Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies

Un Y.ung Choi; Won Y.oung Choi; Ji Y.eon Hur; Young Joon Kim

doi:10.1038/emm.2015.12

Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies

Un Y.ung Choi, Won Y.oung Choi, Ji Y.eon Hur, Young Joon Kim

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

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.

Original language	English
Pages (from-to)	e159
Journal	Experimental & molecular medicine
Volume	47
DOIs	https://doi.org/10.1038/emm.2015.12
Publication status	Published - 2015

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Medicine
Molecular Biology
Clinical Biochemistry

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title = "Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies",

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. ",

author = "Choi, {Un Y.ung} and Choi, {Won Y.oung} and Hur, {Ji Y.eon} and Kim, {Young Joon}",

year = "2015",

doi = "10.1038/emm.2015.12",

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journal = "Experimental and Molecular Medicine",

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AU - Choi, Un Y.ung

AU - Choi, Won Y.oung

AU - Hur, Ji Y.eon

AU - Kim, Young Joon

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

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SN - 1226-3613

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Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies

Abstract

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