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TLK1B mediated phosphorylation of Rad9 regulates its nuclear/cytoplasmic localization and cell cycle checkpoint
RAD9 has a prominent role in the ATR (Montrer ANTXR1 Protéines)-Chk1 (Montrer CHEK1 Protéines) pathway that is necessary for successful formation of the damage-sensing complex and DNA damage checkpoint signaling.
these results demonstrate a positive feedback loop involving Rad9A-dependend activation of Chk1 (Montrer CHEK1 Protéines).
Intramolecular binding of the rad9 C-terminus in the checkpoint clamp (Montrer PDZK1 Protéines) Rad9-Hus1 (Montrer HUS1 Protéines)-Rad1 is closely linked with its DNA binding.
The role of Rad9 in homologous recombination is independent of its function in checkpoint activation, and this function is important for preventing alternative non-homologous end joining.
we found that H1299 cells with reduced RAD9 protein levels showed a higher frequency of radiation induced bystander micronuclei formation
These data reveal that human Rad9 interacts directly with N-terminal region of human MYH (Montrer MUTYH Protéines).
Downregulation of RAD9 when combined with ionizing radiation results in reduction of ITGB1 (Montrer ITGB1 Protéines) protein levels in prostate cancer cells, and increased lethality.
Loss of hrad9 expression is associated with breast and lung cancer.
These data suggest that v-Src (Montrer SRC Protéines) attenuates ATR (Montrer ANTXR1 Protéines)-Chk1 (Montrer CHEK1 Protéines) signaling through the inhibition of Rad17 (Montrer RAD17 Protéines)-Rad9 interaction.
RAD9 has a prominent role in the ATR-Chk1 (Montrer CHEK1 Protéines) pathway that is necessary for successful formation of the damage-sensing complex and DNA damage checkpoint signaling.
We demonstrated that Mrad9 null enhances chromatid aberration frequency induced by radiation in bystander mouse embryonic stem cells
RAD9A is essential for male fertility and for repair of DNA double-strand breaks during meiotic prophase I.
HUS1 (Montrer HUS1 Protéines) acts as a component of the canonical 9-1-1 complex during meiotic prophase I to promote DSB repair and further propose that RAD1 (Montrer RAD1 Protéines) and TOPBP1 (Montrer TOPBP1 Protéines) respond to unsynapsed chromatin through an alternative mechanism that does not require RAD9 or HUS1 (Montrer HUS1 Protéines).
A review of the many activities assigned to Rad9, and speculation as to which influence its function in tumor development.
Data show that Rad9 plays dual roles in generating functional antibodies and in maintaining the integrity of the whole genome in B cells.
Rad9A-mediated Claspin localization is a vital step during checkpoint activation.
tousled-like kinases play important roles in DNA repair, not only by modulation of chromatin assembly via Asf1, but also by a more direct function in processing the ends of a tousled-like kinase via interaction with Rad9.
HRAD9 and Mrad9 are part of a gene family and reveal a new genetic element encoding a product that interacts with multiple, known cell cycle checkpoint control proteins.
Results establish mouse rad9 as a key mammalian genetic element of pathways that regulate the cellular response to DNA damage, maintenance of genomic integrity, and proper embryonic development.
Data show that Rad17 (Montrer RAD17 Protéines) mediates the interaction of the Rad9-Hus1 (Montrer HUS1 Protéines)-Rad1 (9-1-1) complex with the ATR-activating protein TopBP1 (Montrer TOPBP1 Protéines) in Xenopus egg extracts.
interaction of the 9-1-1 complex (Rad9-Hus1-Rad1) with the BRCT I-II region of TopBP1 is necessary for binding of ATR-ATRIP to the ATR-activating domain of TopBP1 and the ensuing activation of ATR
TopBP1 (Montrer TOPBP1 Protéines) and DNA polymerase-alpha directly recruit the 9-1-1 complex (rad9-rad1-Hus1 (Montrer HUS1 Protéines)) to stalled DNA replication forks.
This gene product is highly similar to Schizosaccharomyces pombe rad9, a cell cycle checkpoint protein required for cell cycle arrest and DNA damage repair. This protein possesses 3' to 5' exonuclease activity, which may contribute to its role in sensing and repairing DNA damage. It forms a checkpoint protein complex with RAD1 and HUS1. This complex is recruited by checkpoint protein RAD17 to the sites of DNA damage, which is thought to be important for triggering the checkpoint-signaling cascade. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
DNA repair exonuclease rad9 homolog A
, cell cycle checkpoint control protein RAD9A
, RAD9 homolog A (S. pombe)
, cell cycle checkpoint control protein RAD9A-like
, Rad9-like protein
, RAD9 homolog A
, PCNA-like DNA checkpoint protein Rad9
, RAD9 checkpoint clamp component A L homeolog