| 2018 |
FBP17 and CIP4 prime the plasma membrane for fast endophilin-mediated endocytosis (FEME) by recruiting the 5'-lipid phosphatase SHIP2 and lamellipodin to mediate local production of phosphatidylinositol-3,4-bisphosphate and endophilin pre-enrichment. Membrane-bound GTP-loaded Cdc42 recruits FBP17 and CIP4, which are then locally deactivated by RICH1 and SH3BP1 GAPs, generating transient assembly and disassembly of endophilin spots. |
Colocalization screens of BAR domain proteins with endophilin, Co-IP, lipid phosphatase recruitment assays, live imaging of endophilin foci dynamics |
Nature cell biology |
High |
30061681
|
| 2001 |
FBP17 interacts with sorting nexin SNX2 as identified by yeast two-hybrid screening of a human kidney library, providing a link between the EGF receptor pathway and FBP17. FBP17 contains a C-terminal SH3 domain, an N-terminal region homologous to cdc15 (an actin cytoskeleton regulator in S. pombe), and a consensus Rho-binding motif; however, none of the Rho family proteins tested interacted with FBP17 in yeast two-hybrid assays. |
Yeast two-hybrid screen, domain analysis |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
11438682
|
| 2009 |
FBP17 recruits WASP, WIP (WASP-interacting protein), and dynamin-2 to the plasma membrane, and this recruitment is necessary for the formation of podosomes and phagocytic cups in macrophages. The N-terminal EFC/F-BAR domain of FBP17 mediates membrane binding and deformation, enabling simultaneous membrane deformation and actin polymerization at the same sites. |
FBP17 knockdown/overexpression, fluorescence microscopy, domain deletion constructs, podosome and phagocytic cup formation assays |
The Journal of biological chemistry |
High |
19155218
|
| 2019 |
FBP17 is recruited to caveolae to induce formation of caveolar rosettes and buffer plasma membrane tension. c-Abl tyrosine kinase directly phosphorylates the FBP17 F-BAR domain in response to mechanical tension, which inhibits FBP17 membrane-bending activity and releases FBP17-controlled inhibition of mDia1-dependent stress fibers, allowing membrane adaptation to increased mechanical tension. |
FBP17 knockout cells, osmotic shock assays, phosphorylation assays with c-Abl, live imaging, caveolar rosette quantification, stress fiber analysis |
Nature communications |
High |
31862885
|
| 2011 |
FBP17 localizes to invadopodia in invasive bladder tumor cells, and its knockdown decreases invadopodia formation to 13–14% of control and decreases invasive capacity to 14–16%. Both the EFC/F-BAR domain (membrane deformation) and the SH3 domain (dynamin-2 recruitment) of FBP17 are necessary for invadopodia formation and invasion. |
FBP17 knockdown, phalloidin staining for invadopodia, Transwell invasion assay, domain mutant constructs |
The Journal of urology |
Medium |
21421245
|
| 2003 |
FBP17 binds to tankyrase (TNKS), an ADP-ribose polymerase involved in telomere maintenance and MAPK signaling, via a specific TNKS-binding motif in FBP17. This interaction was identified by yeast two-hybrid assay and confirmed by co-immunoprecipitation of endogenous proteins in 293T cells. |
Yeast two-hybrid assay, co-immunoprecipitation of endogenous proteins in 293T cells |
FEBS letters |
Medium |
14596906
|
| 2009 |
FBP17-induced membrane tubulation directs actin polymerization toward membrane tubules, suggesting that actin polymerization occurs toward the neck of endocytic vesicles during clathrin-dependent endocytosis to facilitate vesicle fission. |
Fluorescence imaging of actin dynamics at FBP17-induced membrane tubules |
FEBS letters |
Low |
19835875
|
| 2020 |
The F-BAR domain of FBP17 alone displays minimal curvature-sensing activity in vitro. Instead, an alternatively spliced intrinsically disordered region (IDR) adjacent to the F-BAR domain has curvature-sensing ability greatly exceeding that of the F-BAR domain alone. In living cells, presence of the IDR delayed FBP17 recruitment in curvature-coupled cortical waves. |
Nanobar-supported lipid bilayer system for in vitro curvature sensing, live cell imaging of cortical waves |
iScience |
Medium |
33205024
|
| 2021 |
FBP17 accumulates at the interface between RasV12-transformed and normal cells and promotes formation of finger-like membrane protrusions that mediate cell competition. Cdc42 acts upstream of FBP17 in this process. FBP17 plays a positive role in apical elimination of RasV12 cells from the epithelium. |
Electron microscopy of cell interfaces, FBP17 knockdown/overexpression, fluorescence imaging, Cdc42 epistasis experiments |
iScience |
Medium |
34485872
|
| 2024 |
FNBP17 interacts with Daam1 formin, co-localizes with it in an actin cytoskeletal complex responsive to Wnt stimulation, and is required for vertebrate gastrulation in Xenopus. FNBP1 and Daam1 function within the same non-canonical Wnt signaling pathway, as suboptimal doses of both synergize to produce severe gastrulation defects. FNBP1 can induce intracellular tubule-like structures and localizes to focal adhesions. |
Co-IP/domain interaction mapping, immunofluorescence co-localization, Xenopus loss-of-function (morpholino knockdown), genetic epistasis (synergy between FNBP1 and Daam1) |
Developmental biology |
Medium |
38945423
|
| 2018 |
FBP17 associates with dynamin and cortactin in invasive breast cancer cells (MDA-MB-231), and its stable knockdown compromises ECM degradation, demonstrating a role in invadopodia-mediated invasion. |
Co-immunoprecipitation, stable shRNA knockdown, ECM degradation assay |
Medical oncology |
Low |
29651632
|
| 2024 |
Membrane curvature triggers condensation and activation of N-WASP orchestrated by FBP17: FBP17 senses curvature via its BAR domain and induces hierarchical assembly of FBP17/N-WASP clusters that activate N-WASP in synergy with Cdc42. The stoichiometry of FBP17 to N-WASP within multivalent assemblies is modulated by local curvature radius to tune actin nucleation. |
Nanolithography-controlled curvature substrates, reconstituted Cdc42/FBP17/N-WASP system in vitro, quantitative imaging of condensate formation and actin polymerization |
The EMBO journal |
High |
41484371
|
| 2023 |
FNBP1 promotes cervical cancer cell survival through constitutive activation of the FAK/PI3K/AKT/mTOR signaling pathway. FNBP1 knockdown reduces cell adhesion, attenuates FAK/PI3K/AKT signaling, and leads to apoptosis. EGF treatment rescues all FNBP1 knockdown effects except the cell adhesion decrease, indicating FNBP1 maintains FAK activity by promoting cell adhesion. |
siRNA knockdown, phospho-signaling assays (FAK, PI3K, AKT, mTOR), apoptosis assays, EGF rescue experiments, cell adhesion assays |
Cells |
Medium |
37566043
|
| 2025 |
FNBP1 interacts with LASP1, upregulates LASP1 protein expression, and subsequently activates the Smad3 signaling pathway to promote glycolysis in glioblastoma cells. FNBP1 mRNA stability is enhanced by RBM15B-mediated m6A modification recognized by IGF2BP2. |
Co-IP (FNBP1-LASP1 interaction), m6A modification assays (RBM15B, IGF2BP2), shRNA knockdown, glycolysis assays, xenograft mouse models |
Drug development research |
Medium |
41086050
|
| 2025 |
FBP17 overexpression induces premature neurite outgrowth in cortical neurons in culture, and either knockdown or overexpression of FBP17 disrupts radial neuron migration and neurite dynamics in vivo in the developing mouse cortex, demonstrating FBP17 is essential for proper cortical neuron migration. |
In utero electroporation with Double UP technique for concurrent knockdown/overexpression comparison, in vivo mouse cortex migration assays |
The Journal of neuroscience |
Medium |
40721321
|
| 2021 |
Sp1 transcription factor drives FNBP1 expression in EMT-type gastric cancer cells; pharmacological inhibition and knockdown of Sp1 reduced FNBP1 promoter activity and transcription. Loss of FNBP1 results in loss of 3D invasive ability and reduced actin dynamics. |
Promoter analysis, Sp1 inhibitor/knockdown experiments, FNBP1 knockdown, 3D invasion assay, live imaging of actin dynamics |
International journal of molecular sciences |
Medium |
34202606
|
| 2022 |
Wild-type p53 suppresses FBP17 expression; cell lines with mutant p53 express higher FBP17, and stabilization of wild-type p53 reduces FBP17 levels. Double knockdown of p53 and FBP17 showed FBP17 contributes to invasion when p53 loses regulatory control, placing FBP17 downstream of p53 in an invasion-regulatory axis. |
p53 stabilization experiments, FBP17 expression measurement, double knockdown epistasis, invasion assays, IHC of breast cancer tissue microarrays |
Carcinogenesis |
Low |
35134126
|