| 2020 |
PFN2 is a stable interaction partner of the actin N-terminal acetyltransferase NAA80. PFN2 binding to NAA80 via NAA80's proline-rich loop specifically increases NAA80's intrinsic catalytic activity. NAA80, actin, and PFN2 form a ternary complex (shown by SAXS), and PFN2 binding promotes interaction between the globular domains of actin and NAA80, facilitating actin N-terminal acetylation. The majority of cellular NAA80 is stably bound to PFN2 rather than actin, suggesting the PFN2-NAA80 complex acetylates G-actin before filament incorporation. |
Interaction proteomics, analytical ultracentrifugation, in vitro enzyme assays, small-angle X-ray scattering (SAXS), deletion mutagenesis of NAA80 proline-rich loop |
The Journal of biological chemistry |
High |
32978259
|
| 2020 |
PFN2 is a target of the miR-290 family of microRNAs in embryonic stem cells (ESCs). In the absence of miRNAs, PFN2 is upregulated in ESCs, causing decreased endocytosis, impaired ERK signaling, delayed cell cycle progression, and repressed differentiation. Knockout of Pfn2, reintroduction of miR-290, or disruption of the PFN2-dynamin interaction domain all reversed the endocytosis defect. Mutagenesis of the single canonical conserved 3' UTR miR-290-binding site of Pfn2 or overexpression of Pfn2 ORF alone in wild-type cells largely recapitulated these phenotypes. |
miRNA knockout ESCs, Pfn2 knockout, miR-290 re-introduction, Pfn2 3'UTR mutagenesis, endocytosis assays, ERK signaling assays, cell cycle analysis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
32788350
|
| 2018 |
PFN2 is ubiquitinated via differential ubiquitin-linkages (for either degradation or as a regulatory signal) by the E3 ligase cIAP1 (cellular inhibitor of apoptosis 1), targeting PFN2 for proteasomal degradation. PFN2 levels regulated by cIAP1 affect intracellular levels of reactive oxygen species. |
Ubiquitination assays, proteasome inhibition, E3 ligase identification, ROS measurement |
Biochemical and biophysical research communications |
Medium |
30352681
|
| 2021 |
In high-glucose conditions, the transcription factor ETS1 cooperates with KMT5A (which mediates H4K20 monomethylation) to regulate PFN2 promoter activity and transcription, driving endothelial-to-mesenchymal transition (EndMT) in glomerular endothelial cells. ChIP assays showed H4K20me1 and ETS1 occupy the PFN2 promoter region. Knockdown of ETS1 suppressed high glucose-induced PFN2 expression and EndMT, while ETS1 overexpression-mediated EndMT was reversed by PFN2 knockdown. KMT5A upregulation suppressed PFN2 and EndMT, while sh-KMT5A-mediated EndMT was counteracted by PFN2 knockdown. |
ChIP assay, dual luciferase reporter assay, siRNA knockdown, overexpression, Western blot, immunofluorescence, in vivo DN model |
Molecular medicine (Cambridge, Mass.) |
Medium |
34238215
|
| 2025 |
The m6A reader hnRNPA2B1 binds to the m6A site ('AGACU') of PFN2 mRNA and enhances its stability. This hnRNPA2B1-PFN2 axis promotes ferroptosis in cardiomyocytes during myocardial ischemia-reperfusion injury, as evidenced by increased lipid ROS, MDA, and Fe2+. PFN2 knockdown attenuated ferroptosis in hnRNPA2B1-overexpressing cardiomyocytes. |
m6A reader interaction studies, RNA stability assay, siRNA knockdown, overexpression, ferroptosis marker measurement (lipid ROS, MDA, Fe2+, GSH, FTH1), in vitro OGD/R model and in vivo MIRI model |
Free radical biology & medicine |
Medium |
40010516
|
| 2024 |
Transcription factor SIX2 directly binds to the PFN2 promoter and promotes PFN2 transcription. In turn, PFN2 promotes mRNA stability of SIX2 by recruiting RNA-binding protein YBX-1, and subsequently activates the downstream MAPK/JNK pathway, forming a SIX2/PFN2 positive feedback loop that enhances gastric cancer cell stemness. |
ChIP, Co-immunoprecipitation, IP-MS, RNA stability assay, RNA-sequencing, JNK pathway inhibition, gain- and loss-of-function experiments |
Journal of translational medicine |
Medium |
39256760
|
| 2024 |
The Pfn2 3'UTR contains both a miR-290 binding site and an Iron Response Element (IRE). Deletion of the IRE leads to decreased PFN2 protein, a Wnt signaling defect, reduced nuclear beta-catenin, and a block in mesendodermal lineage differentiation. Deletion of the miR-290 site leads to increased PFN2 and reduced FGF signaling during pluripotency transition. This coordinated miRNA-IRE axis on the Pfn2 transcript controls two sequential signal transduction steps during ESC differentiation into primary germ layers. |
3'UTR mutagenesis (IRE deletion, miRNA site deletion), ESC differentiation assays, Wnt/FGF signaling readouts, nuclear beta-catenin measurement |
bioRxivpreprint |
Medium |
bio_10.1101_2024.10.02.616359
|
| 2020 |
PFN2 promotes proliferation, migration, invasion, and epithelial-to-mesenchymal transition (EMT) in triple-negative breast cancer (TNBC) cells. PFN2 overexpression upregulates Smad2 and Smad3, further inducing EMT. PFN2-overexpressing cells exhibit stronger tumorigenicity in vivo. |
CCK-8 assay, transwell migration/invasion assay, Western blot (Smad2/3, EMT markers), xenograft tumor model |
Breast cancer (Tokyo, Japan) |
Low |
33047272
|
| 2022 |
OCT1 transcription factor directly regulates PFN2 expression in AR-negative castration-resistant prostate cancer cells, as identified by ChIP-seq. PFN2 knockdown by siRNA significantly inhibited migration of AR-negative prostate cancer cells and showed a marked inhibitory effect on tumor growth in vivo. |
ChIP-seq, siRNA knockdown, cell migration assay, in vivo tumor growth assay, immunohistochemistry |
Scientific reports |
Medium |
35413990
|