Affinage

MOV10

Helicase MOV-10 · UniProt Q9HCE1

Length
1003 aa
Mass
113.7 kDa
Annotated
2026-06-10
66 papers in source corpus 42 papers cited in narrative 42 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MOV10 is an ATP-dependent superfamily-1 RNA helicase that translocates 5'-to-3' along RNA and acts broadly in post-transcriptional RNA regulation, retroelement restriction, and antiviral defense (PMID:24726324, PMID:23093941). As an RNA clearance factor it binds 3' UTRs upstream of structured regions and partners with UPF1 to promote decay of co-bound transcripts (PMID:24726324), and in the brain it forms an FMRP- and AGO2-containing inhibitory complex on synaptic mRNAs whose balance is set by FMRP's RGG box and MOV10's N-terminal domain (PMID:25464849, PMID:31291981, PMID:31740951). MOV10 is a potent suppressor of LINE-1, Alu, and SVA retrotransposons, acting through its helicase domain by associating with the L1 ribonucleoprotein and ORF1p to reduce L1 RNA, sequestering L1 RNP into cytoplasmic/stress-granule aggregates, recruiting the decapping enzyme DCP2 in a phase-separating complex to degrade L1 RNA, and cooperating with RNASEH2 to resolve L1 RNA-DNA hybrids (PMID:23093941, PMID:23754279, PMID:37437058, PMID:29315404, PMID:35856394). It restricts a wide range of viruses by both helicase-dependent and helicase-independent routes: it is packaged into HIV-1 virions via the nucleocapsid and blocks replication post-entry (PMID:20215113, PMID:20668078, PMID:22105071), degrades influenza vRNA and retains viral nucleoprotein in the cytoplasm to block nuclear import (PMID:26842467, PMID:30617221), and similarly targets the nucleoproteins of bunyaviruses, coronaviruses, and other RNA viruses, in some cases by boosting IRF3/IKKε-driven type I interferon induction (PMID:33284835, PMID:34517762, PMID:27016603). MOV10 activity is regulated by S970 phosphorylation, which restricts helicase-mediated G-quadruplex unwinding and switches transcripts toward AGO2-mediated degradation (PMID:36871759), and by CRL4-DCAF12-directed ubiquitination and proteasomal turnover (PMID:34065512). In neurons, MOV10 undergoes NMDA-receptor-driven, proteasome-dependent degradation to relieve translational silencing of synaptic mRNAs (PMID:20064393), and it is required for neurite outgrowth and dendritic arborization through regulation of cytoskeletal and NUMA1 mRNAs (PMID:28662698, PMID:39915816). MOV10 is essential for development, with knockout causing embryonic lethality in mice and gastrulation/neurulation defects in Xenopus, and it supports reproductive fitness by restraining LINE-1 in the germline (PMID:28662698, PMID:29266590, PMID:37126510).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 1994 Medium

    Before any protein function was known, the question was how MOV10 expression is controlled; this established differentiation-coupled transcriptional regulation of the gene.

    Evidence CAT reporter assays, DNase I footprinting, and mutational analysis of a 133-bp intronic enhancer in F9 embryonal carcinoma cells

    PMID:8065313

    Open questions at the time
    • Does not address the protein's molecular function
    • Identity of the undifferentiated-cell-specific GT-box factor unresolved
  2. 2008 Medium

    The first functional clue placed MOV10 in RNA-directed processes; its requirement for HDV replication but not HDAg translation implicated it in RNA-templated transcription rather than translation.

    Evidence HDAg-interaction screen with MOV10 knockdown and separate HDV replication and translation readouts

    PMID:18552826

    Open questions at the time
    • Helicase activity not directly tested here
    • Mechanism of action on HDV RNA undefined
  3. 2009 High

    Two independent contexts established MOV10 as a regulated RNA-handling factor: activity-dependent proteasomal degradation at synapses controlling local translation, and a contested telomerase association.

    Evidence Synaptic translational trap, polysome fractionation, proteasome inhibition and NMDAR stimulation in neurons; separately, co-purification of telomerase activity with anti-MOV10 IP and telomere DNA binding

    PMID:19665004 PMID:20064393

    Open questions at the time
    • The telomerase association (idx 27) is Low-confidence, single-lab, and not replicated
    • Direct helicase action on the synaptic target mRNAs not shown in 2009
  4. 2010 High

    MOV10 was defined as a broad retroviral restriction factor and a nuclear chromatin-associated regulator, establishing its antiviral identity and a PRC1-linked epigenetic role.

    Evidence Reciprocal overexpression/knockdown HIV-1 infectivity assays, virion incorporation, and domain mapping; plus chromatin fractionation, PRC1 co-IP and ChIP at the INK4a locus

    PMID:20215113 PMID:20543829 PMID:20668078

    Open questions at the time
    • N-terminal vs helicase contributions to HIV restriction only partly resolved
    • Mechanism of PRC1 recruitment to chromatin undefined
  5. 2012 High

    MOV10 was established as a helicase-dependent restrictor of endogenous retroelements and its interface with the RISC/APOBEC3G machinery was mapped, distinguishing antiretroelement from antiretrovirus activity.

    Evidence Retrotransposition assays across L1/Alu/SVA with helicase mutants and L1 RNP co-IP; RNAi specificity for endogenous elements; APOBEC3G domain-mapped competition for AGO2 binding via 7SL RNA

    PMID:22105071 PMID:22727223 PMID:22791714 PMID:23093941

    Open questions at the time
    • Exact step in retrotransposition blocked not fully defined
    • Whether RISC association is required for antiretroelement activity unresolved
  6. 2013 High

    Mechanistic dissection showed MOV10 suppresses L1 by helicase-dependent reduction of L1 RNA, and clarified that P-body localization is dispensable for HIV restriction.

    Evidence Helicase-motif mutagenesis with L1 RNA quantification and ORF1 co-IP; P-body disruption by DDX6 knockdown and helicase-V mutant analysis with HIV infectivity readouts

    PMID:23754279 PMID:23926332

    Open questions at the time
    • Nuclease/effector that degrades L1 RNA not identified in 2013
    • How helicase translocation triggers RNA degradation unclear
  7. 2014 High

    Biochemical reconstitution and CLIP defined MOV10's directional helicase activity and its role as an RNA clearance factor for UPF1-mediated decay, and revealed a dual relationship with the miRNA/FMRP machinery.

    Evidence In vitro 5'-to-3' unwinding with helicase mutants, PAR-CLIP, UPF1 co-IP and mRNA half-life measurements; reciprocal FMRP co-IP, iCLIP and reporter assays

    PMID:24726324 PMID:25464849

    Open questions at the time
    • How MOV10 both promotes and antagonizes AGO2 on different transcripts not mechanistically resolved
    • Determinants of UPF1 vs FMRP coupling unknown
  8. 2016 Medium

    Helicase-independent antiviral modes were established: cytoplasmic retention of influenza nucleoprotein blocking nuclear import, and IFN-pathway amplification via IRF3/IKKε independent of RIG-I/MAVS.

    Evidence Knockdown/KO with minigenome, importin-α binding and fractionation assays for influenza NP; IFN reporter and kinase KO experiments for broad RNA-virus restriction

    PMID:26842467 PMID:27016603

    Open questions at the time
    • How MOV10 activates IKKε specifically is undefined
    • Connection between NP sequestration and IFN induction unclear
  9. 2018 Medium

    A nuclear partner for L1 restriction was identified, linking MOV10 to RNASEH2-dependent resolution of L1 RNA-DNA hybrids.

    Evidence Proteomic co-IP, nuclear co-localization, shRNA knockdown, retrotransposition and RNA-DNA hybrid detection

    PMID:29315404

    Open questions at the time
    • Order of MOV10 and RNASEH2 action on hybrids not established
    • Whether helicase activity feeds hybrid formation unclear
  10. 2019 Medium

    In vivo and biochemical work established MOV10's essential developmental and neuronal roles, refined its synaptic FMRP/AGO2 switch, and extended antiviral targeting to HBV.

    Evidence Mov10 KO/heterozygote mice (embryonic lethality, RIP-seq, neurite outgrowth), synaptoneurosome co-IP/polysome NMDAR stimulation, N-terminus/RGG-box G-quadruplex mapping, and HBV helicase-mutant RNA-binding assays

    PMID:28662698 PMID:31252377 PMID:31291981 PMID:31722967 PMID:31740951

    Open questions at the time
    • In vivo function of helicase activity in neurons not isolated
    • Kinase responsible for the FMRP/MOV10 phospho-switch unidentified
  11. 2020 Medium

    MOV10 was shown to disable viral nucleoprotein assembly across diverse viruses and to relocalize to viral replication sites, defining a recurring nucleoprotein-targeting antiviral strategy.

    Evidence Mass spectrometry, N-polymerization/RNA-binding and minigenome assays with in vivo infection for bunyaviruses; CRISPR KO and mutagenesis for HCV with lipid-droplet relocalization imaging

    PMID:32496609 PMID:33284835

    Open questions at the time
    • Why MOV10 is proviral for HCV but antiviral for most viruses unresolved
    • Structural basis of N-arm binding limited to one virus family
  12. 2021 Medium

    MOV10 turnover was placed under CRL4-DCAF12 control with a germline phenotype, and helicase-dependent coronavirus restriction plus a NUMA1-dependent dendritic role were established.

    Evidence CRL4-DCAF12 co-purification with DCAF12 KO mice; CRISPR KO/helicase-dead complementation for MERS-CoV with RNA-IP; brain-specific Mov10 KO with NUMA1/HAUS rescue (idx 36 reported 2025)

    PMID:34065512 PMID:34517762

    Open questions at the time
    • Signals controlling DCAF12-mediated MOV10 degradation unknown
    • Link between MOV10 levels and meiotic progression not mechanistic
  13. 2023 Medium

    The L1-clearance effector and a regulatory phospho-switch were defined: MOV10 recruits DCP2 to decap L1 RNA in a phase-separating complex, and S970 phosphorylation restricts helicase activity to redirect transcripts toward AGO2 degradation.

    Evidence Co-IP, phase-separation and in vitro decapping assays with retrotransposition readout; mass-spectrometry-identified S970 with G-quadruplex unwinding assays, RNA-seq and AGO2 knockdown

    PMID:36871759 PMID:37437058

    Open questions at the time
    • Kinase phosphorylating S970 not identified
    • How phase separation couples to decapping efficiency unresolved
  14. 2025 Medium

    Domain-level dissection separated MOV10's helicase/RNP-binding and granule-forming functions and distinguished its N-terminal regulatory domain from the UPF1 CH domain in NMD coupling.

    Evidence Domain truncation/mutagenesis with retrotransposition and G3BP1 co-IP for L1 restriction; in vitro biochemistry and interaction mapping with UPF2/UPF1

    PMID:40408535 PMID:40570961

    Open questions at the time
    • Structural basis of MOV10-UPF2 engagement not solved
    • How granule formation enhances catalytic restriction unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • How MOV10 selects between its opposing outputs — protecting versus degrading bound mRNAs, restricting versus assisting viruses, and acting via helicase-dependent versus helicase-independent routes — remains unresolved.
  • No unifying model for substrate/context selection
  • Upstream kinases for S970 and the synaptic FMRP switch unidentified
  • Structural mechanism of nucleoprotein sequestration vs RNA unwinding undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 5 GO:0098772 molecular function regulator activity 3 GO:0140098 catalytic activity, acting on RNA 3 GO:0140657 ATP-dependent activity 2 GO:0003677 DNA binding 1
Localization
GO:0031410 cytoplasmic vesicle 4 GO:0005634 nucleus 3 GO:0005829 cytosol 3 GO:0005694 chromosome 1
Pathway
R-HSA-168256 Immune System 5 R-HSA-112316 Neuronal System 4 R-HSA-1643685 Disease 4 R-HSA-8953854 Metabolism of RNA 4
Partners
AGO2APOBEC3GDCP2FMRPG3BP1RNASEH2UPF1UPF2
Complex memberships
MOV10-FMRP-AGO2 inhibitory complexMOV10-UPF1 complexPRC1RISC (with AGO2)

Evidence

Reading pass · 42 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2014 MOV10 has ATP-dependent 5' to 3' RNA unwinding activity in vitro and translocates 5' to 3' on mRNA targets. MOV10 helicase mutants are impaired in translocation. MOV10 predominantly binds 3' UTRs upstream of regions predicted to form local secondary structures. MOV10 interacts with UPF1, and PAR-CLIP shows MOV10 and UPF1 bind RNA in close proximity. Knockdown of MOV10 increased mRNA half-lives of MOV10-bound and UPF1-regulated transcripts, implicating MOV10 as an RNA clearance factor in UPF1-mediated mRNA degradation. In vitro RNA unwinding assay, PAR-CLIP, Co-IP, mRNA half-life measurement, helicase mutant analysis Molecular cell High 24726324
2009 MOV10 is present at synapses and is rapidly degraded by the proteasome in an NMDA-receptor-mediated, activity-dependent manner. When MOV10 is suppressed, specific mRNAs (including alpha-CaMKII, Limk1, and Lypla1) enter the polysome compartment, and activity-dependent protein synthesis driven by Lypla1 and alpha-CaMKII 3'UTRs is MOV10- and proteasome-dependent. Translational trap assay, polysome fractionation, proteasome inhibitor treatment, NMDA-receptor stimulation, photoconvertible translation reporter (Kaede) Neuron High 20064393
2014 FMRP associates with MOV10 both directly and in an RNA-dependent manner and facilitates MOV10's association with RNAs in brain. MOV10 has a dual function: it facilitates microRNA-mediated translation repression of some mRNAs, but also prevents AGO2 function on a subset of mRNAs co-bound by FMRP, thereby increasing their expression. FMRP binding near MOV10 binding sites prevents MOV10-mediated microRNA suppression. Co-IP, RNA immunoprecipitation (RIP), iCLIP, reporter assays Cell reports High 25464849
2012 MOV10 severely restricts human LINE-1 (L1), Alu, and SVA retrotransposons. MOV10 associates with the L1 ribonucleoprotein particle and colocalizes with L1 ORF1 protein in stress granules. This inhibitory activity is dependent on intact helicase domains. Retrotransposition assay, Co-IP/co-fractionation, immunofluorescence colocalization, helicase domain mutant analysis PLoS genetics High 23093941
2013 MOV10 suppresses LINE-1 transposition through its helicase activity; mutating helicase motifs impairs this function. MOV10 post-transcriptionally reduces LINE-1 RNA levels and associates with both LINE-1 RNA and ORF1 protein, indicating MOV10 interacts with LINE-1 RNP to cause RNA degradation. Retrotransposition assay, helicase motif mutagenesis, RT-qPCR for RNA levels, Co-IP with LINE-1 ORF1 The Journal of biological chemistry High 23754279
2010 MOV10 (a superfamily-1 RNA helicase and RISC component) inhibits retrovirus replication. When overexpressed in viral producer cells, MOV10 reduces HIV-1 infectivity. MOV10 interacts with HIV-1 nucleocapsid protein in an RNA-dependent manner and is packaged into virions. It blocks HIV-1 replication at a post-entry step. Silencing MOV10 increases HIV-1 infectivity. Overexpression/knockdown, infectivity assays, Co-IP, virion incorporation western blot The Journal of biological chemistry High 20215113
2010 MOV10 is a P-body-associated protein; its overexpression in virus producer cells inhibits HIV-1 at multiple stages including reducing steady-state Gag protein levels, virus production, and virion infectivity partly by inhibiting reverse transcription. MOV10 is efficiently incorporated into virions. The N-terminal half of MOV10 is required for its HIV inhibitory activity; removing it abolishes activity, whereas helicase mutation or C-terminal truncation retains most inhibitory activity. Overexpression, siRNA knockdown, infectivity assays, reverse transcription assays, domain truncation/mutation analysis, virion western blot Journal of virology High 20668078
2010 Endogenous MOV10 is mostly nuclear in human cells, and a proportion associates with chromatin in an RNA-dependent manner. MOV10 co-purifies and interacts with components of Polycomb-repressive complex 1 (PRC1). ShRNA-mediated knockdown of MOV10 leads to upregulation of the INK4a tumor suppressor, dissociation of PRC1 proteins from the INK4a locus, and reduction in H3K27me3 at that locus. Co-purification, Co-IP, chromatin fractionation, shRNA knockdown, ChIP for H3K27me3 and PRC1 components Nature structural & molecular biology High 20543829
2016 MOV10 inhibits influenza A virus replication by interacting (via RNA-mediated interaction) with the nucleoprotein (NP) subunit of the vRNP complex, preventing NP binding to importin-α and causing retention of NP in the cytoplasm, thereby inhibiting nuclear import of NP and vRNP function. This inhibitory effect is independent of MOV10's helicase activity. MOV10 knockdown, minigenome assay, Co-IP, importin-α binding assay, subcellular fractionation/immunofluorescence Journal of virology High 26842467
2012 Endogenous MOV10 suppresses retrotransposition of LTR and non-LTR endogenous retroelements (shown by RNAi-mediated silencing enhancing retrotransposon replication), but RNAi knockdown has no impact on infectious retrovirus particle production, demonstrating natural MOV10 levels specifically regulate endogenous retroelements in somatic cells. MOV10 is not necessary for miRNA or siRNA-mediated mRNA silencing (negative finding). RNAi knockdown, retrotransposition assay, retrovirus infectivity assay, miRNA/siRNA reporter assays Retrovirology Medium 22727223
2016 MOV10 exhibits antiviral activity against positive- and negative-strand RNA viruses by enhancing type I IFN induction, independent of its helicase function. This activity requires IRF3-mediated IFN induction and downstream IFN receptor signaling. MOV10 specifically requires IKKε (not TBK1) for antiviral activity, and this IFN induction pathway is independent of RIG-I/MAVS. Viral proteases from picornavirus family specifically targeted MOV10 as an immune evasion mechanism. Genome-edited knockout human cells, IFN reporter assays, viral replication assays, kinase knockdown/knockout experiments Journal of immunology Medium 27016603
2008 MOV10 (human homolog of Arabidopsis SDE3 and Drosophila Armitage) interacts with hepatitis delta antigen (HDAg). MOV10 knockdown inhibited HDV replication but not HDAg mRNA translation, supporting a role for MOV10 in RNA-directed transcription rather than translation. HDAg-interaction screen, MOV10 knockdown, HDV replication assay, translation assay Nature structural & molecular biology Medium 18552826
2011 MOV10 is packaged into HIV-1 virions via binding to the nucleocapsid (NC) basic linker region of Gag; the Gag binding region on MOV10 maps to N-terminal amino acids 261-305 (a Cys-His-rich domain). Packaging also requires nearly all C-terminal helicase motifs. Simultaneous mutation of residues Cys-188, Cys-195, His-199, His-201, and His-202 significantly compromised anti-HIV-1 activity. The minimal antiviral region maps to amino acids 99-949. Domain deletion/mutagenesis, virion incorporation assay, infectivity assay, structural domain modeling The Journal of biological chemistry Medium 22105071
2012 APOBEC3G (A3G) counteracts miRNA-mediated translation repression by inhibiting the interaction between MOV10 and AGO2. A3G binds to a C-terminal domain of MOV10 and competitively inhibits AGO2 binding to the same domain. The A3G-MOV10 interaction relies on 7SL RNA; the A3G mutant W127L, which cannot bind 7SL RNA, loses this ability. Co-IP, domain deletion mapping, reporter assay for miRNA repression, RNA-dependence assay with RNase treatment The Journal of biological chemistry Medium 22791714
2018 MOV10 interacts with RNASEH2 (identified by proteomics). RNASEH2 and MOV10 co-localize in the nucleus and their interplay restricts L1 retrotransposition. RNASEH2 binds to L1 RNAs in a MOV10-dependent manner. Depletion of either RNASEH2A or MOV10 results in accumulation of L1-specific RNA-DNA hybrids, suggesting they prevent formation of L1 heteroduplexes during retrotransposition. Proteomic Co-IP, Co-IP, immunofluorescence co-localization, shRNA knockdown, retrotransposition assay, RNA-DNA hybrid detection Nucleic acids research Medium 29315404
2017 MOV10 interacts with IRAV (FLJ11286) in P-bodies of uninfected cells. After dengue virus infection, IRAV and MOV10 (along with Xrn1) localize to the DENV replication complex. Depletion of either IRAV or MOV10 increases dengue viral RNA levels. Co-IP, immunofluorescence, siRNA knockdown, viral RNA quantification Journal of virology Medium 27974568
2019 MOV10 restricts hepatitis B virus replication by interacting with HBV RNA and blocking the early step of viral reverse transcription, impairing viral DNA synthesis without affecting viral gene expression or pregenomic RNA encapsidation. Mutation of the helicase domain caused loss of HBV RNA binding and anti-HBV activity. Overexpression/knockdown, viral DNA quantification, RNA co-IP, helicase domain mutagenesis, Southern blot The Journal of biological chemistry Medium 31722967
2015 MOV10 functions as a co-factor of HIV-1 Rev, interacting with Rev in an RNA-independent manner to enhance nuclear export of viral mRNAs via the Rev/RRE axis. The DEAG-box of MOV10 is required for this enhancement; a DEAG-box mutant shows dominant-negative activity. Co-IP, nuclear export assay, DEAG-box mutagenesis, Gag protein expression assay Virology Medium 26379090
2019 MOV10 is localized to P-bodies in uninfected cells, but during HCV infection it relocalizes to circular structures surrounding cytoplasmic lipid droplets with NS5A and core protein. Mov10 overexpression suppresses HCV RNA and reduces infectivity. The RNA-binding activity of MOV10 is required for HCV inhibition, while P-body localization, helicase, and ATP-binding functions are not required. Endogenous MOV10 promotes HCV replication (CRISPR depletion decreases HCV replication). Confocal imaging, MOV10 overexpression/CRISPR KO, HCV RNA quantification, infectivity assay, mutagenesis FASEB journal Medium 32496609
2021 MOV10 is a substrate of the CRL4-DCAF12 ubiquitin ligase; DCAF12 controls MOV10 protein levels via MOV10's C-terminal motif in a proteasome- and CRL-dependent manner. DCAF12 knockout mice show elevated MOV10 levels and produce fewer mature sperm, with imbalances in meiotic markers SCP3 and γ-H2AX. Co-purification of CRL4-DCAF12 complexes, proteasome inhibitor treatment, CRL inhibitor treatment, DCAF12 KO mouse, western blot International journal of molecular sciences Medium 34065512
2017 In mouse brain, Mov10 suppresses retroelements in the nucleus by directly inhibiting complementary DNA synthesis. Cytosolic Mov10 binds cytoskeletal mRNAs and regulates neurite outgrowth. Loss of Mov10 in hippocampal neurons (heterozygote mouse) reduces dendritic arborization. Mov10 knockout causes embryonic lethality. Mov10, Fmrp, and Ago2 bind a common set of mRNAs in the brain. Mov10 KO/heterozygote mouse, retrotransposition/cDNA synthesis assay, RIP-seq, neurite outgrowth assay, behavioral testing BMC biology Medium 28662698
2019 In rat cortical synaptoneurosomes, MOV10 forms an inhibitory complex with FMRP and AGO2 on a subset of NMDAR-responsive mRNAs. Upon NMDAR stimulation, MOV10 dissociates from AGO2 and promotes translation of its target mRNAs. FMRP is required to form the MOV10-AGO2 inhibitory complex and to promote translation of MOV10-associated mRNAs. Phosphorylation of FMRP appears to be the switch for NMDAR-mediated translation. Synaptoneurosome preparation, Co-IP, polysome fractionation, pharmacological NMDAR stimulation, western blot Molecular brain Medium 31291981
2020 MOV10 targets the nucleoproteins (N) of emerging high-pathogenic bunyaviruses (including SFTSV) in an RNA-independent manner. MOV10 blocks N polymerization, N-RNA binding, and N-polymerase interaction, thereby disabling RNP assembly. This anti-bunyavirus activity is independent of MOV10's helicase activity and the cellular interferon pathway. The N-terminus of MOV10 binds a 34-amino-acid N-arm domain of N critical for N function. Mass spectrometry, protein-interaction assays, minigenome assay, MOV10 knockdown/in vivo animal infection, N polymerization/RNA binding assay, domain mapping PLoS pathogens Medium 33284835
2020 The N-terminus of MOV10 is required for FMRP-mediated protection of a subset of co-bound mRNAs from AGO association: overexpression of the N-terminus leads to increased levels of endogenous proteins encoded by this co-bound subset. The RGG box of FMRP protects co-bound mRNAs from AGO association. The N-terminus of MOV10 increases RGG box-dependent binding to SC1 RNA G-Quadruplex and is required for neurite outgrowth. Domain mapping by Co-IP, western blot for protein levels, RNA G-quadruplex binding assay, neurite outgrowth assay, AGO2 RIP Nucleic acids research Medium 31740951
2023 MOV10 recruits the decapping enzyme DCP2 to LINE-1 RNA, forming a complex of MOV10, DCP2, and LINE-1 RNP that exhibits liquid-liquid phase separation (LLPS) properties. DCP2 cooperates with MOV10 to decap LINE-1 RNA, causing LINE-1 RNA degradation and reduced retrotransposition. Co-IP, phase separation assay, LINE-1 RNA decapping assay, retrotransposition assay, fluorescence microscopy EMBO reports Medium 37437058
2023 MOV10 is phosphorylated at serine 970 (S970) at the C-terminus. Phospho-mimic S970D substitution blocks MOV10 unfolding of an RNA G-quadruplex (similar to helicase domain mutation K531A), while the S970A substitution retains unfolding activity. S970D causes decreased expression of MOV10-enhanced CLIP targets in an AGO2-dependent manner. MOV10 activity normally protects mRNAs from AGO2; S970 phosphorylation restricts this protection, resulting in AGO2-mediated mRNA degradation. Mass spectrometry, site-directed mutagenesis, RNA G-quadruplex unwinding assay, RNA-seq, AGO2 knockdown, Co-IP The Journal of biological chemistry Medium 36871759
2019 MOV10 and MOV10L1 can both resolve RNA G-quadruplex (RG4) structures in vitro, but MOV10L1 does so more efficiently. Both proteins are ATP-dependent. MOV10 does not show preference for binding at a junction between single-stranded RNA and RG4 (in contrast to MOV10L1). In vitro helicase assay with RG4 substrates, binding assays, ATP hydrolysis assays iScience Medium 31252377
2009 MOV10 was isolated as a telomerase-associated protein from porcine testis; it purified with telomerase activity. Anti-MOV10 antibody precipitated telomerase activity from cancer cell extracts and inhibited telomerase activity in vitro. MOV10 binds to the G-rich strand of both single- and double-stranded telomere-sequenced DNA. ChIP assay showed MOV10 binding to telomere regions in vivo. Protein purification co-purifying telomerase activity, anti-MOV10 immunoprecipitation, in vitro telomerase inhibition, DNA binding assay, ChIP Biochemical and biophysical research communications Low 19665004
2019 MOV10 is a nucleocytoplasmic protein in spermatogonia. Nuclear MOV10 associates with splicing factors, particularly SRSF1, with intronic binding sites near splice sites. Knockdown of MOV10 impairs miRNA biogenesis (partially via decreased primary transcript levels and/or retention of miRNA via splicing control) and disrupts spermatogonial progenitor cell proliferation and repopulation. Immunofluorescence, RIP-seq/CLIP-seq, MOV10 knockdown, transplantation experiment, miRNA profiling BMC biology Low 31088452
2021 MOV10 interacts with MERS-CoV nucleocapsid (N) protein (confirmed by endogenous Co-IP), colocalizes with N protein in cytoplasmic aggregates, and sequesters viral RNA in these complexes (RNA-IP). MOV10 silencing increases both N protein levels and virus titer. The helicase activity of MOV10 is required for its antiviral effect against MERS-CoV, shown using CRISPR KO cells expressing WT vs. helicase-dead MOV10. MOV10-N interaction is conserved across human CoVs including SARS-CoV-2. Co-IP (endogenous), RNA immunoprecipitation, CRISPR KO cell lines, WT vs. helicase-dead mutant complementation, viral titer assay mBio Medium 34517762
2013 MOV10 and APOBEC3G localization to P-bodies is NOT required for virion incorporation or antiviral activity against HIV-1. A helicase V mutant of MOV10 has significantly reduced P-body localization but still efficiently inhibits viral infectivity via virion incorporation. CRISPR/DDX6-knockdown-disrupted P-bodies confirmed MOV10 antiviral activity without P-body localization. AGO2-mediated RNA-induced silencing is required for MOV10's ability to reduce Gag expression upon overexpression, but NOT for virion incorporation or infectivity effects. P-body disruption by DDX6 knockdown, helicase V mutant analysis, sucrose gradient sedimentation, AGO2 depletion, infectivity assay Journal of virology Medium 23926332
2018 MOV10 inhibits PRRSV replication by interacting with the viral nucleocapsid (N) protein in the cytoplasm and retaining N protein in the cytoplasm, preventing its nuclear import. MOV10 does not affect virus attachment or internalization. Stable MOV10 overexpression, Co-IP, immunofluorescence co-localization, subcellular fractionation, adsorption assay Biochemical and biophysical research communications Low 30172377
2022 MOV10 forms a complex with UPF1 in mouse testis and primarily binds 3' UTRs of somatically expressed transcripts. Loss of MOV10 in mice results in an altered testis transcriptome and increased LINE-1 retrotransposition in somatic and reproductive tissues in a dosage-dependent manner. MOV10 deficiency reduces reproductive fitness over successive generations. MOV10 KO mouse (conditional), LINE-1 reporter transgene, RNA-seq, biochemical Co-IP for UPF1 complex PLoS genetics Medium 37126510
2017 MOV10 inhibits Vif-mediated degradation of APOBEC3G by interfering with assembly of the Vif-CBF-β-Cullin5-ElonginB-ElonginC E3 ubiquitin ligase complex. The DEAG-box of MOV10 is required for this inhibition. Co-IP for E3 ligase complex components, western blot for A3G levels, DEAG-box mutagenesis, proteasome assay Retrovirology Low 29258557
2019 MOV10 sequesters influenza A virus RNP in the cytoplasm by interacting with viral NP, and this leads to degradation of viral vRNA. P-body integrity is required for MOV10's antiviral activity. Viral NS1 protein antagonizes MOV10 by interfering with MOV10-NP interaction and promoting MOV10 degradation via the lysosomal pathway. Co-IP, RNA degradation assay, P-body disruption (DDX6 knockdown), NS1 co-expression, lysosome inhibitor treatment, viral RNA quantification The Biochemical journal Medium 30617221
2018 Knockdown of maternal Mov10 in Xenopus laevis embryos causes defects in gastrulation, notochord and paraxial mesoderm development, and failure to neurulate. Degradation of the miR-427 target mRNA cyclin A1 (maternal-to-zygotic transition event) is delayed in Mov10 knockdowns. Zygotic Mov10 knockdown impairs head, eye, and brain development. Translation-blocking morpholino knockdown in Xenopus, RNA-seq, developmental phenotype analysis, cyclin A1 mRNA stability assay Developmental dynamics Medium 29266590
2021 MOV10 regulates dendritic arborization and NUMA1 mRNA translation in hippocampal neurons. In brain-specific Mov10 KO mice, NUMA1 expression is decreased. Restoration of NUMA1 expression or knockdown of HAUS rescued abnormal dendritic phenotypes in Mov10 KO hippocampal neurons. Enhanced fear memory is observed in Mov10 KO mice. Brain-specific MOV10 KO mouse, MOV10 CLIP-seq (NUMA1 identified as target), rescue experiments with NUMA1 overexpression and HAUS knockdown, dendritic morphometry BMC biology Medium 39915816
2025 The extended motif II (residues 563-675) and the C-terminal domain (residues 907-1003) of MOV10 cooperate for maximal inhibition of LINE-1 retrotransposition. The extended motif II mediates MOV10-LINE-1 RNA/RNP interaction and is dominant for anti-LINE-1 activity. The C-terminal domain mediates MOV10's association with G3BP1 and formation of cytoplasmic granules, which promotes maximal inhibition. Domain deletion/truncation mutagenesis, retrotransposition assay, Co-IP for G3BP1, immunofluorescence for granule formation PLoS genetics Medium 40408535
2025 The N-terminal domain of MOV10 is functionally distinct from the CH domain of UPF1: it impacts catalytic helicase activity differently and mediates different protein-protein interactions. MOV10 engages the NMD factor UPF2 via its N-terminal regulatory domain, but at a different region than UPF1's CH domain binds UPF2. The MOV10 N-terminal domain dictates its localization to cytoplasmic RNA condensates (P-bodies and stress granules), distinct from UPF1 whose localization is RNA-driven. In vitro biochemical assays, domain mutagenesis, protein-protein interaction mapping, localization studies The Journal of biological chemistry Medium 40570961
2022 MOV10 drives sequestration of LINE-1 ribonucleoprotein complexes into cytoplasmic aggregates, restricting retrotransposition. Combined overexpression of L1 ORF1p and MOV10 is sufficient to create L1 RNP aggregates. In Dicer KO mESCs, MOV10 is upregulated due to loss of direct miRNA regulation, and this elevated MOV10 drives L1 aggregate formation. Dicer KO mESCs, co-overexpression experiments, immunofluorescence, retrotransposition assay, miRNA regulation of Mov10 3'UTR EMBO reports Medium 35856394
2024 MOV10 is ISGylated (modified by ISG15), and ISGylated MOV10 enhances IFN-β production/secretion. The deubiquitylase USP24 specifically de-ISGylates MOV10 to negatively regulate the innate immune IFN-I response. USP24 depletion increases ISG15 conjugate accumulation and was identified as a novel ISG15 cross-reactive DUB by activity-based protein profiling. Activity-based protein profiling (ABPP), in vitro USP24 ISG15-substrate cleavage assay, proteomics (total proteome/GG-peptidome/ISG15 interactome), USP24 depletion, IFN-β reporter assay bioRxivpreprint Low bio_10.1101_2024.09.06.611391
1994 The gb110 gene (MOV10) has a 133-bp intronic enhancer that activates expression ~50-100 fold in undifferentiated F9 embryonal carcinoma cells. This enhancer is inactive in differentiated cells, mediating differentiation-specific downregulation. Four protein-binding sites were identified, including GC/GT-box motifs bound cooperatively by Sp1-related proteins; one GT-box-binding protein is present only in undifferentiated F9 cells. Transient chloramphenicol acetyltransferase (CAT) reporter assay, DNase I footprinting, gel mobility shift assay, mutational analysis of binding sites Molecular and cellular biology Medium 8065313

Source papers

Stage 0 corpus · 66 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2009 A coordinated local translational control point at the synapse involving relief from silencing and MOV10 degradation. Neuron 191 20064393
2012 MOV10 RNA helicase is a potent inhibitor of retrotransposition in cells. PLoS genetics 180 23093941
2014 MOV10 Is a 5' to 3' RNA helicase contributing to UPF1 mRNA target degradation by translocation along 3' UTRs. Molecular cell 159 24726324
2010 P body-associated protein Mov10 inhibits HIV-1 replication at multiple stages. Journal of virology 128 20668078
2010 Perturbation of the P-body component Mov10 inhibits HIV-1 infectivity. PloS one 100 20140200
2012 Modulating human proteinase activated receptor 2 with a novel antagonist (GB88) and agonist (GB110). British journal of pharmacology 99 21806599
2010 Moloney leukemia virus 10 (MOV10) protein inhibits retrovirus replication. The Journal of biological chemistry 98 20215113
2019 MOV10 binding circ-DICER1 regulates the angiogenesis of glioma via miR-103a-3p/miR-382-5p mediated ZIC4 expression change. Journal of experimental & clinical cancer research : CR 97 30621721
2014 MOV10 and FMRP regulate AGO2 association with microRNA recognition elements. Cell reports 94 25464849
2013 The MOV10 helicase inhibits LINE-1 mobility. The Journal of biological chemistry 90 23754279
2012 Endogenous MOV10 inhibits the retrotransposition of endogenous retroelements but not the replication of exogenous retroviruses. Retrovirology 85 22727223
2016 Host Protein Moloney Leukemia Virus 10 (MOV10) Acts as a Restriction Factor of Influenza A Virus by Inhibiting the Nuclear Import of the Viral Nucleoprotein. Journal of virology 77 26842467
2012 Mixture models and wavelet transforms reveal high confidence RNA-protein interaction sites in MOV10 PAR-CLIP data. Nucleic acids research 71 22844102
2008 Capped small RNAs and MOV10 in human hepatitis delta virus replication. Nature structural & molecular biology 66 18552826
2017 IRAV (FLJ11286), an Interferon-Stimulated Gene with Antiviral Activity against Dengue Virus, Interacts with MOV10. Journal of virology 63 27974568
2010 Role for the MOV10 RNA helicase in polycomb-mediated repression of the INK4a tumor suppressor. Nature structural & molecular biology 55 20543829
2016 MOV10 Provides Antiviral Activity against RNA Viruses by Enhancing RIG-I-MAVS-Independent IFN Induction. Journal of immunology (Baltimore, Md. : 1950) 54 27016603
2020 Caenorhabditis elegans ADAR editing and the ERI-6/7/MOV10 RNAi pathway silence endogenous viral elements and LTR retrotransposons. Proceedings of the National Academy of Sciences of the United States of America 49 32123111
2018 Interplay between RNASEH2 and MOV10 controls LINE-1 retrotransposition. Nucleic acids research 46 29315404
2012 APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10. The Journal of biological chemistry 46 22791714
2017 Mov10 suppresses retroelements and regulates neuronal development and function in the developing brain. BMC biology 42 28662698
2011 Identification of molecular determinants from Moloney leukemia virus 10 homolog (MOV10) protein for virion packaging and anti-HIV-1 activity. The Journal of biological chemistry 42 22105071
2013 Mov10 and APOBEC3G localization to processing bodies is not required for virion incorporation and antiviral activity. Journal of virology 36 23926332
2020 Host restriction of emerging high-pathogenic bunyaviruses via MOV10 by targeting viral nucleoprotein and blocking ribonucleoprotein assembly. PLoS pathogens 33 33284835
2021 Unwinding the roles of RNA helicase MOV10. Wiley interdisciplinary reviews. RNA 29 34327836
2019 Biological and RNA regulatory function of MOV10 in mammalian germ cells. BMC biology 29 31088452
2020 The FMRP-MOV10 complex: a translational regulatory switch modulated by G-Quadruplexes. Nucleic acids research 25 31740951
2019 MOV10L1 Binds RNA G-Quadruplex in a Structure-Specific Manner and Resolves It More Efficiently Than MOV10. iScience 22 31252377
2021 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase during Spermatogenesis and T Cell Activation. International journal of molecular sciences 21 34065512
2019 The MOV10 helicase restricts hepatitis B virus replication by inhibiting viral reverse transcription. The Journal of biological chemistry 21 31722967
2018 MOV10 inhibits replication of porcine reproductive and respiratory syndrome virus by retaining viral nucleocapsid protein in the cytoplasm of Marc-145 cells. Biochemical and biophysical research communications 20 30172377
2015 RNA helicase MOV10 functions as a co-factor of HIV-1 Rev to facilitate Rev/RRE-dependent nuclear export of viral mRNAs. Virology 20 26379090
2019 NMDAR mediated translation at the synapse is regulated by MOV10 and FMRP. Molecular brain 18 31291981
1994 Interaction of several related GC-box- and GT-box-binding proteins with the intronic enhancer is required for differential expression of the gb110 gene in embryonal carcinoma cells. Molecular and cellular biology 18 8065313
2019 MOV10 sequesters the RNP of influenza A virus in the cytoplasm and is antagonized by viral NS1 protein. The Biochemical journal 17 30617221
2009 MOV10 as a novel telomerase-associated protein. Biochemical and biophysical research communications 17 19665004
2020 Effect of P-body component Mov10 on HCV virus production and infectivity. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 15 32496609
2017 Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin-proteasome pathway. Retrovirology 15 29258557
2016 MOV10 interacts with Enterovirus 71 genomic 5'UTR and modulates viral replication. Biochemical and biophysical research communications 14 27666477
2015 Regulation of lipid synthesis by the RNA helicase Mov10 controls Wnt5a production. Oncogenesis 14 26029828
2021 Drosophila MOV10 regulates the termination of midgut regeneration. Genetics 13 33693718
2022 Host MOV10 is induced to restrict herpes simplex virus 1 lytic infection by promoting type I interferon response. PLoS pathogens 12 35157734
2023 MOV10 recruits DCP2 to decap human LINE-1 RNA by forming large cytoplasmic granules with phase separation properties. EMBO reports 11 37437058
2014 Altered mRNA levels of MOV10, A3G, and IFN-α in patients with chronic hepatitis B. Journal of microbiology (Seoul, Korea) 11 24871977
2022 Sequestration of LINE-1 in cytosolic aggregates by MOV10 restricts retrotransposition. EMBO reports 10 35856394
2022 Evolutionary and Expression Analysis of MOV10 and MOV10L1 Reveals Their Origin, Duplication and Divergence. International journal of molecular sciences 10 35886872
1993 Consecutive inactivation of both alleles of the gb110 gene has no effect on the proliferation and differentiation of mouse embryonic stem cells. Gene 10 8482544
2021 FMRP and MOV10 regulate Dicer1 expression and dendrite development. PloS one 9 34847178
2020 Roles of MOV10 in Animal RNA Virus Infection. Frontiers in veterinary science 9 33195554
2021 MOV10 Helicase Interacts with Coronavirus Nucleocapsid Protein and Has Antiviral Activity. mBio 8 34517762
2018 RNA helicase Mov10 is essential for gastrulation and central nervous system development. Developmental dynamics : an official publication of the American Association of Anatomists 8 29266590
2023 The MOV10 RNA helicase is a dosage-dependent host restriction factor for LINE1 retrotransposition in mice. PLoS genetics 6 37126510
2017 s8ORF2 protein of infectious salmon anaemia virus is a RNA-silencing suppressor and interacts with Salmon salar Mov10 (SsMov10) of the host RNAi machinery. Virus genes 5 29218433
2024 S100A16 stabilizes the ITGA3‑mediated ECM‑receptor interaction pathway to drive the malignant properties of lung adenocarcinoma cells via binding MOV10. Molecular medicine reports 4 39450567
2023 Serine 970 of RNA helicase MOV10 is phosphorylated and controls unfolding activity and fate of mRNAs targeted for AGO2-mediated silencing. The Journal of biological chemistry 4 36871759
2023 Melatonin Regulates lncRNA NEAT1/miR-138-5p/HIF-1α Axis through MOV10 to Affect Acid-Related Esophageal Epithelial Cell Pyroptosis. Pharmacology 3 37231999
2019 Unraveling the role of the MOV10 RNA helicase during influenza A virus infection. The Biochemical journal 3 30918067
2014 [Host factor Moloney leukemia virus 10 (MOV10) protein inhibits replication of the xenotropic murine leukemia virus-related virus (XMRV)]. Bing du xue bao = Chinese journal of virology 2 25562960
2025 RNA helicase MOV10 suppresses fear memory and dendritic arborization and regulates microtubule dynamics in hippocampal neurons. BMC biology 1 39915816
2026 MOV10-mediated alternative splicing regulates mesangial cell proliferation in diabetic kidney disease. Biochimica et biophysica acta. Gene regulatory mechanisms 0 41638360
2026 MOV10 Promotes the Proliferation of Goat Mammary Epithelial Cells by Regulating the miR-21-5p-Mediated TGFβ/Smad7 Signaling Pathway. ACS omega 0 41867542
2026 Mov10 mitigates hematopoietic stem cell exhaustion under stress by modulating the Camp-mediated inflammatory pathway. Journal of genetics and genomics = Yi chuan xue bao 0 42217731
2026 Reduced MOV10 reveals novel functional cortical connections in an increased fear response. bioRxiv : the preprint server for biology 0 42239320
2025 Maximal inhibitory effect of MOV10 on LINE-1 retrotransposition requires both the MOV10/LINE-1 association and granule formation. PLoS genetics 0 40408535
2025 Functional investigation of the RNA helicase MOV10 with respect to its interplay with factors involved in nonsense-mediated mRNA decay. The Journal of biological chemistry 0 40570961
2021 Association study of hypertension susceptibility genes ITGA9, MOV10, and CACNB2 with preeclampsia in Chinese Han population. The journal of maternal-fetal & neonatal medicine : the official journal of the European Association of Perinatal Medicine, the Federation of Asia and Oceania Perinatal Societies, the International Society of Perinatal Obstetricians 0 33491517

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