| 2002 |
SSX2IP was identified as a direct binding partner of SSX2 via yeast two-hybrid screening, and the interaction was confirmed by GST pull-down assay in vitro. SSX2IP interacts with the N-terminal moiety of SSX2. SSX2IP colocalizes with SSX2 in the nucleus of transfected cells. |
Yeast two-hybrid, GST pull-down assay, immunofluorescence of transfected cells |
Genes, chromosomes & cancer |
Medium |
12007189
|
| 2013 |
SSX2IP accumulates at spindle poles in a Dynein-dependent manner in Xenopus egg extracts, interacts with the γ-tubulin ring complex (γ-TuRC) and centriolar satellite protein PCM-1. Immunodepletion of SSX2IP impedes γ-TuRC loading onto centrosomes, leading to reduced microtubule nucleation and spindle assembly failure. In medaka blastomeres and somatic cells, SSX2IP knockdown causes fragmentation of pericentriolar material and chromosome segregation errors, establishing SSX2IP as a centrosome maturation and maintenance factor. |
Quantitative proteomics, immunodepletion in Xenopus egg extracts, co-immunoprecipitation, morpholino knockdown in medaka embryos, siRNA knockdown in somatic cells |
The Journal of cell biology |
High |
23816619
|
| 2013 |
SSX2IP localizes to the basal body of primary cilia in human and murine ciliated cells. siRNA knockdown of SSX2IP in human cells reduces recruitment of Cep290 to both centriolar satellites and the basal body, drastically reduces entry of the BBSome and Rab8 accumulation at the ciliary base, limits targeting of the ciliary membrane protein somatostatin receptor 3, and significantly reduces axoneme length. SSX2IP is thus a targeting factor for ciliary membrane proteins that cooperates with Cep290, the BBSome, and Rab8. |
siRNA knockdown, immunofluorescence, localization studies in human and murine ciliated cells |
Molecular biology of the cell |
High |
24356449
|
| 2014 |
hMsd1/SSX2IP is delivered to the centrosome in a centriolar satellite-dependent manner and binds the γ-tubulin complex. Depletion of hMsd1/SSX2IP leads to disorganized interphase microtubules and misoriented mitotic spindles with reduced length, establishing SSX2IP as a microtubule-anchoring protein. Knockdown of the zebrafish orthologue causes ciliary defects and disturbed left-right asymmetry, confirming a conserved role in ciliogenesis. |
siRNA knockdown, co-immunoprecipitation, immunofluorescence, zebrafish morpholino knockdown |
EMBO reports |
High |
24397932
|
| 2015 |
hMsd1/SSX2IP-mediated microtubule anchoring to the centrosome is essential for proper centriole assembly and duplication. Upon hMsd1/SSX2IP knockdown, centriolar satellites become stuck at the microtubule minus end near the centrosome and accumulate centrosomal proteins ectopically. Microtubule structures (even when not properly anchored) are still required for satellite aggregation. Superresolution and electron microscopy revealed faulty centriole structures under these conditions. SSX2IP-depleted cells are insensitive to Plk4 overproduction-induced ectopic centriole formation but accelerate centrosome reduplication upon hydroxyurea arrest. |
siRNA knockdown, superresolution microscopy, electron microscopy, Plk4 overexpression epistasis, hydroxyurea arrest |
Molecular biology of the cell |
High |
25833712
|
| 2015 |
Wdr8 constitutively localizes to the proximal end of the mother centriole and forms a complex with hMsd1/SSX2IP identified by mass spectrometry. Wdr8 depletion reduces recruitment of hMsd1/SSX2IP to the mitotic centrosome (but not vice versa), and knockdown of either protein produces similar spindle defects (shortened and misoriented spindle microtubules), placing Wdr8 upstream of hMsd1/SSX2IP in centrosome function. |
Mass spectrometry, co-immunoprecipitation, siRNA knockdown, superresolution microscopy, immunofluorescence |
Biochemical and biophysical research communications |
Medium |
26545777
|
| 2021 |
Targeted proximity biotinylation identified SSX2IP as a binding partner of the N-terminal domain of Wtip (a LIM-domain adaptor). Physical association was confirmed and the two proteins formed mixed aggregates upon overexpression. Double depletion of Wtip and SSX2IP in Xenopus embryos disrupted neural tube closure, indicating a functional interaction during neurulation and cell junction remodeling. |
Targeted proximity biotinylation (BirA-anti-GFP), co-expression aggregation assay, double morpholino knockdown in Xenopus embryos |
PloS one |
Medium |
34710136
|
| 2024 |
SSX2IP physically interacts with FANCI (FA Complementation Group I) as confirmed by co-immunoprecipitation. SSX2IP positively regulates FANCI expression, and FANCI overexpression partially rescues the anti-proliferative and anti-migratory effects of SSX2IP knockdown in breast cancer cells, placing SSX2IP upstream of FANCI in a pro-tumorigenic pathway. |
Co-immunoprecipitation, siRNA knockdown, overexpression rescue, functional proliferation/migration assays, xenograft |
Cell biology international |
Medium |
39533770
|
| 2026 |
SSX2IP was confirmed as a direct transcriptional/functional target of miR-625-3p by reporter assays, and its upregulation promotes cisplatin export via extracellular vesicles in ovarian cancer cells, thereby enhancing cisplatin resistance. Mass spectrometry and high-speed confocal microscopy supported SSX2IP's role in mediating EV-based cisplatin secretion. |
Luciferase reporter assay, mass spectrometry, high-speed confocal microscopy, cell death ELISA, in vitro and in vivo functional assays |
Cancers |
Medium |
41827805
|