| 2015 |
SPTBN1 functions as an adapter protein required for Smad3/Smad4 complex formation during TGF-β signal transduction; loss of SPTBN1 in HCC cells activates Wnt signaling by downregulating the Wnt inhibitor kallistatin, leading to decreased β-catenin phosphorylation and increased β-catenin nuclear localization. |
siRNA knockdown in HCC cell lines, Western blot, xenograft tumor assay, kallistatin restoration rescue experiments |
Hepatology |
Medium |
25307947
|
| 2013 |
SPTBN1 is a required host factor for HIV-1 infection in macrophages; it associates with HIV-1 Gag proteins. IL-27 inhibits HIV-1 infection by down-regulating SPTBN1 through a TAK-1-mediated MAPK signaling pathway. Knockdown of SPTBN1 strongly inhibits HIV-1 infection, while overexpression restores susceptibility in IL-27-treated macrophages. |
siRNA knockdown, overexpression, co-immunoprecipitation (SPTBN1 with HIV-1 Gag), IL-27 treatment with SPTBN1 modulation |
The Journal of experimental medicine |
High |
23460728
|
| 2014 |
SPTBN1 and SMAD3 collaborate to suppress STAT3 transcription in HCC; loss of SPTBN1 or SMAD3 upregulates STAT3 promoter activity via CRE and STAT-binding elements, mediated by increased binding of ATF3 and CREB2 to the STAT3 promoter CRE site. |
siRNA knockdown in HCC cell lines, luciferase reporter assay, ChIP-qPCR, Western blot, colony formation assay; validated in SPTBN1+/- mouse livers |
Carcinogenesis |
Medium |
25096061
|
| 2021 |
Loss of SPTBN1 in HCC cells increases p65 protein stability by downregulating SOCS1 (an E3 ligase of p65), leading to enhanced NF-κB activation and increased expression of pro-inflammatory cytokines IL-1α, IL-1β, and IL-6. Restoration of SOCS1 abrogates SPTBN1 loss-associated p65 elevation. |
siRNA knockdown, immunoprecipitation-Western blot, luciferase reporter assay, ChIP-qPCR, EMSA, ELISA, FACS; validated in Sptbn1+/- mice |
Theranostics |
High |
33754058
|
| 2007 |
SPTBN1-FLT3 fusion protein (from t(2;13) translocation) constitutively activates FLT3 kinase activity, transforms Ba/F3 cells to growth factor independence, and constitutively phosphorylates ERK1/2; growth is inhibited by FLT3-targeted TKIs (SU11657, PKC412, TKI258) but not imatinib. |
Ba/F3 transformation assay, RT-PCR fusion identification, phosphorylation analysis, small-molecule inhibitor dose-response |
Experimental hematology |
Medium |
17764812
|
| 2021 |
SPTBN1 promotes SETD7-mediated YAP methylation leading to YAP degradation and inactivation; loss of SPTBN1 reduces SETD7 expression, increases YAP stability and nuclear localization, and impairs autophagy in hepatic stem cells and HCC cells. YAP inhibition reverses the autophagy impairment caused by SPTBN1 deficiency. |
Sptbn1+/- mouse model with DDC treatment, rapamycin autophagy assay, YAP inhibition rescue, Western blot for SETD7/YAP |
Cellular and molecular gastroenterology and hepatology |
Medium |
34737104
|
| 2021 |
SPTBN1 and CASPASE-3 interact in the context of a high-fat/western diet: HFD/WD induces SPTBN1 and SREBP1 cleavage by CASPASE-3, and the cleaved SPTBN1 product interacts with cleaved SREBP1 to promote expression of lipogenic genes with sterol response elements, driving steatohepatitis and liver cancer. Hepatocyte-specific knockout of SPTBN1 protects mice from HFD/WD-induced liver disease. |
Hepatocyte-specific SPTBN1 knockout mice, siRNA therapy in mice, biochemical analysis of CASPASE-3 cleavage, co-immunoprecipitation of SPTBN1/SREBP1 cleavage products, human NASH tissue analysis |
Science translational medicine |
High |
34910547
|
| 2012 |
SPTBN1 directly interacts with α-synuclein via GST pull-down and co-immunoprecipitation; the two proteins colocalize in neuronal cells. SPTBN1 overexpression induces excessive neurite branching in SH-SY5Y cells, which is reversed by co-expression of α-synuclein, indicating α-synuclein modulates SPTBN1-driven neurite outgrowth. |
Phage display, GST pull-down, co-immunoprecipitation, co-localization, transfection/overexpression in SH-SY5Y cells |
Biochemical and biophysical research communications |
Medium |
22771809
|
| 2020 |
SPTBN1 suppresses JAK/STAT3 signaling in epithelial ovarian cancer via upregulation of SOCS3; loss of SPTBN1 activates p-JAK2 and p-STAT3, promotes EMT (increased Vimentin, decreased E-cadherin), and enhances cell proliferation and migration. These effects were reversed by SOCS3 overexpression or JAK2 inhibition. |
siRNA knockdown in EOC cell lines (A2780, HO8910), SOCS3 overexpression rescue, JAK2 inhibitor treatment, mouse embryonic fibroblasts from Sptbn1 KO, xenograft in vivo model, IHC |
Aging |
Medium |
32516133
|
| 2022 |
SPTBN1 functions as an RNA-binding protein that regulates the mRNA stability of GPT2 (glutamate pyruvate transaminase 2); loss of SPTBN1 upregulates GPT2, activating GPT2-dependent glycolysis to promote renal clear cell carcinoma progression. |
RNA immunoprecipitation (RIP), actinomycin D mRNA stability assay, gain/loss-of-function cell models, in vitro and in vivo assays, specific inhibitors and rescue experiments |
Journal of translational medicine |
Medium |
36527113
|
| 2023 |
SPTBN1 anchors PTTG1 (securin) in the cytoplasm, preventing its nuclear translocation and oncogenic transcriptional activity (on MMP-2 and E-cadherin). SPTBN1 downregulation causes PTTG1 nuclear translocation and promotes invasiveness. A PTTG1 deletion mutant lacking the SPTBN1-binding domain localizes strongly to the nucleus. |
PTTG1 immunoprecipitation proteomics, co-immunoprecipitation, Western blot, confocal microscopy, cytoplasmic/nuclear fractionation, deletion mutant analysis, sphere-forming assay |
International journal of molecular sciences |
Medium |
38069214
|
| 2022 |
SPTBN1 binds to PIK3R2 in fibroblast-like synoviocytes (FLSs); this interaction suppresses the PI3K/AKT signaling pathway. In SPTBN1-overexpressed RA-FLSs, PIK3R2 depletion reverses reduced MMP2, MMP9, IL-8, IL-1β, IL-6, and Bcl2 levels and increases p-PI3K and p-AKT. |
Co-immunoprecipitation (IP), Western blot, siRNA knockdown of PIK3R2, functional assays (proliferation, migration, invasion, apoptosis, inflammation) |
Immunity, inflammation and disease |
Medium |
36444616
|
| 2021 |
Loss of SPTBN1 inhibits growth and promotes EMT in breast cancer via upregulation of miR-21; this miR-21 upregulation is dependent on stability and nuclear translocation of NF-κB p65. ChIP-qPCR and immunofluorescence showed SPTBN1 regulates miR-21 at the transcriptional level through p65. |
siRNA knockdown, ChIP-qPCR, immunofluorescence, xenograft model, Western blot, qPCR |
European journal of pharmacology |
Medium |
34358482
|
| 2023 |
Tumor cell SPTBN1 inhibits M2 macrophage polarization and migration by suppressing CXCL1 expression via inhibition of p65 nuclear localization; CXCL1 neutralizing antibody reverses M2 polarization and migration promoted by SPTBN1-deficient tumor conditioned medium. |
Cytoplasmic/nuclear protein isolation, ChIP-qPCR, RT-qPCR, cell migration assays, CXCL1 neutralizing antibody rescue, co-culture experiments |
Journal of cellular physiology |
Medium |
37921259
|
| 2025 |
SPTBN1 inhibits TRIM37 expression by promoting METTL14-mediated m6A methylation of TRIM37 mRNA; this suppresses TRIM37-driven K63-linked ubiquitination of TRAF2 and downstream NF-κB activation, thereby reducing oxidative stress and inflammation in endothelial cells. |
Co-immunoprecipitation (SPTBN1-METTL14), MeRIP-qPCR (m6A methylation of TRIM37), TRIM37 overexpression rescue, AS mouse model with SPTBN1 overexpression |
European journal of medical research |
Medium |
40836352
|
| 2024 |
In osteocytes, SPTBN1 (β2-spectrin) maintains plasma membrane integrity under mechanical loading; knockdown or conditional knockout of Sptbn1 increases the number and size of plasma membrane disruptions (PMD) formed by fluid shear stress, impairs post-wounding cell survival, mildly alters calcium signaling from wounded osteocytes, and blunts bone adaptation (cortical thickening) to osteogenic tibial loading in vivo. |
siRNA knockdown in MLO-Y4 cells, diamide treatment, Sptbn1 conditional KO mice (DMP1-Cre), fluid shear stress assay, PMD quantification, calcium imaging, tibial loading in vivo protocol, histomorphometry |
Calcified tissue international |
Medium |
39276238
|
| 2025 |
IGF2BP3 interacts with NUDT21 and, by recognizing an m6A-modified site in intron 32 of SPTBN1, recruits NUDT21 to promote usage of the SPTBN1 proximal polyadenylation site, generating a short SPTBN1 transcript isoform with oncogenic activity in ovarian cancer. The long SPTBN1 isoform inhibits tumor growth and metastasis by binding CDK1 and blocking the G2/M cell cycle transition. |
IGF2BP3-NUDT21 interaction assay, m6A site identification, APA reporter assays, CDK1 co-immunoprecipitation, cell cycle analysis, in vitro and in vivo tumor growth assays |
Communications biology |
Medium |
40301554
|