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The authors show that human Cyclin (show PCNA Proteins)-Dependent-Kinases (CDKs) target the RAD9 subunit of the 9-1-1 checkpoint clamp (show PDZK1 Proteins) on Thr292, to modulate DNA damage checkpoint activation. Thr292 phosphorylation on RAD9 creates a binding site for Polo-Like-Kinase1 (PLK1), which phosphorylates RAD9 on Thr313.
TLK1B mediated phosphorylation of Rad9 regulates its nuclear/cytoplasmic localization and cell cycle checkpoint
RAD9 has a prominent role in the ATR (show ANTXR1 Proteins)-Chk1 (show CHEK1 Proteins) 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 (show CHEK1 Proteins).
Intramolecular binding of the rad9 C-terminus in the checkpoint clamp (show PDZK1 Proteins) Rad9-Hus1 (show HUS1 Proteins)-Rad1 (show ERCC4 Proteins) 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 (show MUTYH Proteins).
Downregulation of RAD9 when combined with ionizing radiation results in reduction of ITGB1 (show ITGB1 Proteins) protein levels in prostate cancer cells, and increased lethality.
Loss of hrad9 expression is associated with breast and lung cancer.
Rad9a is indispensable for spermatogonia differentiation and testicular development in mice.
RAD9 has a prominent role in the ATR-Chk1 (show CHEK1 Proteins) 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 (show HUS1 Proteins) acts as a component of the canonical 9-1-1 complex during meiotic prophase I to promote DSB repair and further propose that RAD1 (show RAD1 Proteins) and TOPBP1 (show TOPBP1 Proteins) respond to unsynapsed chromatin through an alternative mechanism that does not require RAD9 or HUS1 (show HUS1 Proteins).
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.
MiR (show MYLIP Proteins)-2425-5p targets RAD9A and MYOG (show MYOG Proteins) to regulate the proliferation and differentiation of bovine skeletal muscle-derived satellite cells.
Data show that Rad17 (show RAD17 Proteins) mediates the interaction of the Rad9-Hus1 (show HUS1 Proteins)-Rad1 (show ERCC4 Proteins) (9-1-1) complex with the ATR-activating protein TopBP1 (show TOPBP1 Proteins) 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 (show TOPBP1 Proteins) and DNA polymerase-alpha directly recruit the 9-1-1 complex (rad9-rad1 (show ERCC4 Proteins)-Hus1 (show HUS1 Proteins)) 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