Related Experiment Video
Updated: Jan 17, 2026

Mapping the Structure-Function Relationships of Disordered Oncogenic Transcription Factors Using Transcriptomic Analysis
Published on: June 27, 2020
FET fusion oncoproteins enrich SWI/SNF complex subtypes and interaction partners
Malin Lindén1, Lisa Andersson1, Heba Albatrok1
1Department of Laboratory Medicine, Institute of Biomedicine, Sahlgrenska Center for Cancer Research, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
FET oncoproteins interact with SWI/SNF complexes in sarcomas, influencing their composition and function. These interactions, along with epigenetic changes, contribute to specific tumor types in FET sarcoma.
Area of Science:
- Oncology
- Molecular Biology
- Epigenetics
Background:
- FET (FUS, EWSR1, TAF15) fusion oncoproteins are key in sarcomas and leukemias.
- FET oncoproteins interact with SWI/SNF chromatin remodeling complex subtypes.
- The precise impact on SWI/SNF composition and epigenetic effects is not fully understood.
Purpose of the Study:
- To investigate how FET oncoproteins affect SWI/SNF complex composition and interactomes.
- To determine the downstream epigenetic consequences in FET sarcomas.
Main Methods:
- Utilized immunoprecipitation and quantitative mass spectrometry.
- Validated complex composition and interactions using glycerol gradient sedimentation and co-immunofluorescence.
- Analyzed chromatin accessibility (ATAC-seq) and gene regulation (RNA-seq) in FET sarcomas.
Main Results:
- FET sarcomas exhibit distinct SWI/SNF complex compositions with unique subunit paralogs and interaction partners.
- FET oncoproteins do not significantly disrupt SWI/SNF complex integrity.
- FUS::DDIT3-bound SWI/SNF complexes in myxoid liposarcoma are enriched in PBAF and GBAF components.
Conclusions:
- FET oncoproteins function with assembled, functional SWI/SNF complexes and recruited partners.
- SWI/SNF composition, interactomes, and epigenetics collectively influence FET sarcoma tumor type.
Related Concept Videos
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
Protein Complexes with Interchangeable Parts
Tagging and Fusion Proteins
SNAREs and Membrane Fusion
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Fusion of Secretory Vesicles with the Plasma Membrane
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...

