Ask about this productRelated genes to: DMAP1 Blocking Peptide
- Gene:
- DMAP1 NIH gene
- Name:
- DNA methyltransferase 1 associated protein 1
- Previous symbol:
- -
- Synonyms:
- DNMAP1, FLJ11543, KIAA1425, DNMTAP1, EAF2, MEAF2, SWC4
- Chromosome:
- 1p34.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-03-12
- Date modifiied:
- 2016-10-05
Related products to: DMAP1 Blocking Peptide
Related articles to: DMAP1 Blocking Peptide
- Despite substantial progress in targeted and immune therapies, lung cancer remains the leading cause of cancer-related mortality, highlighting the urgent need for novel therapeutic strategies. Through a CRISPR-based knock-out screen, we identified the DNA methyltransferase 1-associated protein 1 (DMAP1) as a critical regulator of lung cancer progression. Functional studies demonstrated that DMAP1 deficiency exerts its anti-tumor effects through attenuating tumor cell proliferation and activating T cell-mediated adaptive anti-tumor effects. Mechanistically, DMAP1 deficiency causes replication fork retardance, disturbs genome stability, and induces endogenous DNA damage, thereby activating IFN signaling-mediated anti-tumor immune response. Clinical data analyses revealed that high DMAP1 expression is associated with a "cold" tumor microenvironment and poorer overall survival in lung cancer. These findings significantly advance our knowledge of DMAP1's function in lung cancer development and offer a scientific basis for designing novel treatment approaches. - Source: PubMed
Publication date: 2026/03/29
Huang KanDai XiLi ShuaihuChen YingxueYu YaxinWang LinLiu KunLyu ShuhanLi ChongyangSun YihuaLi Fei - Glycine decarboxylase (GLDC) is overexpressed in multiple tumor types and contributes to tumorigenesis or immune evasion by unclarified mechanisms. Here we report that GLDC is polyubiquitinated at K636 following EGFR activation, which drives GLDC-dependent transcriptional inhibition of MHC-I genes and induces tumor cells to evade CD8 T cell-mediated immunosurveillance. Mechanistically, EGFR activation triggers SRC-mediated FBXL3 phosphorylation at Y306, enabling its interaction with GLDC in nucleus. FBXL3 targets GLDC for K63-linked polyubiquitination, and promotes the interaction of GLDC with SMARCE1/DMAP1 to inhibit STAT1-triggered transcriptional activation, resulting in transcriptional inhibition of downstream MHC-I genes. Phosphorylation of FBXL3 decreases MHC-I levels in tumor cells and inhibits CD8 T cells immunity in tumors. Consistently, inhibitors of SRC improves tumor-specific CD8 T cells functions in TME and sensitizes antitumor effects of anti-PD-1 therapy. Our findings reveal an SRC-FBXL3-GLDC-MHC-I regulatory circuit that underlies CD8 T cells immune evasion, and provide a potential therapeutic target to enhance ICB therapy. - Source: PubMed
Publication date: 2026/02/03
Liu RuiLi Shu - The chromatin landscape surrounding integrated HIV proviruses critically shapes viral transcription. We systematically examined ATP-dependent chromatin remodeling complexes (SWI/SNF, ISWI, CHD, and INO80) as regulators of HIV expression and identified the p400 complex, a member of the INO80 family, as a potent repressor. Depleting p400 subunits, including the EP400 ATPase and DMAP1, markedly increased HIV transcription and RNAPII elongation at the proviral locus. Mechanistically, EP400 associates with the RNAPII C-terminal domain, while DMAP1 directly engages the viral transactivator Tat, with repression requiring simultaneous interactions among EP400, DMAP1, and Tat. Loss of either EP400 or DMAP1 selectively increased infection and transcription of Tat-competent, but not Tat-deficient, viruses. Although p400 is recruited to active HIV chromatin via RNAPII in a Tat-independent manner, it restrains elongation once Tat accumulates during reactivation. DMAP1 binding to Tat's basic domain blocks Tat-TAR RNA interaction, thereby limiting p-TEFb-mediated RNAPII Ser2 phosphorylation and elongation. Thus, the p400 complex functions as a host restriction factor that limits Tat-dependent HIV transcription via a Tat-dependent proximal mechanism, highlighting the p400-Tat interface as a potential target for HIV cure strategies. - Source: PubMed
Li ChuanMa YuanMori Luisa PYang HuimingWang YiVenables Thomas TBronson RonaldMilione Ryan RPipkin Mathew EValente Susana T - Eradicating HIV-1 is complicated by latently infected CD4+T cells harboring dormant proviruses capable of reactivation. Through a pooled shRNAmir screen targeting human chromatin regulators, we identified EP400, a member of the p400 chromatin remodeling complex, as a potent inhibitor of HIV-1 transcription in Jurkat and primary CD4+T cells. EP400 and its complex partner DMAP1 co-localize with paused RNA Polymerase II (RNAPII) at transcriptional start sites of protein-coding genes and their depletion modestly reduced RNAPII pausing. At the HIV-1 locus, EP400 and DMAP1 were co-recruited with RNAPII across the entire HIV-1 genome, and their depletion markedly increases RNAPII pause release. Together this suggests that EP400 may play a role in limiting HIV-1 transcriptional elongation. Additionally, EP400 depletion increased expression of key T-cell factors known to activate HIV-1 transcription. Therefore, the p400 complex reduces efficient HIV-1 transcriptional elongation and contributes to a CD4+T cell state unfavorable for HIV-1 transcription. - Source: PubMed
Mori Luisa PLi ChuanVenables ThomasMcAuley Andrew TGetzler Adam JWang QifanTsuda Shanel MJablonski Joseph APipkin Matthew EValente Susana T - To adapt to seasonal changes, many animals, particularly insects, enter a dormancy-like condition known as diapause, which is primarily accomplished by sensing photoperiodic signals. The circadian clock, which is driven by positive regulators Clock (CLK) and Cycle (CYC), and negative regulators Period and Timeless, is thought to mediate this response. However, it remains unclear whether diapause induction involves a canonical rhythmic mechanism or occurs independently of their traditional roles in timekeeping. Using the ladybug as a model for short-day-induced winter diapause, we demonstrate that knockdown of and , but not or , disrupted entry into reproductive diapause. This finding demonstrated that regulates diapause independently of and . We further show that the DNA methyltransferase 1-associated protein 1 (DMAP1)-mediated Nucleosome Acetyltransferase of H4 (NuA4)/TIP60 histone acetyltransferase complex impinges on diapause regulation by acting simultaneously as a downstream effector and a physical interactor of CLK-CYC. Application of the juvenile hormone (JH) receptor agonist methoprene effectively rescued the diapause phenotypes caused by , , and knockdowns, highlighting the central role of the CLK-CYC-NuA4/TIP60 complex in JH production. Additionally, using a corpora allata (CA)-specific driver in , we demonstrate that this complex functions locally in the CA to mediate JH biosynthesis. Collectively, our findings identify a previously unrecognized pathway by which circadian clock proteins interact with an epigenetic regulator to specifically govern JH biosynthesis in a critical endocrine tissue, thereby regulating diapause entry independently of canonical circadian clock mechanisms. - Source: PubMed
Publication date: 2025/07/10
Gao QiaoDai Yi-FeiZhao Yu-LianLi XueAn Hao-MinKing-Jones KirstWang Jia-LuWang Xiao-PingLiu Wen