ArticleNature communications2020
Molecular mechanism of the MORC4 ATPase activation.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Two Glu/Asp residues cooperatively mediate an early step of ATP hydrolysis in GHKL ATPases MutL and GyrB.eLife · 2026Article
- MORC1 coordinates TRIM28 interaction and nuclear condensate formation for transposon silencing.iScience · 2026Article
- MORC2 is a phosphorylation-dependent DNA compaction machine.Nature communications · 2025Article
- Regulation of MORC-1 is key to the CSR-1-mediated germline gene licensing mechanism inScience advances · 2025Article
- Expression significance of biomarker MORC4 in colorectal cancer patients and its relationship with pathological features and prognosis.World journal of gastrointestinal oncology · 2025Article
- Identification and characterization of a human MORC2 DNA binding region that is required for gene silencing.Nucleic acids research · 2025Article
- Comparison of chromatin accessibility remodeling of granulosa cells in patients with endometrioma or pelvic/tubal infertility.Journal of assisted reproduction and genetics · 2025Article
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- Identification and characterization of a human MORC2 DNA binding region that is required for gene silencing.bioRxiv : the preprint server for biology · 2024Article
- Histone H4K16ac Binding Function of the Triple PHD Finger Cassette of MLL4.Journal of molecular biology · 2024Article
- Oncogenic MORC2 in cancer development and beyond.Genes & diseases · 2024Review
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- Molecular basis for nuclear accumulation and targeting of the inhibitor of apoptosis BIRC2.Nature structural & molecular biology · 2023Article
- Alternative Mechanisms for DNA Engagement by BET Bromodomain-Containing Proteins.Biochemistry · 2022Article
- Microrchidia CW-Type Zinc Finger 2, a Chromatin Modifier in a Spectrum of Peripheral Neuropathies.Frontiers in cellular neuroscience · 2022Review
- Binding Specificity of ASHH2 CW Domain Toward H3K4me1 Ligand Is Coupled to Its Structural Stability Through Its α1-Helix.Frontiers in molecular biosciences · 2022Article
- Mechanistic similarities in recognition of histone tails and DNA by epigenetic readers.Current opinion in structural biology · 2021Review
- MORC protein family-related signature within human disease and cancer.Cell death & disease · 2021Review
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Human Microrchidia 4 (MORC4) is associated with acute and chronic pancreatitis, inflammatory disorders and cancer but it remains largely uncharacterized. Here, we describe the structure-function relationship of MORC4 and define the molecular mechanism for MORC4 activation. Enzymatic and binding assays reveal that MORC4 has ATPase activity, which is dependent on DNA-binding functions of both the ATPase domain and CW domain of MORC4. The crystal structure of the ATPaseCW cassette of MORC4 and mutagenesis studies show that the DNA-binding site and the histone/ATPase binding site of CW are located on the opposite sides of the domain. The ATPase and CW domains cooperate in binding of MORC4 to the nucleosome core particle (NCP), enhancing the DNA wrapping around the histone core and impeding binding of DNA-associated proteins, such as transcription factors, to the NCP. In cells, MORC4 mediates formation of nuclear bodies in the nucleus and has a role in the progression of S-phase of the cell cycle, and both these functions require CW and catalytic activity of MORC4. Our findings highlight the mechanism for MORC4 activation, which is distinctly different from the mechanisms of action observed in other MORC family members.
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