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Lead Time
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Usage
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.
Gene References into Functions
results provide insights into the structure of the Rev1/Polzeta TLS assembly and highlight the function of Rev7 homo- and heterodimerization.PMID:30111544
Skp2, a confirmed APC/C-CDH1 substrate and E-cadherin destroyer, was increased in TGF-beta1-treated proximal tubular epithelial cells, which could be blocked by MAD2B depletion.PMID:27488450
structure-based interaction analyses revealed an unprecedented mechanism involving CAMP's WK motif. Surprisingly, in one of the crystal forms, the MAD2L2-CAMP complex formed a dimeric structure in which the C-terminal region of MAD2L2 was swapped and adopted an immature structurePMID:28887307
REV7 is a previously undescribed FA gene, which we term FANCVPMID:27500492
Knockdown of REV7 inhibited the migration, invasion, and epithelial-mesenchymal transition (EMT) of breast cancer cells. Meanwhile, overexpression of REV7 promoted the migration, invasion, and EMT of breast cancer cells.PMID:27712588
hMAD2 also binds to the hREV7-binding sequence in hREV3, whereas hMAD2 does not bind to a similar sequence in ADAM9 or ELK-1 and hREV7 does not bind to the hMAD2-binding sequence in hMAD1 or hCDC20.PMID:20088965
data establish MAD2L2 as a crucial contributor to the control of DNA repair activity by 53BP1 that promotes NHEJ by inhibiting 5' end resection downstream of RIF1PMID:25799990
results reveal an unexpected crucial function of REV7 downstream of 53BP1 in coordinating pathological DSB repair pathway choices in BRCA1-deficient cellsPMID:25799992
that MAD2B may play an important role in high glucose-mediated podocyte injury of diabetic nephropathy via modulation of Cdh1, cyclin B1, and Skp2 expressionPMID:25651564
Rev7 is essential for mutagenesis and S phase progression in UV-irradiated fibroblasts.PMID:18295554
These findings indicate that depletion of REV7 enhances sensitivity to cisplatin treatment in ovarian clear cell carcinoma (CCC), suggesting that REV7 is a candidate molecular target in CCC management.PMID:24597627
MAD2L2 helps to ensure a robustly bistable switch between APC/C(CDC20) and APC/C(CDH1) during the metaphase-to-anaphase transition, thereby contributing to mitotic fidelity.PMID:24100295
REV7 is required for anaphase-promoting complex-dependent ubiquitination and degradation of translesion DNA polymerase REV1.PMID:23287467
MAD2B may mediate Sim2 function during development in CNS and thereby play a critical role in pathophysiological mechanisms in Down syndromePMID:22660985
analysis of the crystal structure of the ternary complex composed of the C-terminal domain of human REV1, REV7, and a REV3 fragmentPMID:22859296
the Rev1 C-terminal domain utilizes independent interaction interfaces to simultaneously bind a fragment of the 'inserter' poleta and Rev7 subunit of the 'extender' polvarsigma, thereby serving as a cassette that may accommodate several polymerasesPMID:22828282
ternary complex of the C-terminal domain of human REV1 in complex with REV7 bound to a REV3 fragment has been crystallized. The crystals belonged to space group P3(1)21, with unit-cell parameters a = b = 74.7, c = 124.5 APMID:22869133
The REV1/Polzeta complex maintains genomic stability by directly participating in DNA double-stranded break repair.PMID:21926160
Data show that MAD2B interacts with CLTA during the G2/M phase of the cell cycle and that depletion of MAD2B leads to a marked increase in the percentage of misaligned chromosomes and a redistribution of CLTA during mitosis.PMID:21152103
The hRev7 is required for TLS past BPDE-induced DNA lesions but that it is not essential for inserting nucleotides opposite such lesions suggest a role for hPolzeta in the extension step of translesion synthesis.PMID:21143968
show the first crystal structure of REV7 in complex with a fragment of REV3 polymerase (residues 1847-1898) and reveal the mechanism underlying REV7-REV3 interactionPMID:20164194
To clarify the structural basis of the interaction between REV7 and REV3, REV7 was crystallized in complex with a REV3 fragment.PMID:20054135
the small GTPase RAN is a novel MAD2B binding proteinPMID:19753112
purified human REV1 and REV7 proteins form a heterodimer in solution, which is stable through intensive purification steps.PMID:12529368
Upregulated MAD2L2 expression is associated with colorectal tumorsPMID:17044027
Human Rev7 (hRev7)/MAD2B/MAD2L2 is an interaction partner for Elk-1 and hRev7 acts to promote Elk-1 phosphorylation by the c-Jun N-terminal protein kinase (JNK) MAP kinases.PMID:17296730
Chromophobe renal cell carcinoma presented underexpression of MAD1, and MAD2L2.PMID:17333263
Hepatocellular carcinoma-associated gene 2 interacts with MAD2L2.PMID:17541814
Study provides the first evidence for the involvement of MAD2B in TCF4-mediated epithelial-mesenchymal transdifferentiation.PMID:19443654