| 1999 |
EHD1 was identified as a member of the EH-domain-containing protein family, with an EH domain at its C-terminus (including an EF Ca2+-binding motif), a central coiled-coil structure, and a nucleotide-binding consensus site (P-loop) at its N-terminus. As a GFP fusion protein, EHD1 localizes to transferrin-containing endocytic vesicles in cultured cells. |
cDNA cloning, domain analysis, GFP fusion protein live-cell imaging |
Genomics |
Medium |
10395801
|
| 2001 |
EHD1 interacts directly with SNAP29 (GS32) via its EH domain and with alpha-adaptin of AP-2, forms complexes with IGF-1R in endocytic vesicles, and co-localizes intracellularly with IGF-1R after IGF-1 stimulation. Overexpression of EHD1 suppresses IGF-1-mediated MAPK and Akt phosphorylation, establishing EHD1 as a negative regulator of IGF-1 signaling. |
Co-immunoprecipitation, co-localization immunofluorescence, overexpression with downstream signaling readout (MAPK/Akt phosphorylation) |
The Journal of biological chemistry |
Medium |
11423532
|
| 2002 |
EHD1 associates with Arf6-containing long membrane tubules and induces tubule formation. Mutations in the N-terminal P-loop domain or deletion of the C-terminal EH domain prevent tubule association and tubule induction. EHD1-associated tubules contain MHC-I molecules trafficked through the Arf6 clathrin-independent pathway, and EHD1 overexpression enhances MHC-I recycling to the plasma membrane. Tubule formation requires nucleotide cycling on Arf6 and intact microtubules. |
Transgenic tagged EHD1 expression, domain deletion/point mutation analysis, MHC-I recycling assay, immunofluorescence co-localization, Arf6 dominant-negative/active mutants |
The EMBO journal |
High |
12032069
|
| 2002 |
EHD1 and EHD3 interact with each other as shown by yeast two-hybrid assay and confirmed by co-immunoprecipitation. The N-terminal domain of EHD proteins is responsible for tubular vs. vesicular localization, and both N-terminal and C-terminal (EH) domains of EHD3 are required for its tubular localization. Co-expression of EHD1 and EHD3 results in their colocalization on microtubule-dependent tubular structures. |
Yeast two-hybrid, co-immunoprecipitation, GFP fusion proteins, chimeric domain swapping, fluorescence microscopy |
Traffic (Copenhagen, Denmark) |
High |
12121420
|
| 2004 |
EHD1 directly interacts with Rabenosyn-5 (a Rab4/Rab5 effector) via the EH domain of EHD1 and the first two NPF motifs of Rabenosyn-5. RNAi depletion of EHD1 delays recycling of transferrin and MHC-I, causing cargo accumulation in a compact juxtanuclear compartment. Simultaneous RNAi of both proteins phenocopies Rabenosyn-5 depletion alone, establishing that Rabenosyn-5 acts upstream of EHD1 in endocytic recycling from early endosomes to the endosomal recycling compartment and back to the plasma membrane. |
GST pulldown from brain cytosol, mass spectrometry identification, co-immunoprecipitation, RNAi knockdown, recycling assays, immunofluorescence |
Molecular biology of the cell |
High |
15020713
|
| 2004 |
EHD1 interacts through its EH domain with EHBP1, and both EHD1 and EHBP1 are required for perinuclear localization of GLUT4-containing membranes and insulin-stimulated recycling of GLUT4 to the plasma membrane in adipocytes. A dominant-negative EHD1 lacking the EH domain (ΔEH-EHD1) disperses perinuclear GLUT4 and inhibits GLUT4 translocation. |
Co-immunoprecipitation, dominant-negative overexpression, siRNA knockdown, immunofluorescence co-localization, glucose transport assay |
The Journal of biological chemistry |
High |
15247266
|
| 2004 |
EHD1 interacts with GS32/SNAP-29 via the EH domain binding to the N-terminal NPF-containing region of GS32, and with syndapin II via the EH domain binding to NPF repeats. These two interactions are mutually exclusive. Both interactions were confirmed by co-immunoprecipitation from cell extracts. |
GST pulldown, co-immunoprecipitation, competition binding assay |
Molecular membrane biology |
Medium |
15371016
|
| 2006 |
EHD1 knockout mice show delayed recycling of transferrin to the plasma membrane with accumulation in the endocytic recycling compartment, confirming the role of EHD1 in exit of membrane proteins from recycling endosomes in vivo. |
Ehd1 knockout mouse model, transferrin recycling assay in embryonic fibroblasts |
Traffic (Copenhagen, Denmark) |
High |
16445686
|
| 2007 |
EHD1 directly and preferentially binds phosphatidylinositols (preferring PI with a phosphate at position 3) via a positively charged lysine residue (Lys-483) in the third helix of the EH domain, on the opposite face from the NPF-binding pocket. This phospholipid-binding activity was characterized by 2D NMR analysis. |
Lipid-binding assay (dot blot/overlay), 2D NMR analysis, site-directed mutagenesis (K483 substitution) |
The Journal of biological chemistry |
High |
17412695
|
| 2007 |
EHD1 interacts with retromer and co-localizes with retromer on tubular/vesicular endosomes. P-loop mutation of EHD1 exerts a dominant-negative effect on retromer localization and endosome-to-Golgi retrieval. RNAi-mediated EHD1 depletion destabilizes SNX1-positive tubules and inhibits endosome-to-Golgi retrieval of the cation-independent mannose 6-phosphate receptor. |
Comparative proteomics, co-immunoprecipitation, P-loop dominant-negative mutation, RNAi knockdown, retrograde trafficking assay |
Traffic (Copenhagen, Denmark) |
High |
17868075
|
| 2007 |
EHD1 regulates beta1 integrin recycling from a transferrin-containing endocytic recycling compartment to the plasma membrane. EHD1 knockout MEFs display lower surface beta1 integrin but higher activated beta1 integrin, larger focal adhesions (slower disassembly), and impaired cell spreading and migration on fibronectin. These defects are rescued by re-introduction of wild-type EHD1. |
EHD1 knockout MEFs, RNAi knockdown, integrin recycling assay, focal adhesion analysis, cell migration and spreading assay |
Journal of cell science |
High |
17284518
|
| 2007 |
Myosin Vb interacts with Rab8a (confirmed by yeast two-hybrid and FRET), and Rab8a co-localizes with Myosin Vb on a tubular network containing EHD1 and EHD3 that is distinct from the Rab11a compartment, defining a separate non-clathrin recycling pathway. |
Yeast two-hybrid, FRET, fluorescence microscopy co-localization |
Molecular biology of the cell |
Medium |
17507647
|
| 2007 |
The solution NMR structure of the C-terminal 133 residues of EHD1 (including the EH domain) was solved. While overall resembling the second EH domain of Eps15, the EHD1 EH domain has significant differences in surface charge and the NPF/DPF tripeptide-binding pocket. |
NMR spectroscopy, solution structure determination |
Journal of biomolecular NMR |
High |
17899392
|
| 2007 |
EHD1 depletion in EHD1 knockout MEFs reduces cholesterol uptake via LDL receptor, results in reduced esterified and free cholesterol levels, and smaller lipid droplets. These phenotypes are rescued by wild-type but not dysfunctional EHD1, implicating EHD1 in LDL receptor internalization and cholesterol homeostasis. |
EHD1 knockout MEFs, siRNA, cholesterol measurement, lipid droplet analysis, LDL receptor internalization assay, rescue with wild-type EHD1 |
Biochemical and biophysical research communications |
Medium |
17451452
|
| 2008 |
EHD1 undergoes serine phosphorylation, enhanced by serum stimulation, with PKC identified as one of the relevant kinases. Inhibitors of clathrin-mediated endocytosis decrease EHD1 phosphorylation, suggesting phosphorylation occurs between early endosomes and the endocytic recycling compartment. |
Phosphorylation assay, serum stimulation, PKC inhibitors, endocytosis inhibitors, immunoprecipitation |
Cellular & molecular biology letters |
Medium |
18661112
|
| 2009 |
C. elegans AMPH-1 (Amphiphysin/BIN1 ortholog) co-localizes with RME-1 (EHD1 ortholog) on recycling endosomes; AMPH-1 deletion mutants show defective recycling endosome morphology and function. AMPH-1 NPF motifs bind to the RME-1 EH domain to promote cargo recycling. Human BIN1 is required for EHD1-regulated endocytic recycling. In vitro, purified AMPH-1 and RME-1 together produce short coated membrane tubules distinct from those made by either protein alone. |
In vivo C. elegans genetics, co-localization, in vitro membrane tubulation reconstitution with purified proteins, EH-domain binding assay |
Nature cell biology |
High |
19915558
|
| 2009 |
MICAL-L1 interacts with EHD1 via its NPF motifs (binding the EH domain of EHD1), recruits EHD1 to long tubular recycling endosomes, and links EHD1 and Rab8a on these structures. MICAL-L1 depletion causes loss of EHD1 and Rab8a from tubular membranes and impairs endocytic recycling of transferrin and integrin receptors. |
Co-immunoprecipitation, siRNA knockdown, in vitro binding assay, live-cell imaging, immunofluorescence co-localization |
Molecular biology of the cell |
High |
19864458
|
| 2010 |
EHD1 is essential for spermatogenesis; EHD1 knockout male mice are infertile with abnormal acrosomal development, clumping of acrosomes, misaligned spermatids, absence of mature spermatozoa, and abnormal phagocytosis of elongated spermatids by Sertoli cells. |
Cre/loxP conditional knockout mice, histopathology, light and electron microscopy, in situ hybridization, immunohistochemistry |
BMC developmental biology |
High |
20359371
|
| 2010 |
EHD1 binds directly to the second C2 domain of Fer1L5, and reduction of EHD1 inhibits myoblast fusion and impairs Fer1L5 translocation to the plasma membrane. |
Direct protein binding assay, siRNA knockdown, myoblast fusion assay, membrane localization analysis |
The Journal of biological chemistry |
Medium |
21177873
|
| 2010 |
Overexpression of EHD1 impairs L1/NgCAM endocytosis in neurons (but not in fibroblasts), while downregulation of EHD1 causes increased endosomal accumulation of NgCAM. Balanced EHD1:EHD4 levels are required for NgCAM endocytosis; EHD1 oligomerization is required for the endocytosis defect. An endogenous EHD1-EHD4 complex was identified. |
shRNA knockdown, overexpression, endocytosis assay, co-immunoprecipitation, live imaging |
The Journal of neuroscience |
Medium |
20463227
|
| 2010 |
In neurons, EHD1 functions primarily at EEA1-positive early endosomes. Downregulation of EHD1 delays exit of L1/NgCAM from EEA1-positive endosomes, impairing axonal targeting. EHD1 stably associates with endosomal membranes during maturation into EEA1-positive compartments. |
shRNA knockdown, live imaging, immunofluorescence, endosomal maturation tracking |
The Journal of neuroscience |
Medium |
21147988
|
| 2010 |
EHD1 interacts with snapin via its EH domain, competes with SNAP-25 for overlapping binding sites on the C-terminus of snapin, and affects synaptotagmin-1 coupling to the SNARE complex. EHD1 overexpression reduces depolarization-induced exocytosis in PC12 cells; this effect requires the EH domain since N-terminal EHD1 (unable to bind snapin) does not reduce exocytosis. |
Yeast two-hybrid, EH domain binding assay, electrophysiology/exocytosis assay, SNARE complex analysis |
Molecular and cellular neurosciences |
Medium |
20696250
|
| 2010 |
EHD1 depletion causes rapid Rab5-independent coalescence of CD59 (a GPI-AP) in the endocytic recycling compartment region, revealing a role for EHD1 in regulating CD59 trafficking from pre-sorting endosomes to the ERC in a PKC-dependent manner. |
siRNA knockdown, Arf6-Q67L dominant-active mutant, PKC inhibitor treatment, immunofluorescence |
Traffic (Copenhagen, Denmark) |
Medium |
20961375
|
| 2012 |
EHD1 is required for retrograde transport of Shiga toxin B from recycling endosomes to the TGN, while CI-M6PR retrograde trafficking was not significantly dependent on EHD1, demonstrating cargo-selective roles in retrograde traffic. |
EHD1 knockdown, retrograde trafficking assay with Shiga toxin B and CD8-CI-M6PR, immunofluorescence |
Traffic (Copenhagen, Denmark) |
Medium |
22540229
|
| 2012 |
Rabankyrin-5 interacts with EHD1 via the EH domain binding to the NPFED motif of Rank-5, confirmed by GST-pulldown, yeast two-hybrid, isothermal calorimetry, and co-immunoprecipitation. Rank-5 also interacts with retromer component Vps26. Depletion of Rank-5 causes mislocalization of Vps26, impairs mannose 6-phosphate receptor retrieval, and depletion of either Rank-5 or EHD1 impairs VSV-G secretion. |
GST-pulldown, yeast two-hybrid, isothermal calorimetry, co-immunoprecipitation, siRNA knockdown, trafficking assays |
Traffic (Copenhagen, Denmark) |
High |
22284051
|
| 2012 |
cPLA2α and EHD1 interact in vivo (co-proximity <40 nm, co-immunoprecipitation). Depletion of cPLA2α induces hypertubulation of CD59-containing endosomes, and depletion of EHD1 similarly induces hypertubulation, while lysophospholipid accumulation causes vesiculation. Results indicate cPLA2α and EHD1 cooperate in vesiculation of GPI-AP-containing endosomes. |
Co-immunoprecipitation, proximity ligation assay (<40 nm), siRNA knockdown, lipid manipulation, immunofluorescence morphology |
Molecular biology of the cell |
Medium |
22456504
|
| 2014 |
GRAF1 forms a complex with EHD1 and MICAL-L1. GRAF1 overexpression causes vesiculation of MICAL-L1-containing tubular recycling endosomes, while GRAF1 depletion leads to impaired TRE vesiculation and delayed receptor recycling. Co-addition of purified EHD1 and GRAF1 in a semi-permeabilized cell vesiculation assay produces synergistic tubular recycling endosome vesiculation. |
Co-immunoprecipitation, siRNA knockdown, overexpression, semi-permeabilized cell vesiculation assay with purified proteins, immunofluorescence |
Frontiers in cell and developmental biology |
Medium |
25364729
|
| 2014 |
EHD1 depletion impairs receptor recycling and mislocalizes caveolin-3 and Fer1L5 in myoblasts, reduces myoblast fusion, and causes smaller muscles in vivo. EHD1 localizes to the T-tubule in skeletal muscle, and its loss leads to T-tubule overgrowth with excess vesicle accumulation. EHD1 ATPase domain is required for tubule formation in myoblasts, and EHD1 regulates BIN1-induced tubule formation. |
EHD1-null mice, myoblast fusion assay, T-tubule morphology analysis by electron microscopy, ATPase domain mutants, BIN1 tubulation assay |
Developmental biology |
High |
24440153
|
| 2014 |
MICAL-L1 and EHD1 are required for Src activation and transport to the cell periphery in response to growth factor and integrin stimulation. MICAL-L1-mediated recruitment of EHD1 to Src-containing recycling endosomes is required for release of Src from the perinuclear endocytic recycling compartment. |
siRNA knockdown, Src kinase activation assay, immunofluorescence localization, co-immunoprecipitation, migration/spreading assay |
Journal of cell science |
Medium |
24481818
|
| 2014 |
Depletion of EHD1 or MICAL-L1 results in increased numbers of bi-nucleated cells due to impaired recycling endosome transport during late cytokinesis. MICAL-L1 but not EHD1 depletion also causes aberrant chromosome alignment and lagging chromosomes, indicating an EHD1-independent mitotic role for MICAL-L1. Both proteins influence microtubule dynamics during mitosis. |
siRNA knockdown, bi-nucleation quantification, live-cell imaging of cytokinesis, chromosome analysis |
Traffic (Copenhagen, Denmark) |
Medium |
25287187
|
| 2015 |
EHD1 and EHD3 function in early ciliogenesis by promoting membrane tubulation and ciliary vesicle formation from distal appendage vesicles (DAVs) at the mother centriole, working in association with the Rab11-Rab8 cascade. EHD1 and EHD3 localize to preciliary membranes and the ciliary pocket. EHD-dependent membrane tubulation drives mother centriole to basal body transformation and recruits transition zone proteins and IFT20. SNAP29 (an EHD1-binding protein and SNARE regulator) is also required for DAV-mediated ciliary vesicle assembly. |
siRNA knockdown, live-cell imaging, electron microscopy, immunofluorescence localization, Rab11/Rab8 cascade manipulation |
Nature cell biology |
High |
25686250
|
| 2015 |
PS flipping by the P4-ATPase ATP8A1 is required for EHD1 recruitment to recycling endosomes. Depletion of ATP8A1 impairs PS asymmetry in recycling endosomes, dissociates EHD1 from recycling endosomes, and generates aberrant endosomal tubules resistant to fission. EHD1 did not show membrane localization in cells defective in PS synthesis. |
siRNA knockdown of ATP8A1, PS distribution analysis, EHD1 localization assay, endosomal tubule morphology analysis |
The EMBO journal |
High |
25595798
|
| 2016 |
EHD1 knockout in mice on a B6 background causes embryonic lethality at mid-gestation with failure of neural tube closure, axial turning, and neural tube patterning. Ehd1-null embryos display short stubby cilia on neuroepithelium at E9.5. Loss of EHD1 deregulates ciliary SHH signaling with downregulation of GLI3 repressor formation and increase in SHH-specified ventral neuronal markers. EHD1 co-localizes with and directly binds Smoothened in primary cilia upon ligand stimulation, co-trafficking with Smoothened into developing primary cilia. |
EHD1 knockout mice, immunofluorescence, co-immunoprecipitation (EHD1-Smoothened), cilia morphology analysis, SHH pathway readouts |
Scientific reports |
High |
26884322
|
| 2018 |
EHD1 forms membrane-active scaffolds when ATP-bound that bulge tubular membranes. ATP hydrolysis promotes scaffold self-assembly, causing extension and thinning of membrane tube intermediate regions, leading to scission of tubes below 25 nm radius. Deletion of N-terminal residues causes defects in stable scaffolding, scission, and endocytic recycling. Cross-complementation assays in C. elegans confirm that both membrane binding and ATP hydrolysis activities are necessary for endocytic recycling. |
In vitro membrane tubulation with purified EHD1, supported membrane tubes assay, molecular dynamics simulation, C. elegans cross-complementation, N-terminal deletion mutants |
Nature communications |
High |
30518883
|
| 2018 |
EHD1 is identified as an ATP-dependent membrane fission catalyst, distinct from GTP-dependent dynamin. In a screen using supported membrane tubes monitored by microscopy, EHD1 drives ATP-dependent membrane tube scission. |
Supported membrane tube fission assay, biochemical fractionation, mass spectrometry identification |
Biochemistry |
High |
30403133
|
| 2019 |
MICAL-L1 recruits EHD1 to basal bodies to promote ciliogenesis. MICAL-L1 knockdown prevents CP110 removal from the mother centriole (similar to EHD1 knockdown) and prevents EHD1 localization to basal bodies. MICAL-L1 directly interacts with α-tubulin-β-tubulin heterodimers and γ-tubulin at centrosomes, suggesting centriolar tubulin anchors MICAL-L1 which then recruits EHD1. |
siRNA knockdown, mass spectrometry, direct binding assay (MICAL-L1 with tubulins), immunofluorescence localization, co-localization analysis |
Journal of cell science |
Medium |
31615969
|
| 2020 |
EHD4 preferentially dimerizes with EHD1 and is required for the recruitment of EHD1 to sorting endosomes. EHD4 knockdown (by siRNA, shRNA, or CRISPR/Cas9) leads to impaired EHD1 SE-recruitment and enlarged sorting endosomes. EHD1 binding partners Rabenosyn-5, Syndapin2, and MICAL-L1 (NPF motif-containing proteins localized to sorting endosomes) are each required for EHD1 recruitment to sorting endosomes; knockdown of any one leads to enlarged sorting endosomes. |
Co-immunoprecipitation (EHD4-EHD1 dimerization), siRNA/shRNA/CRISPR knockdown, endosomal size quantification, EHD1 localization assay |
PloS one |
Medium |
32966336
|
| 2020 |
SNX17 directly interacts with EHD1. Internalization of LRP1 (a SNX17 cargo) recruits cytoplasmic EHD1 to endosomal membranes. EHD1 depletion results in larger SNX17-containing endosomes, suggesting impaired EHD1-mediated endosomal fission downstream of SNX17-dependent cargo sorting. |
Co-immunoprecipitation, in vitro binding assay, endosomal size quantification, EHD1 recruitment assay |
The Journal of biological chemistry |
Medium |
32041776
|
| 2020 |
EHD1 knockdown impairs Cx43 internalization in cardiomyocytes, preserving gap junction-intercellular coupling. EHD1 interaction with Cx43 is mediated by Eps15 and is promoted by Cx43 phosphorylation and ubiquitination. EHD1 overexpression accelerates Cx43 internalization and exacerbates ischemia-induced Cx43 lateralization. |
siRNA knockdown, overexpression, co-immunoprecipitation, gap junction coupling assay, immunofluorescence |
Circulation research |
Medium |
32138615
|
| 2022 |
Coronin2A (CORO2A) is a novel EHD1 interaction partner. CORO2A localizes to endosomal structures as well as stress fibers. CORO2A depletion impairs recycling of clathrin-independent cargo and causes enlarged endosomes, supporting a role in EHD1-mediated endosomal fission. CORO2A depletion decreases internalization of clathrin-dependent cargo but does not affect uptake of clathrin-independent cargo. |
Co-immunoprecipitation, siRNA knockdown, cargo recycling and uptake assays, immunofluorescence |
Molecular biology of the cell |
Medium |
35921168
|
| 2022 |
A homozygous missense variant (p.R398W) in EHD1 causes autosomal recessive tubular proteinuria and sensorineural deafness in humans. In silico analysis predicts R398W destabilizes the protein and impairs nucleotide binding, leading to defective EHD1 oligomerization and membrane remodeling. Ehd1 knockout and knockin mice recapitulate the renal (impaired receptor-mediated endocytosis in proximal tubules) and auditory phenotypes. Ciliogenesis appeared unaffected in patients and mouse models. |
Human genetics (homozygous missense), knockout and knockin mouse models, zebrafish model, receptor-mediated endocytosis assay, in silico structural analysis |
Journal of the American Society of Nephrology |
High |
35149593
|
| 2023 |
EHD1 promotes CP110 ubiquitination during ciliogenesis by transporting centriolar satellites (containing the E3 ubiquitin ligase HERC2) to the mother centriole. HERC2 and MIB1 were identified as E3 ligases that interact with and ubiquitinate CP110. HERC2 is required for ciliogenesis and localizes to centriolar satellites. EHD1 controls centriolar satellite movement to deliver HERC2 for CP110 ubiquitination and degradation. |
co-immunoprecipitation, siRNA knockdown, ubiquitination assay, centriolar satellite transport imaging, immunofluorescence |
EMBO reports |
High |
37074924
|
| 2023 |
EHD1 is required for endocytic recycling and Golgi-to-plasma membrane traffic of IGF-1R to maintain IGF-1R surface expression and downstream signaling in Ewing sarcoma cells. EHD1 overexpression-dependent oncogenic traits require IGF-1R expression and kinase activity, establishing RTK traffic regulation as a proximal oncogenic mechanism. |
shRNA knockdown, CRISPR knockout, mouse Ehd1 rescue, RTK antibody array, IGF-1R surface expression and signaling assays |
Communications biology |
Medium |
37474760
|
| 2009 |
Drosophila Past1 (ortholog of EHD1) is involved in endocytosis; Past1 mutant garland cells show markedly decreased fluorescent avidin endocytosis. Past1 mutants are infertile, temperature-sensitive, and die prematurely. Past1 genetically interacts with Notch signaling pathway components. |
P-element excision mutants, fluorescent endocytosis assay, genetic interaction analysis |
Journal of cell science |
Medium |
19174465
|
| 2021 |
EHD1 contributes to 14-3-3ζ dimerization and subsequent β-catenin/c-Myc signaling activation in NSCLC cells. Co-IP, native gel electrophoresis, and immunoblotting showed the EHD1/14-3-3ζ interaction. This activates a positive feedback circuit: c-Myc binds the EHD1 promoter and transcriptionally activates EHD1. |
Co-immunoprecipitation, native gel electrophoresis, ChIP analysis of EHD1 promoter, siRNA knockdown, Wnt pathway inhibitor |
Cancer letters |
Medium |
34217785
|
| 2025 |
EHD1 interacts with PD-L1 protein (confirmed by molecular docking, immunofluorescence, and immunoprecipitation) and promotes PD-L1 endosomal recycling back to the cell surface. EHD1 knockdown inhibits PD-L1 recycling and promotes its lysosomal degradation. EHD1 mRNA carries m6A modification recognized by YTHDF1, which enhances EHD1 mRNA stability in an m6A-dependent manner. |
Molecular docking, co-immunoprecipitation, immunofluorescence, receptor internalization and recycling assays, MeRIP-qPCR, RIP assay, m6A-binding site mutation |
Cancer communications |
Medium |
40703029
|