Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies
Experimental & Molecular Medicine
; : e159-2015.
Article
in Korean
| WPRIM (Western Pacific)
| ID: wpr-147141
Responsible library:
WPRO
ABSTRACT
Viral infection induces numerous tripartite motif (TRIM) proteins to control antiviral immune signaling and viral replication. Particularly, SPRY-containing TRIM proteins are found only in vertebrates and they control target protein degradation by their RING-finger and SPRY domains, and proper cytoplasmic localization. To understand TRIM30 function, we analyzed its localization pattern and putative roles of its RING-finger and SPRY domains. We found that TRIM30 is located in actin-mediated cytoplasmic bodies and produces colocalized ubiquitin chains in SPRY domain- and RING-finger domain-dependent ways that are degraded by autophagy and the proteasome. These results suggest a TRIM protein-dependent degradation mechanism by cytoplasmic body formation with actin networks.
Full text:
Available
Database:
WPRIM (Western Pacific)
Main subject:
Autophagy
/
Molecular Sequence Data
/
Cell Line
/
Inclusion Bodies
/
Amino Acid Sequence
/
Protein Transport
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Polyubiquitin
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Proteasome Endopeptidase Complex
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Intracellular Signaling Peptides and Proteins
/
RING Finger Domains
Limits:
Animals
Language:
Korean
Journal:
Experimental & Molecular Medicine
Year:
2015
Document type:
Article