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TRIM21 undergoes phase separation dependent CC domain to regulate autophagy
Yatao Chen1, Yuzhi Wang2, Tan Wang1
1Department of Biochemistry, School of Life Sciences, Nanjing Normal University, Nanjing, China.
Biochemical and Biophysical Research Communications
|October 25, 2023
Summary
Tripartite motif 21 (TRIM21) protein undergoes liquid-liquid phase separation, crucial for recruiting autophagy proteins to autophagosomes. This process mediated by TRIM21
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Tripartite motif (TRIM) family proteins function as E3-ligases in diverse biological processes.
- TRIM21, identified as the first autoantibody protein, has known associations with autophagy.
- The specific role of TRIM21 in mediating autophagy remains largely undefined.
Purpose of the Study:
- To elucidate the role of TRIM21 in the process of autophagy.
- To investigate the mechanism by which TRIM21 influences autophagosome formation and function.
- To determine the contribution of TRIM21's phase separation properties to its autophagic activity.
Main Methods:
- Observation of TRIM21 puncta formation in cellular cytoplasm.
- In vitro analysis of TRIM21 liquid-liquid phase separation.
- Identification of the specific TRIM21 domain responsible for phase separation and protein recruitment.
Main Results:
- TRIM21 forms significant puncta within the cytoplasm.
- TRIM21 exhibits liquid-liquid phase separation capabilities in vitro.
- Phase separation of the coiled-coil (CC) domain of TRIM21 is essential for recruiting autophagy-related proteins to the autophagosome.
Conclusions:
- TRIM21 undergoes cytoplasmic phase separation, influencing autophagy.
- The coiled-coil domain of TRIM21 is critical for its phase separation-dependent role in autophagosome formation.
- TRIM21-mediated phase separation impacts autophagosome function and consequently affects cell fate.
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