| 1996 |
hnRNPM proteins (72.5–74 kDa doublet) are components of hnRNP complexes and associate with the nuclear matrix during heat shock; monoclonal antibodies against synthetic hnRNPM peptides directly inhibit in vitro splicing, and heat-shocked nuclear extracts lacking hnRNPM lose splicing capacity, indicating hnRNPM is required for pre-mRNA splicing. |
Monoclonal antibody inhibition of in vitro splicing; heat-shock nuclear extract fractionation; cDNA cloning and sequencing; in situ hybridization (gene mapped to chromosome 19) |
Nucleic acids research |
High |
8692693
|
| 2010 |
hnRNP-M directly interacts with spliceosome proteins CDC5L and PLRG1 in vivo; a central region of hnRNP-M is required for this interaction. This interaction is inhibited during heat-shock stress. An hnRNP-M mutant lacking the CDC5L/PLRG1 interaction domain cannot modulate alternative 5′ and 3′ splice site choices of an adeno-E1A mini-gene substrate. |
Co-immunoprecipitation (in vivo); domain deletion mutagenesis; mini-gene alternative splicing assay |
EMBO reports |
High |
20467437
|
| 2014 |
hnRNPM promotes breast cancer metastasis by activating an alternative splicing switch during EMT, including switching CD44 from the epithelial (CD44v) to mesenchymal (CD44s) isoform. hnRNPM acts in a mesenchymal-specific manner by competing with the epithelial splicing regulator ESRP1 for the same GU-rich cis-regulatory RNA elements. Enforced CD44s expression overrides hnRNPM loss and restores EMT and metastasis. |
Genome-wide RNA-seq; shRNA knockdown and overexpression in cell lines and mouse metastasis models; epistasis (CD44s rescue experiment); ESRP1 competition assay |
Genes & development |
High |
24840202
|
| 2015 |
hnRNPM and p54nrb/NONO cooperate as components of protein complexes bound to both the FGF1 promoter and the FGF1 mRNA IRES to activate IRES-dependent translation during myoblast differentiation in a promoter-dependent manner. Knockdown of either protein blocks FGF1 induction and myotube formation. |
RNA immunoprecipitation; co-immunoprecipitation; knockdown/overexpression; mRNA transfection; promoter deletion assays |
PloS one |
Medium |
26332123
|
| 2017 |
hnRNPM regulates an alternative splicing program in Ewing sarcoma cells downstream of PI3K/AKT/mTOR pathway inhibition; hnRNPM binding motifs are enriched in introns flanking BEZ235-regulated exons, and knockdown of hnRNPM abolishes a subset of BEZ235-induced splicing changes and enhances cytotoxicity. |
Splicing-sensitive arrays; bioinformatics motif enrichment; shRNA knockdown; clonogenicity assays |
Nucleic acids research |
Medium |
29036465
|
| 2018 |
hnRNPM and ESRP1 coregulate overlapping sets of cassette exon alternative splicing events in a largely discordant (antagonistic) manner; GU-rich motifs downstream of hnRNPM-repressed/ESRP1-enhanced exons support a model of competitive binding to these cis-elements during EMT. |
Genome-wide RNA-seq comparison of hnRNPM and ESRP1 splicing targets; motif enrichment analysis near coregulated exons |
RNA (New York, N.Y.) |
Medium |
30042172
|
| 2018 |
A cancer-associated MORC2 M276I mutation enhances binding of MORC2 to hnRNPM; this interaction promotes an hnRNPM-mediated CD44 splicing switch from CD44v to CD44s, driving EMT and lung metastasis. Knockdown of hnRNPM reduces mutant MORC2 binding to CD44 pre-mRNA and reverses the splicing switch. |
Co-immunoprecipitation; shRNA knockdown; splicing assays; cell migration/invasion assays; mouse lung metastasis model |
Cancer research |
Medium |
30093560
|
| 2019 |
Under hypoxia, hnRNPM translocates from nucleus to cytoplasm where it binds target mRNA IRESs and promotes IRES-dependent translation initiation of a distinct set of genes involved in metabolic processes and cancer neoplasia. |
Proteomic/bioinformatic identification of hnRNPM as IRES-interacting factor; subcellular fractionation showing cytosolic translocation under hypoxia; transcriptomic and translatomic analyses; mouse carcinogenesis model |
EBioMedicine |
Medium |
30852162
|
| 2019 |
hnRNPM is a negative regulator of RLR-mediated innate antiviral signaling; viral infection causes translocation of hnRNPM from the nucleus to the cytoplasm, where it interacts with RIG-I and MDA5 and impairs their binding to viral RNA, thereby inhibiting innate antiviral responses. |
Overexpression and knockdown experiments; viral infection assays; Co-immunoprecipitation of hnRNPM with RIG-I and MDA5; RNA-binding competition assay; subcellular fractionation |
PLoS pathogens |
Medium |
31433824
|
| 2020 |
hnRNPM physically and functionally interacts with Matrin-3 (MATR3) in an RNA-dependent manner in mammalian cells; in Drosophila, rump (the hnRNPM homolog) modifies mutant MATR3 toxicity in vivo, and common RNA targets converge on biological processes important for neuronal health. |
Co-immunoprecipitation (RNA-dependent, mammalian cells); Drosophila genetic modifier screen; eCLIP dataset analysis |
Acta neuropathologica communications |
Medium |
32811564
|
| 2021 |
HNRNPM binds to GU-rich elements in long flanking proximal introns of key homeostatic gene transcripts to prevent aberrant exon inclusion and backsplicing events (circular RNA formation), thereby maintaining transcriptome integrity and supporting prostate cancer cell growth. |
Pooled shRNA screens (in vitro and in vivo); eCLIP-seq; RNA-seq; splice-switching antisense oligonucleotides |
eLife |
High |
34075878
|
| 2021 |
hnRNPM directly interacts with CDR1as circular RNA in periodontal ligament stem cells (PDLSCs) and regulates its expression, thereby influencing PDLSC stemness through the CDR1as/miR-7/KLF4 axis. |
RNA immunoprecipitation; knockdown and overexpression experiments; stemness and differentiation assays |
Journal of cellular and molecular medicine |
Low |
33837664
|
| 2021 |
Knockdown of hnRNPM in the mouse CA1 hippocampal region impairs learning and memory, reduces pre- and post-synaptic protein levels (synaptophysin and PSD95), impairs dendritic spine morphology, and hnRNPM directly binds to the 3′UTR of synaptophysin and PSD95 mRNAs to stabilize them. |
In vivo shRNA knockdown in mouse CA1; behavioral memory tests; immunofluorescence/western blot; RNA immunoprecipitation (3′UTR binding) |
Neuroscience letters |
Medium |
33727124
|
| 2021 |
circURI1 directly interacts with hnRNPM to modulate alternative splicing of genes involved in cell migration, thereby suppressing gastric cancer metastasis. |
RNA pulldown; RNA immunoprecipitation; alternative splicing analysis (RNA-seq); in vitro migration/invasion assays; in vivo metastasis model |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
34385309
|
| 2022 |
HNRNPM regulates alternative splicing of MBD2 pre-mRNA by binding to its flanking introns, generating isoforms with opposing roles; MBD2a promotes FZD3 expression and activates Wnt/β-catenin signaling, driving cancer stemness and immune evasion in hepatocellular carcinoma. |
RIP-seq; RNA-seq; chromatin immunoprecipitation; knockdown/antisense oligonucleotides; CD8+ T cell co-culture assays |
Cellular and molecular gastroenterology and hepatology |
Medium |
35158098
|
| 2024 |
hnRNPM preferentially binds to GU-rich elements at intronic LINE transposable elements in deep introns to repress pseudo splice site usage and suppress cryptic exon inclusion; loss of hnRNPM leads to cryptic exons that generate long dsRNAs (via base-pairing of inverted ALU elements among LINEs), triggering an interferon response. |
eCLIP-seq; RNA-seq; loss-of-function experiments; dsRNA detection; interferon pathway analysis; immune cell infiltration analysis in hnRNPM-deficient tumors |
Molecular cell |
High |
38815579
|
| 2024 |
hnRNPM is a positive regulator of IRF3 phosphorylation and type-I IFN induction downstream of both cGAS/STING and RIG-I/MAVS pathways; hnRNPM interacts with ELAVL1/HuR, TBK1, IKKε, IKKβ, and NF-κB p65, and confocal microscopy shows cytosolic/perinuclear co-localization of hnRNPM, ELAVL1, and TBK1. |
Interactome analysis by mass spectrometry; genome editing (knockouts); confocal microscopy; viral infection assays (HSV-1, Sendai virus); IRF3 phosphorylation assays |
The EMBO journal |
Medium |
39707025
|
| 2024 |
FMRP interacts with hnRNPM to recognize splice sites and modulate exon-skipping splicing of SLC7A11 pre-mRNA, generating a specific SLC7A11-S splice variant that promotes ferroptosis resistance in breast cancer cells. |
Co-immunoprecipitation of FMRP and hnRNPM; splicing assays; overexpression/knockdown experiments; ferroptosis assays |
Redox biology |
Medium |
39388855
|
| 2024 |
PARP4 interacts with hnRNPM as a novel binding partner (identified by quantitative mass spectrometry interactomics); loss of PARP4 or hnRNPM results in overlapping intronic splicing perturbations and promotes lung adenocarcinoma tumorigenicity. |
Quantitative mass spectrometry interactomics; transcriptomic splicing analysis; in vitro and in vivo tumorigenicity assays |
Genome medicine |
Medium |
39034402
|
| 2025 |
hnRNPM is SUMOylated at lysine 17; SENP1 is the de-SUMOylation enzyme (eraser). SUMOylated hnRNPM interacts with PFKFB3 and inhibits its phosphorylation and nuclear localization, thereby suppressing glycolysis. SUMO-deficient hnRNPM promotes colorectal cancer cell proliferation and tumorigenesis in mice. |
Global SUMOylated proteomic screening; site-specific mutagenesis (K17); Co-immunoprecipitation; SUMO-deficient mutant in vivo mouse model; lactate production and PFKFB3 phosphorylation assays |
Cancer letters |
Medium |
39983892
|
| 2025 |
hnRNPM interacts with PTBP1 to co-regulate alternative splicing during spermatogenesis; conditional knockout of hnRNPM in germ cells causes male infertility, sperm morphology defects, and 1617 alternative splicing changes including abnormal exon skipping in Cep152, Cyld, Inpp4b, and Cd59b. |
Conditional knockout mouse model; co-immunoprecipitation and mass spectrometry (identifying PTBP1 interaction); RNA-seq (alternative splicing analysis) |
Reproductive biology and endocrinology |
Medium |
39780247
|
| 2025 |
AURKB binds to HNRNPM and interferes with HNRNPM's interaction with PSAT1 mRNA, thereby suppressing HNRNPM-mediated PSAT1 mRNA degradation and increasing PSAT1 protein levels; this represents a kinase-independent oncogenic function of AURKB in colorectal cancer. |
Co-immunoprecipitation; proximity ligation assay; RNA immunoprecipitation-qPCR; mRNA stability assays; mass spectrometry |
Journal of experimental & clinical cancer research |
Medium |
40784984
|
| 2025 |
hnRNPM directly binds via its RRM2 domain to constitutive exon 9 of PLEKHB2 pre-mRNA, facilitating skipping of alternative exon 8 and generating the PLEKHB2-S isoform that promotes colorectal cancer cell proliferation. |
In vivo CLIP assay; minigene reporter splicing assay; RNA-seq; knockdown experiments in vitro and in vivo |
Oncogene |
Medium |
41109930
|
| 2025 |
hnRNPM interacts with BCAS2 (a known splicing factor) in oocytes and modulates BCAS2 binding to pre-mRNA loci to control alternative splicing; conditional ablation of hnRNPM in oocytes causes cytoplasmic defects, meiotic arrest, and complete female infertility, with widespread alternative splicing disruption identified by SCAN-seq and LACE-seq. |
Genetic ablation (conditional knockout); SCAN-seq (novel isoform discovery); LACE-seq (single-nucleotide resolution binding sites); Co-immunoprecipitation of hnRNPM with BCAS2 |
Nature communications |
High |
41680151
|
| 2025 |
hnRNPM promotes apoptosis in pseudorabies virus (PRV)-infected cells by upregulating cleaved caspase-3, -6, -7, and Bax while downregulating Bcl-2; PRV infection induces nuclear translocation of hnRNPM, and hnRNPM co-localizes with caspase-6. |
Overexpression and knockdown in PK15/3D4/21 cells; viral replication assays; western blot for apoptosis markers; subcellular fractionation; co-localization (immunofluorescence) |
Veterinary microbiology |
Low |
40068468
|
| 2025 |
KHSRP interacts with hnRNPM, which directly binds to GPX4 mRNA; hnRNPM overexpression rescues the decrease in GPX4 expression and ferroptosis induced by KHSRP knockdown, indicating that the KHSRP-hnRNPM complex regulates GPX4 mRNA stability post-transcriptionally. |
Co-immunoprecipitation; RNA immunoprecipitation; knockdown/overexpression rescue experiments; ferroptosis assays (lipid peroxidation, MDA, GSH) |
Experimental cell research |
Low |
41176204
|