p53 from deubiquitylation
Data suggest that the UBL domain of HHR23A negatively regulates polyubiquitin/UBA interactions and identify leucine 8 of ubiquitin as an important determinant of chain recognition.
hHR23A regulates the function of xeroderma pigmentosum C by its association with the nucleotide excision repair activator p53
Ufd4, the E3 component of the UFD pathway, is involved in controlling the degradation of Rad4, and Ufd4 and Rad23 exhibit a synthetic inhibitory effect on Rad4 degradation
hHR23B thus plays a critical role in the activation and function of p53 after specific genotoxic exposures.
hHR23a and hPLIC2 interact via UBL/UBA domain interactions
UIM2 domain of S5a binds preferentially to hHR23a over polyubiquitin, and a model is provided for the ternary complex that represents one of the mechanisms used by the proteasome to capture ubiquitylated substrates.
Pyramidal crystals of the UbL domain of hHR23A were diffracted to beyond 2 A resolution and the structure was solved by molecular replacement.
data demonstrate that sequestration and impairment of nuclear HR23 and nucleocytoplasmic transport proteins is an outcome of, and a contributor to, poly(GA) pathology.
the mammalian RAD23 proteins play a direct role in damage recognition by enhancing the binding of XPC to DNA damage in living cells in addition to stabilizing XPC. RAD23 proteins rapidly dissociated from XPC upon binding to damaged DNA.
analysis of mHR23A/B double-mutant cells showed that HR23 proteins function in nucleotide excision repair by governing xeroderma pigmentosum group C protein stability via partial protection against proteasomal degradation
The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in nucleotide excision repair. Proteins in this family have a modular domain structure consisting of an ubiquitin-like domain (UbL), ubiquitin-associated domain 1 (UbA1), XPC-binding domain and UbA2. The protein encoded by this gene plays an important role in nucleotide excision repair and also in delivery of polyubiquitinated proteins to the proteasome. Alternative splicing results in multiple transcript variants encoding multiple isoforms.
RAD23 homolog A
, UV excision repair protein RAD23 homolog A
, RAD23 homolog A (S. cerevisiae)
, RAD23, yeast homolog, A