| 2002 |
STEAP2 (STAMP1) protein localizes to the Golgi complex (predominantly trans-Golgi network), plasma membrane, and vesicular tubular structures in the cytosol; it colocalizes with early endosome antigen 1 (EEA1), suggesting involvement in secretory/endocytic pathways. |
GFP-fusion construct imaged by quantitative time-lapse and immunofluorescence confocal microscopy; colocalization with EEA1 marker |
The Journal of biological chemistry |
Medium |
12095985
|
| 2002 |
STEAP2 protein localizes mainly to the plasma membrane, as demonstrated by GFP fusion construct. |
GFP fusion construct and fluorescence microscopy |
Laboratory investigation; a journal of technical methods and pathology |
Low |
12429817
|
| 2010 |
STEAP2 (STAMP1) promotes prostate cancer cell proliferation and survival: ectopic expression increased proliferation and activated ERK signaling, while siRNA knockdown inhibited growth, induced cell cycle arrest, and increased apoptosis (including TRAIL-induced apoptosis). Knockdown cells showed dramatically reduced xenograft growth in nude mice. |
Ectopic overexpression in DU145/COS-7 cells; siRNA knockdown in LNCaP cells; cell cycle analysis; apoptosis assays; ERK activation by Western blot; nude mouse xenograft |
Cancer research |
High |
20587517
|
| 2014 |
STEAP2 overexpression in normal prostate epithelial PNT2 cells conferred the ability to migrate and invade, establishing a direct functional role for STEAP2 in driving invasive behavior. |
STEAP2 overexpression in PNT2 cells; migration and invasion assays (transwell) |
Clinical & experimental metastasis |
Medium |
25248617
|
| 2018 |
STEAP2 knockdown in PC3 and LNCaP prostate cancer cells significantly decreased invasion; downstream targets identified include MMP3, MMP10, MMP13, FGFR4, IL1β, KiSS1, SERPINE1 (PC3), MMP7 (LNCaP), and CD82 (both lines), indicating STEAP2 regulates invasion-related gene expression programs. |
siRNA knockdown; proliferation, migration, and invasion assays; gene expression analysis |
Scientific reports |
Medium |
29674723
|
| 2018 |
STEAP2 undergoes rapid internalization from the cell surface and traffics to the Golgi region and endosome-like puncta; acute inhibition of endocytosis increases detectable STEAP2 at the plasma membrane. Membrane cholesterol content modulates a conformation-sensitive epitope in the second extracellular loop of STEAP2, suggesting cholesterol-dependent conformational regulation during trafficking. STEAP2's metalloreductase activity was not detectable at the plasma membrane (negative finding). |
Monoclonal antibody recognizing conformation-sensitive epitope; antibody internalization assay; cholesterol manipulation; endocytosis inhibition; cell-based metalloreductase activity assay using STEAP4 as positive control |
Experimental cell research |
Medium |
29940176
|
| 2019 |
STEAP2 upregulation in breast cancer cells inhibited EMT and suppressed PI3K/AKT/mTOR signaling pathway activity, reducing proliferation and invasion; conversely, STEAP2 downregulation promoted EMT and activated PI3K/AKT/mTOR signaling. |
Lentiviral overexpression and shRNA knockdown; Western blot for PI3K/AKT/mTOR phosphorylation; EMT marker profiling; in vitro invasion assays; in vivo xenograft |
Cancer biology & therapy |
Medium |
31696760
|
| 2022 |
METTL3-mediated m6A modification of STEAP2 mRNA stabilizes STEAP2 mRNA and promotes its translation in an m6A-dependent manner via the reader protein YTHDF1; this METTL3-STEAP2 axis suppresses EMT and Hedgehog signaling in papillary thyroid cancer cells. |
m6A modification assays; METTL3 overexpression/silencing; YTHDF1 reader identification; rescue experiments; cell proliferation, migration and invasion assays; in vivo xenograft |
Cell death & disease |
Medium |
35436987
|
| 2022 |
STEAP2 promotes osteosarcoma cell EMT, invasion, and migration via the PI3K/AKT/mTOR signaling axis; EFEMP2 overexpression reduces invasiveness and EMT partly by targeting STEAP2, and EFEMP2-induced PI3K/AKT/mTOR activation and EMT are abrogated when STEAP2 or Akt is knocked down, placing STEAP2 downstream of EFEMP2 in this pathway. |
STEAP2 and EFEMP2 overexpression/knockdown; Western blot for PI3K/AKT/mTOR; EMT markers; invasion/migration assays; epistasis via double KD; in vivo assays |
Cancer biology & therapy |
Medium |
36316642
|
| 2024 |
STEAP2 functions as a metalloreductase that drives HCC cell migration and invasion by increasing intracellular copper levels and activating stress-activated MAP kinases p38 and JNK; copper supplementation rescued migration defects caused by STEAP2 knockdown, and p38 or JNK inhibitors blocked copper-mediated migration rescue. |
Stable STEAP2 KD and overexpression in HCC cell lines; intracellular copper measurement; Western blot for p38 and JNK activation; copper rescue experiment; p38/JNK pharmacological inhibition; in vitro migration/invasion; in vivo tumor growth |
Scientific reports |
High |
38830975
|
| 2025 |
High-resolution crystal structures of the STEAP2 N-terminal cytosolic oxidoreductase domain (OxRD) bound to NADPH were solved; single-crystal spectroscopy directly validated the redox state of bound NADPH. Comparison with cryo-EM structure revealed conformational differences in the FAD-binding region, suggesting domain reorientation between OxRD and the transmembrane domain facilitates FADH2 loading and FAD release as part of the electron transfer pathway (NADPH→FAD→heme→extracellular metal ions). |
High-resolution X-ray crystallography; single-crystal UV-visible spectroscopy for redox-state validation; comparison with cryo-EM structure |
The Journal of biological chemistry |
High |
41101505
|
| 2026 |
ETV1 transcriptionally activates miR-3175 through direct promoter binding; miR-3175 directly suppresses STEAP2 expression via conserved 3'UTR binding sites; STEAP2 functions as a tumor suppressor in glioma such that its overexpression inhibits malignant phenotypes. This ETV1/miR-3175/STEAP2 axis was confirmed by rescue experiments. |
Chromatin immunoprecipitation (ChIP); luciferase reporter assays; biotin-streptavidin pulldown; RNA immunoprecipitation; gain/loss-of-function studies; rescue experiments; in vivo xenograft |
BioFactors (Oxford, England) |
Medium |
41856673
|