Affinage

FMNL2

Formin-like protein 2 · UniProt Q96PY5

Length
1086 aa
Mass
123.3 kDa
Annotated
2026-06-09
43 papers in source corpus 20 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/7 claims corpus-supported (86%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

FMNL2 is a Diaphanous-related formin that drives actin filament elongation to power membrane protrusion, intracellular trafficking, and cell migration (PMID:22608513). Its activity is gated by cotranslational N-terminal myristoylation at Gly2 and by binding to active Cdc42, both of which are required for membrane association and targeting to lamellipodia and filopodia tips; the FH1-FH2 domain elongates (rather than nucleates) actin filaments in the presence of profilin and captures Arp2/3-generated barbed ends (PMID:22608513, PMID:22790947). The structural basis of GTPase selectivity is defined by Cdc42 contacting all five N-terminal armadillo repeats via its Rho-GTPase insert helix (PMID:25963737). At filopodia, FMNL2 acts through coupled membrane-bending and actin mechanisms: it cooperates with the I-BAR protein IRTKS, where membrane bending to recruit IRTKS is its primary filopodial function (PMID:36259517), it binds and controls the phosphorylation state and localization of fascin (PMID:32294157), and its filopodial tip localization and activity require PKCα-mediated phosphorylation of Ser1072 in the DAD domain (PMID:36979484). Beyond protrusion, FMNL2 builds a Golgi-associated actin meshwork downstream of Cdc42 to support Golgi integrity, endosome maturation, and anterograde VSV-G trafficking (PMID:28852060), mediates Rac1-dependent (Cdc42-independent) assembly of epithelial cell-cell contacts (PMID:29579104), and in oocytes localizes to the cortex and spindle periphery to drive cytoplasmic actin polymerization, spindle migration, and organelle distribution (PMID:38747713). In cancer, FMNL2 promotes invasion through multiple effector arms: a direct cortactin interaction at invadopodia (PMID:29374558), TGF-β/Smad3 and MAPK/MEK-dependent EMT (PMID:21071512), degradation of COMMD10 to de-repress NF-κB (PMID:28817833), and an FH1-SH3 interaction with SRC that promotes androgen receptor nuclear translocation (PMID:40212590). A patient-derived heterozygous L136P mutation causing loss of autoinhibition and mislocalization links FMNL2 dysfunction to impaired cell spreading, filopodia, and podosome formation (PMID:34043722).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2012 High

    Established FMNL2 as an actin-elongating formin whose membrane targeting and activity depend on N-myristoylation and Cdc42, resolving how it contributes to protrusion and migration.

    Evidence In vitro actin polymerization with profilin, G2A and Cdc42-binding mutants, RNAi with live-cell migration imaging; plus mutagenesis/inhibitor localization in HEK293T

    PMID:22608513 PMID:22790947

    Open questions at the time
    • Does not resolve how myristoylation and Cdc42 binding are coordinated temporally
    • In vivo elongation kinetics relative to other formins not defined
  2. 2015 High

    Defined the structural basis of FMNL2 GTPase selectivity, explaining why Cdc42 and not Rac1 activates it through the armadillo-repeat interface.

    Evidence X-ray crystallography of FMNL N-terminal domains with Cdc42 plus Rac1 gain-of-function mutagenesis validated in cells

    PMID:25963737

    Open questions at the time
    • Full-length autoinhibited structure not resolved
    • Membrane-engaged conformation inferred from FMNL1 dimer, not directly shown for FMNL2
  3. 2010 Medium

    Placed FMNL2 in TGF-β-induced EMT and the MAPK/MEK invasion pathway in colorectal carcinoma, connecting the formin to a transcriptional invasion program.

    Evidence siRNA and overexpression with EMT marker and signaling Western blots, MEK and PI3K inhibitor treatments

    PMID:21071512

    Open questions at the time
    • Direct molecular link between FMNL2 and MEK activation not established
    • Whether actin elongation activity is required for the signaling effect untested
  4. 2017 High

    Identified FMNL2 (with FMNL3) as a Cdc42 effector building Golgi-associated actin required for organelle integrity and anterograde trafficking, extending its role beyond the cell periphery.

    Evidence RNAi and CRISPR deletion with Golgi/endosome imaging, VSV-G trafficking assay, phalloidin staining across cell lines

    PMID:28852060

    Open questions at the time
    • Cargo selectivity of the trafficking defect not defined
    • Functional redundancy boundaries between FMNL2 and FMNL3 unresolved
  5. 2017 High

    Revealed FMNL2 drives invasion non-cytoskeletally by degrading COMMD10 to activate NF-κB, a distinct effector arm from its actin function.

    Evidence Co-IP, GST pull-down, in vitro ubiquitination, NF-κB luciferase reporter, nuclear fractionation in colorectal cancer cells

    PMID:28817833

    Open questions at the time
    • The E3 ligase recruited by FMNL2 to COMMD10 not identified
    • Whether FMNL2 acts catalytically or scaffolds degradation unclear
  6. 2018 Medium

    Resolved two parallel FMNL2 functions: a direct cortactin interaction driving invadopodia, and a Rac1-dependent role in cell-cell contact assembly distinct from its Cdc42-driven filopodia function.

    Evidence Reciprocal Co-IP/GST pull-down with invadopodia and matrix degradation assays; CRISPR KO with optogenetic Rac1 activation and Cdc42 vs Rac1 silencing

    PMID:29374558 PMID:29579104

    Open questions at the time
    • How FMNL2 switches between Cdc42- and Rac1-dependent functions unknown
    • Recruitment mechanism to junctions versus invadopodia not distinguished
  7. 2020 Medium

    Showed FMNL2 directly binds dephosphorylated fascin and governs fascin dynamics within filopodia, integrating bundling control with elongation.

    Evidence Direct binding assay, fascin phosphorylation biosensor, SIM/STED live-cell imaging with formin depletion

    PMID:32294157

    Open questions at the time
    • The kinase/phosphatase coupling fascin state to FMNL2 not identified
    • Stoichiometry of FMNL2-fascin at filopodial tips unmeasured
  8. 2022 Medium

    Reframed FMNL2's primary filopodial role as membrane bending to recruit IRTKS, with FH2 actin dynamics secondary, refining the protrusion-initiation model.

    Evidence Co-IP of FMNL2-IRTKS and FMNL2-IRSp53, coexpression filopodia assays, IRTKS/IRSp53 knockdown, dominant-negative FH2 analysis

    PMID:36259517

    Open questions at the time
    • Biophysical demonstration of FMNL2 membrane-bending activity not provided
    • Selectivity for IRTKS over IRSp53 mechanism unexplained
  9. 2023 Medium

    Defined a PKCα-FMNL2 signaling module in which Ser1072 phosphorylation in the DAD domain licenses filopodia formation, adding kinase-level control to formin activation.

    Evidence SIM imaging, S1072A and G2A mutagenesis, PKC inhibitor treatments, PKCα localization at filopodial base

    PMID:36979484

    Open questions at the time
    • Whether S1072 phosphorylation relieves autoinhibition directly not shown structurally
    • Crosstalk with Cdc42-mediated activation not mapped
  10. 2024 Medium

    Extended FMNL2 function to oocyte meiosis, where it drives cytoplasmic actin polymerization for spindle migration and organelle (mitochondria/ER) distribution.

    Evidence siRNA depletion in mouse and porcine oocytes with rescue, spindle migration imaging, organelle distribution and mitochondrial/ER stress assays, mass spectrometry interactome

    PMID:38747713

    Open questions at the time
    • Direct mechanism linking FMNL2 to organelle positioning unresolved
    • Mass spectrometry associations not validated by orthogonal binding assays
  11. 2025 Medium

    Identified an FMNL2-FH1 / SRC-SH3 interaction promoting androgen receptor nuclear translocation and enzalutamide resistance, a further non-cytoskeletal cancer effector arm.

    Evidence Co-IP with FH1/SH3 domain mapping, AR nuclear/cytoplasmic fractionation, knockdown in resistant cells, dasatinib treatment

    PMID:40212590

    Open questions at the time
    • Whether SRC kinase activity toward AR or FMNL2 itself is required unclear
    • In vivo relevance to resistant prostate tumors not established
  12. 2021 Medium

    Connected FMNL2 dysfunction to human disease through a patient-derived L136P autoinhibition-loss mutation impairing spreading, filopodia, and podosomes.

    Evidence Expression of L136P mutant in fibroblasts and THP-1 macrophages with localization, spreading, filopodia, podosome and matrix degradation assays

    PMID:34043722

    Open questions at the time
    • The specific clinical phenotype/disease entity not detailed in mechanism terms
    • Whether gain-of-function effect is dominant in vivo untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • How FMNL2's distinct effector arms — actin elongation, membrane bending, COMMD10/NF-κB degradation, SRC/AR translocation — are selected and coordinated within a single cell remains unresolved.
  • No unified model linking upstream GTPase/kinase inputs to choice of effector output
  • Whether cytoskeletal and signaling functions are mutually exclusive or simultaneous unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 3 GO:0008092 cytoskeletal protein binding 2 GO:0060089 molecular transducer activity 2
Localization
GO:0005856 cytoskeleton 2 GO:0005886 plasma membrane 2 GO:0005794 Golgi apparatus 1
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-1266738 Developmental Biology 1 R-HSA-9609507 Protein localization 1
Partners
CDC42COMMD10CTTNFMNL3FSCN1IRTKSRAC1SRC

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2012 FMNL2 is cotranslationally modified by N-terminal myristoylation, and this modification together with interaction with Cdc42 is required for proper subcellular targeting to lamellipodia and filopodia tips. In vitro, the C-terminal FH1-FH2 domain drives elongation (not nucleation) of actin filaments in the presence of profilin, and also captures and elongates filament ends generated by Arp2/3-mediated branching. RNAi-mediated silencing decreases lamellipodia protrusion rate and cell migration efficiency. In vitro actin polymerization assays with profilin, myristoylation mutants (G2A), Cdc42-binding mutants, RNAi knockdown with live-cell migration/protrusion rate measurements, subcellular localization by fluorescence microscopy Current biology : CB High 22608513
2015 Crystal structure of FMNL2 N-terminal domains (GBD/DID + armadillo repeats) in complex with active Cdc42 shows Cdc42 contacts all five armadillo repeats with specific interactions formed by the Rho-GTPase insert helix. Mutation of three residues in Rac1 creates a gain-of-function mutant that binds FMNL2 and reconstitutes the Cdc42 phenotype in vivo, demonstrating the structural basis of GTPase selectivity. FMNL1 dimerizes via a parallel coiled-coil to form an umbrella-shaped ~15 nm structure exposing six membrane interaction motifs. X-ray crystallography of FMNL1 and FMNL2 N-terminal domains with Cdc42; Rac1 gain-of-function mutagenesis validated in vivo Nature communications High 25963737
2012 N-terminal myristoylation of FMNL2 (at Gly2) is required for plasma membrane association and for FMNL2-induced cellular morphological changes. Replacement of Gly2 with Ala or pharmacological inhibition of N-myristoylation abolishes membrane localization and morphological effects. Site-directed mutagenesis (G2A), N-myristoylation inhibitor treatment, immunofluorescence localization in HEK293T cells Bioscience, biotechnology, and biochemistry Medium 22790947
2017 FMNL2 and FMNL3 localize to the Golgi apparatus in a manner requiring both N-terminal myristoylation and Cdc42 interaction. At the Golgi, they assemble a phalloidin-detectable actin meshwork. RNAi or CRISPR/Cas9 deletion of FMNL2/3 causes Golgi fragmentation, enlargement of endosomes, defective maturation/sorting into late endosomes/lysosomes, and impaired anterograde trafficking of VSV-G from Golgi to plasma membrane, placing FMNL2/3 downstream of Cdc42 in anterograde transport. RNAi, CRISPR/Cas9 gene deletion, fluorescence microscopy of Golgi markers, VSV-G trafficking assay, phalloidin staining for actin at Golgi Scientific reports High 28852060
2010 FMNL2 is required for TGF-β-induced epithelial-mesenchymal transition (EMT) in colorectal carcinoma cells; FMNL2 knockdown prevents TGF-β-induced upregulation of vimentin/snail/slug and downregulation of E-cadherin, and blocks receptor-Smad3 phosphorylation responses. FMNL2 overexpression activates p-MAPK/p-MEK (but not p-PI3K/p-AKT), and MEK inhibitor U0126 abolishes this, placing FMNL2 upstream of the MAPK/MEK pathway in invasion. siRNA knockdown, forced overexpression, Western blot for EMT markers and signaling molecules, MEK inhibitor (U0126) and PI3K inhibitor (LY294002) treatment Molecular cancer research : MCR Medium 21071512
2017 FMNL2 directly interacts with COMMD10 and targets it for ubiquitin-mediated proteasomal degradation. COMMD10 normally binds the NF-κB p65 subunit and reduces its nuclear translocation, suppressing NF-κB-dependent invasion. FMNL2-mediated COMMD10 destabilization thus activates NF-κB signaling to promote colorectal cancer invasion and metastasis. Co-immunoprecipitation, GST pull-down, immunofluorescence, in vitro ubiquitination assay, dual-luciferase NF-κB reporter assay, nuclear protein extraction assay, Western blot British journal of cancer High 28817833
2020 FMNL2 directly binds dephosphorylated fascin in filopodia and controls fascin dynamics (phosphorylation state, localization, F-actin binding) within filopodia. Fascin phosphorylation, localization, and actin binding are dependent on FMNL2 activity as revealed by a fascin biosensor and advanced live-cell imaging. Direct binding assay between FMNL2 and fascin (dephosphorylated form), fascin phosphorylation biosensor, advanced live-cell structured illumination/STED microscopy, FMNL2 formin depletion experiments The Journal of cell biology Medium 32294157
2018 Cortactin directly binds FMNL2, and this interaction promotes actin polymerization and recycling endosome motility at invadopodia. EGF/Cdc42 stimulation enhances the cortactin–FMNL2 interaction and increases invadopodia number and matrix degradation. FMNL2 is required for invadopodia formation and function in colorectal cancer cells. Co-immunoprecipitation, GST pull-down, fluorescence microscopy, actin polymerization assays, matrix degradation assays (gelatin), in vivo metastasis models Cancer letters Medium 29374558
2018 FMNL2 is required for the formation of epithelial cell-cell contacts via a Rac1-dependent but Cdc42-independent mechanism. CRISPR/Cas9 knockout of FMNL2 impairs intercellular contact establishment; optogenetic Rac1 activation recruits FMNL2 specifically to newly forming junctions, while Cdc42 silencing does not affect FMNL2-mediated contact formation. FMNL2 KO cells also show impaired filopodia formation similar to Cdc42 depletion. CRISPR/Cas9 knockout, optogenetic control of Rac1 activity, live-cell imaging of junction formation, siRNA silencing of Cdc42 vs Rac1 PloS one Medium 29579104
2022 FMNL2 cooperates with the I-BAR domain protein IRTKS (but not IRSp53) to promote filopodia assembly. FMNL2 and IRTKS are mutually dependent cofactors: FMNL2's primary function in filopodia initiation is membrane bending to recruit IRTKS, with its FH2-mediated actin dynamics being secondary. IRTKS and IRSp53 were identified as FMNL2-binding proteins. Co-immunoprecipitation (FMNL2–IRTKS and FMNL2–IRSp53 interactions), coexpression filopodia assays, siRNA knockdown of IRTKS/IRSp53, dominant-negative FH2 domain analysis The Journal of biological chemistry Medium 36259517
2023 FMNL2-dependent filopodia formation requires serine 1072 phosphorylation within the DAD domain by PKCα. N-terminal myristoylation is required for FMNL2 tip localization in filopodia. PKCα localizes to the base of growing filopodia and PKC activity is required for filopodia formation, defining a PKCα–FMNL2 signaling module. Structured illumination microscopy, phospho-site mutagenesis (S1072A), PKC inhibitor treatments, PKCα localization imaging, FMNL2 myristoylation mutant (G2A) Biomolecules Medium 36979484
2021 A patient-derived heterozygous FMNL2 L136P mutation causes subcellular mislocalization and loss of autoinhibition (gain-of-function), impairing cell spreading and filopodia formation in fibroblasts, and disrupting podosome formation and matrix degradation in THP-1 macrophages. Expression of FMNL2 L136P mutant in fibroblasts and THP-1 macrophages, fluorescence microscopy of subcellular localization, cell spreading assay, filopodia quantification, podosome formation assay, matrix degradation assay PloS one Medium 34043722
2024 In mouse and porcine oocytes, FMNL2 localizes at the oocyte cortex and spindle periphery. FMNL2 depletion reduces cytoplasmic actin polymerization, prevents spindle migration to the cortex, causes polar body extrusion failure, and disrupts mitochondria and ER distribution (reduced mitochondrial membrane potential and ER stress). Mass spectrometry identified FMNL2 association with mitochondria- and ER-related proteins. siRNA depletion in mouse and porcine oocytes, live-cell imaging of spindle migration, actin polymerization measurement, immunofluorescence of organelle distribution, mitochondrial membrane potential assay, ER stress markers, mass spectrometry co-IP, mRNA rescue injection eLife Medium 38747713
2020 Caveolin-1 (CAV1) modulates epithelial collective cell migration by controlling cortical FMNL2 availability. CAV1 depletion increases cortical FMNL2 recruitment and impairs collective (but not individual) cell migration; simultaneous FMNL2 depletion rescues the collective migration defect caused by CAV1 knockdown. RNAi (CAV1 alone and double CAV1+FMNL2), live-cell imaging of collective migration, velocity correlation length analysis Biology of the cell Low 33169848
2021 Induced depletion of Arp2/3 complex (via conditional Actr3 knockout) reproducibly increases FMNL2 and FMNL3 formin expression, correlating with explosive induction of filopodia formation, indicating a compensatory upregulation of FMNL formins when branched actin nucleation is lost. Tamoxifen-inducible conditional Arp3 knockout mouse fibroblast cell lines, Western blot for FMNL2/3 expression, fluorescence microscopy of filopodia Frontiers in cell and developmental biology Medium 33598464
2025 FMNL2 directly interacts with SRC kinase through the FMNL2-FH1 domain and SRC-SH3 domain. This interaction promotes AR (androgen receptor) translocation from cytoplasm to nucleus, increasing AR target gene expression and driving enzalutamide resistance in prostate cancer cells. Co-immunoprecipitation of FMNL2 and SRC, domain mapping (FH1 and SH3), nuclear/cytoplasmic fractionation of AR, FMNL2 knockdown in resistant cells, SRC inhibitor (dasatinib) treatment iScience Medium 40212590
2022 Knockdown of fmnl2a in zebrafish prevents gliovascular remodeling (astroglial end-foot detachment from blood vessels), reduces microglial activity, and enhances amyloidosis, demonstrating that FMNL2 controls gliovascular interactions in vivo. Zebrafish fmnl2a morpholino knockdown, live imaging of gliovascular contacts, amyloid quantification, microglial activity assessment Acta neuropathologica Low 35608697
2024 Proximity labeling (BioID) mass spectrometry identified an FMNL2 interactome including known (IRTKS) and novel interacting proteins related to filopodia, lamellipodia force generation, subcellular trafficking, cell-cell junction assembly, focal adhesion formation, and extracellular vesicle assembly. FMNL2 protein was directly detected in exosomes. BioID proximity labeling, quantitative mass spectrometry, exosome isolation and Western blot International journal of molecular sciences Low 38891874
2020 TCP11L2 interacts with FMNL2 (co-immunoprecipitation) and promotes bovine muscle-derived satellite cell migration and differentiation; FMNL2 inhibition blocks TCP11L2-mediated migration and differentiation, placing FMNL2 downstream of TCP11L2 in this pathway. Co-immunoprecipitation, CRISPR/dCas9 overexpression and repression of TCP11L2, wound-healing migration assay, FMNL2 inhibition epistasis Journal of cellular physiology Low 32017087
2022 FMNL2 suppresses breast cancer cell migration and invasion by inhibiting the RhoA/LIMK/Cofilin pathway; FMNL2 silencing activates this pathway and promotes actin cytoskeleton rearrangement. Cytoplasmic p27 promotes FMNL2-mediated cell migration through the RhoA/LIMK/Cofilin pathway. ERα overexpression reduces FMNL2 protein levels via proteasomal degradation (reversed by MG132). siRNA knockdown, forced overexpression, Rho inhibitor (ZOL) and LIMK inhibitor (BMS3) treatment, Western blot for RhoA/LIMK/Cofilin pathway, MG132 proteasome inhibitor, in vivo xenograft assay Cell death discovery Low 35379791

Source papers

Stage 0 corpus · 43 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 FMNL2 drives actin-based protrusion and migration downstream of Cdc42. Current biology : CB 172 22608513
2003 Identification and characterization of human FMNL1, FMNL2 and FMNL3 genes in silico. International journal of oncology 128 12684686
2012 MicroRNA-137, an HMGA1 target, suppresses colorectal cancer cell invasion and metastasis in mice by directly targeting FMNL2. Gastroenterology 117 23201162
2008 Overexpression of FMNL2 is closely related to metastasis of colorectal cancer. International journal of colorectal disease 72 18665374
2015 The structure of FMNL2-Cdc42 yields insights into the mechanism of lamellipodia and filopodia formation. Nature communications 69 25963737
2015 MicroRNA-206 functions as a tumor suppressor in colorectal cancer by targeting FMNL2. Journal of cancer research and clinical oncology 60 26515696
2010 FMNL2 enhances invasion of colorectal carcinoma by inducing epithelial-mesenchymal transition. Molecular cancer research : MCR 56 21071512
2011 FMNL2 is a positive regulator of cell motility and metastasis in colorectal carcinoma. The Journal of pathology 48 21506128
2015 MicroRNA-34a targets FMNL2 and E2F5 and suppresses the progression of colorectal cancer. Experimental and molecular pathology 40 26103003
2021 Induced Arp2/3 Complex Depletion Increases FMNL2/3 Formin Expression and Filopodia Formation. Frontiers in cell and developmental biology 37 33598464
2022 FMNL2 regulates gliovascular interactions and is associated with vascular risk factors and cerebrovascular pathology in Alzheimer's disease. Acta neuropathologica 35 35608697
2017 FMNL2 destabilises COMMD10 to activate NF-κB pathway in invasion and metastasis of colorectal cancer. British journal of cancer 34 28817833
2017 FMNL2 and -3 regulate Golgi architecture and anterograde transport downstream of Cdc42. Scientific reports 32 28852060
2017 Long non-coding RNA TUG1 promotes progression of oral squamous cell carcinoma through upregulating FMNL2 by sponging miR-219. American journal of cancer research 32 28979812
2016 MicroRNA-613 targets FMNL2 and suppresses progression of colorectal cancer. American journal of translational research 32 28078018
2012 Protein N-myristoylation is required for cellular morphological changes induced by two formin family proteins, FMNL2 and FMNL3. Bioscience, biotechnology, and biochemistry 32 22790947
2010 Characterization of Diaphanous-related formin FMNL2 in human tissues. BMC cell biology 30 20633255
2018 A novel long noncoding RNA, LINC00483 promotes proliferation and metastasis via modulating of FMNL2 in CRC. Biochemical and biophysical research communications 28 30594388
2016 FMNL2/FMNL3 formins are linked with oncogenic pathways and predict melanoma outcome. The journal of pathology. Clinical research 28 27499915
2020 FMNL2 regulates dynamics of fascin in filopodia. The Journal of cell biology 27 32294157
2018 Cortactin recruits FMNL2 to promote actin polymerization and endosome motility in invadopodia formation. Cancer letters 26 29374558
2019 LINC00707 promotes cell proliferation and invasion of colorectal cancer via miR-206/FMNL2 axis. European review for medical and pharmacological sciences 19 31115001
2018 KIT, NRAS, BRAF and FMNL2 mutations in oral mucosal melanoma and a systematic review of the literature. Oncology letters 16 29805686
2018 A Rac1-FMNL2 signaling module affects cell-cell contact formation independent of Cdc42 and membrane protrusions. PloS one 14 29579104
2016 A specific FMNL2 isoform is up-regulated in invasive cells. BMC cell biology 14 27578625
2024 FMNL2 regulates actin for endoplasmic reticulum and mitochondria distribution in oocyte meiosis. eLife 13 38747713
2022 circRNA TCFL5 Promote Esophageal Cancer Progression by Modulating M2 Macrophage Polarization via the miR-543-FMNL2 Axis. Journal of oncology 13 35646112
2022 Cooperative assembly of filopodia by the formin FMNL2 and I-BAR domain protein IRTKS. The Journal of biological chemistry 12 36259517
2019 MicroRNA-22 targets FMNL2 to inhibit melanoma progression via the regulation of the Wnt/β-catenin signaling pathway and epithelial-mesenchymal transition. European review for medical and pharmacological sciences 11 31298385
2022 LINC00839 promotes malignancy of liver cancer via binding FMNL2 under hypoxia. Scientific reports 10 36335129
2023 Spatiotemporal Regulation of FMNL2 by N-Terminal Myristoylation and C-Terminal Phosphorylation Drives Rapid Filopodia Formation. Biomolecules 8 36979484
2008 [Expression of FMNL2 and its relation to the metastatic potential of human colorectal cancer cells]. Nan fang yi ke da xue xue bao = Journal of Southern Medical University 8 18971169
2021 Characterization of a L136P mutation in Formin-like 2 (FMNL2) from a patient with chronic inflammatory bowel disease. PloS one 7 34043722
2020 TCP11L2 promotes bovine skeletal muscle-derived satellite cell migration and differentiation via FMNL2. Journal of cellular physiology 7 32017087
2022 FMNL2 suppresses cell migration and invasion of breast cancer: a reduction of cytoplasmic p27 via RhoA/LIMK/Cofilin pathway. Cell death discovery 6 35379791
2021 MiR-466 Inhibits the Progression of Severe Hepatocellular Carcinoma via Regulating FMNL2-Mediated Activation of NF-κB and Wnt/β-Catenin Pathways. Journal of oncology 6 34257650
2020 Caveolin-1 influences epithelial collective cell migration via FMNL2 formin. Biology of the cell 6 33169848
2017 FMNL2 with Functions Related to the Cytoskeleton is Partially Regulated by PAX6. Journal of ophthalmic & vision research 4 29090051
2026 TTC19 and FMNL2 gene variants in a pediatric case of mitochondrial disorder with renal tubular acidosis. Mitochondrion 0 42250897
2025 FMNL2/SRC-mediated androgen receptor translocation into the nucleus promotes enzalutamide resistance of prostate cancer. iScience 0 40212590
2025 The formin FMNL2 plays a role in the response of melanoma cells to substrate stiffness. BMC molecular and cell biology 0 40301744
2024 Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry. International journal of molecular sciences 0 38891874
2023 [Effect of miR-22 Targeting FMNL2 on Cell Migration and Apoptosis in Childhood Acute Myeloid Leukemia]. Zhongguo shi yan xue ye xue za zhi 0 38071036

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