Experimental Data on TRIM28-MAVS Ubiquitination in Antiviral Signaling

This dataset contains experimental results from a study on the TRIM28 protein's role in antiviral innate immunity. The research includes data from TRIM28 overexpression and knockdown systems, protein interaction assays, and in vivo validation using an AAV-mediated lung-specific model. It examines CRM1-dependent nuclear export of TRIM28 and its promotion of K48-linked ubiquitination on MAVS to suppress RIG-I signaling.

Use Cases

• Analyze confocal microscopy data on virus-induced nucleocytoplasmic trafficking of TRIM28 to quantify cytoplasmic accumulation.
• Use co-immunoprecipitation assay data to map protein interactions between TRIM28 and MAVS.
• Examine in-cell ubiquitination assay results to characterize K48-linked polyubiquitination events on MAVS.
• Evaluate data from TRIM28 domain deletion constructs to assess the functional requirement of the RBCC domain.
• Analyze results from MAVS lysine mutants (e.g., Lys136, Lys461) to identify key ubiquitination sites affecting downstream signaling.

Strengths

• Data underpins a peer-reviewed mechanistic study published on figshare.
• Includes both in vitro and in vivo validation from an AAV-mediated lung-specific knockdown model.
• Assays cover multiple experimental techniques: confocal microscopy, co-immunoprecipitation, and ubiquitination assays.
• Released under a permissive CC BY 4.0 license for reuse.

Limitations

• The dataset is small at 12.0 MB, indicating it contains summary results rather than raw high-throughput data.
• Sample data and column definitions are unavailable, complicating direct computational analysis.
• The data is specific to a single study's molecular biology experiments, limiting generalizability.

Provenance

Source

figshare, authored by Ruihua Xin.

Collection Method

Generated via laboratory experiments including protein overexpression/knockdown, confocal microscopy, co-immunoprecipitation, and ubiquitination assays.

Freshness

Last updated March 24, 2026.