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Retinoblastoma binding protein 8

CtIP, RBBP8, CtBP-interacting protein
The protein encoded by this gene is a ubiquitously expressed nuclear protein. It is found among several proteins that bind directly to retinoblastoma protein, which regulates cell proliferation. This protein complexes with transcriptional co-repressor CTBP. It is also associated with BRCA1 and is thought to modulate the functions of BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. It is suggested that this gene may itself be a tumor suppressor acting in the same pathway as BRCA1. Three transcript variants encoding two different isoforms have been found for this gene. More transcript variants exist, but their full-length natures have not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Iris, Mre11, CAN, Atm, Rad50
Papers on CtIP
Structure of BRCA1-BRCT/Abraxas Complex Reveals Phosphorylation-Dependent BRCT Dimerization at DNA Damage Sites.
Blundell et al., Houston, United States. In Mol Cell, Feb 2016
BRCA1-BRCT domains bind to proteins containing the phosphorylated serine-proline-x-phenylalanine (pSPxF) motif including Abraxas, Bach1/FancJ, and CtIP.
TPP1 Blocks an ATR-Mediated Resection Mechanism at Telomeres.
de Lange et al., New York City, United States. In Mol Cell, Feb 2016
DSB resection is positively and negatively regulated by ATM signaling through CtIP/MRN and 53BP1-bound Rif1, respectively.
Hepatoma-derived growth factor-related protein 2 promotes DNA repair by homologous recombination.
Jäättelä et al., Copenhagen, Denmark. In Nucleic Acids Res, Jan 2016
Through its Pro-Trp-Trp-Pro (PWWP) domain, LEDGF/p75 binds to histone marks associated with active transcription and promotes DNA end resection by recruiting DNA endonuclease retinoblastoma-binding protein 8 (RBBP8/CtIP) to broken DNA ends.
Loss of CtIP disturbs homologous recombination repair and sensitizes breast cancer cells to PARP inhibitors.
Masutani et al., Tokyo, Japan. In Oncotarget, Jan 2016
CtIP (RBBP8) is a multifunctional protein that is involved in various cellular functions, including transcription, DNA replication, DNA repair and the G1 and G2 cell cycle checkpoints.
Systematic E2 screening reveals a UBE2D-RNF138-CtIP axis promoting DNA repair.
Jackson et al., Mainz, Germany. In Nat Cell Biol, Nov 2015
Mechanistically, UBE2Ds and RNF138 accumulate at DNA-damage sites and act at early resection stages by promoting CtIP ubiquitylation and accrual.
Biochemical mechanism of DSB end resection and its regulation.
Sung et al., New Haven, United States. In Dna Repair (amst), Aug 2015
Topics addressed will include how resection initiates via the introduction of an endonucleolytic incision close to the break end, the molecular mechanism of the conserved MRE11 complex in conjunction with Sae2/CtIP within such a model, the role of BRCA1 and 53BP1 in regulating resection initiation in mammalian cells, the influence of chromatin in the resection process, and potential roles of novel factors.
CtIP: A DNA damage response protein at the intersection of DNA metabolism.
Paull et al., Austin, United States. In Dna Repair (amst), Aug 2015
The mammalian CtIP protein and its orthologs in other eukaryotes promote the resection of DNA double-strand breaks and are essential for meiotic recombination.
MAD2L2 controls DNA repair at telomeres and DNA breaks by inhibiting 5' end resection.
Jacobs et al., Amsterdam, Netherlands. In Nature, Jun 2015
Consistent with MAD2L2 promoting NHEJ-mediated telomere fusion by inhibiting 5' end resection, knockdown of the nucleases CTIP or EXO1 partially restores telomere-driven genomic instability in MAD2L2-depleted cells.
REV7 counteracts DNA double-strand break resection and affects PARP inhibition.
Rottenberg et al., Amsterdam, Netherlands. In Nature, Jun 2015
Here we show that loss of REV7 (also known as MAD2L2) in mouse and human cell lines re-establishes CTIP-dependent end resection of DSBs in BRCA1-deficient cells, leading to HR restoration and PARP inhibitor resistance, which is reversed by ATM kinase inhibition.
Envisioning the dynamics and flexibility of Mre11-Rad50-Nbs1 complex to decipher its roles in DNA replication and repair.
Tainer et al., Berkeley, United States. In Prog Biophys Mol Biol, Mar 2015
One of them, CtIP, modulates the Mre11 excision activity for homologous recombination repair.
Genome-wide scan for selection signatures in six cattle breeds in South Africa.
Maiwashe et al., South Africa. In Genet Sel Evol, 2014
In addition, a number of candidate genes associated with the nervous system (WNT5B, FMOD, PRELP, and ATP2B), immune response (CYM, CDC6, and CDK10), production (MTPN, IGFBP4, TGFB1, and AJAP1) and reproductive performance (ADIPOR2, OVOS2, and RBBP8) were also detected as being under selection.
53BP1 regulates DSB repair using Rif1 to control 5' end resection.
de Lange et al., New York City, United States. In Science, 2013
Rif1 inhibits resection involving CtIP, BLM, and Exo1; limits accumulation of BRCA1/BARD1 complexes at sites of DNA damage; and defines one of the mechanisms by which 53BP1 causes chromosomal abnormalities in Brca1-deficient cells.
The yeast Fun30 and human SMARCAD1 chromatin remodellers promote DNA end resection.
Llorente et al., Leiden, Netherlands. In Nature, 2012
In yeast, the Mre11-Rad50-Xrs2 complex (Xrs2 is known as NBN or NBS1 in humans) and Sae2 (known as RBBP8 or CTIP in humans) initiate end resection, whereas long-range resection depends on the exonuclease Exo1, or the helicase-topoisomerase complex Sgs1-Top3-Rmi1 together with the endonuclease Dna2 (refs 1-6).
CtIP-dependent DNA resection is required for DNA damage checkpoint maintenance but not initiation.
Sørensen et al., Copenhagen, Denmark. In J Cell Biol, 2012
show that CHK1 was rapidly and robustly activated before detectable end resection
CtIP protein dimerization is critical for its recruitment to chromosomal DNA double-stranded breaks.
Wu et al., Los Angeles, United States. In J Biol Chem, 2012
The severe repair defects of CtIP dimerization mutants are likely due to the failure in localization to chromosomal DSBs upon DNA damage.
Mre11 regulates CtIP-dependent double-strand break repair by interaction with CDK2.
Ferguson et al., Ann Arbor, United States. In Nat Struct Mol Biol, 2012
The authors show that, in human and mouse, Mre11 controls these events through a direct interaction with CDK2 that is required for CtIP phosphorylation and BRCA1 interaction in normally dividing cells.
Regulatory networks integrating cell cycle control with DNA damage checkpoints and double-strand break repair.
Russell et al., Los Angeles, United States. In Philos Trans R Soc Lond B Biol Sci, 2012
Central to this regulation are the proteins that initiate the processing of DNA ends for HR repair, Mre11-Rad50-Nbs1 protein complex and Ctp1/Sae2/CtIP, and the checkpoint kinases Tel1/ATM and Rad3/ATR.
CtIP Mutations Cause Seckel and Jawad Syndromes.
Børglum et al., Århus, Denmark. In Plos Genet, 2011
the SCKL2 mutation creates an alternative splicing site leading to both the normal and aberrant CtIP proteins coexisting in the cells of patients and carriers
H2AX prevents CtIP-mediated DNA end resection and aberrant repair in G1-phase lymphocytes.
Sleckman et al., United States. In Nature, 2011
the histone protein H2AX prevents nucleases other than Artemis from processing hairpin-sealed coding ends; in the absence of H2AX, CtIP can efficiently promote the hairpin opening and resection of DNA ends generated by RAG cleavage
Making the best of the loose ends: Mre11/Rad50 complexes and Sae2 promote DNA double-strand break resection.
Paull, Austin, United States. In Dna Repair (amst), 2011
This review focuses on the Mre11/Rad50/Xrs2(Nbs1) complex and the Sae2(CtIP) protein and their roles in initiating both short-range and long-range resection, the effects of topoisomerase-DNA conjugates on resection in vivo, and the relationship between these factors and NHEJ proteins in regulating 5' strand resection in eukaryotic cells.
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