Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies

Un Yung Choi; Won Young Choi; Ji Yeon Hur; Young Joon Kim

doi:10.1038/EMM.2015.12

Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies

Un Yung Choi, Won Young Choi, Ji Yeon 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
Article number	e159
Journal	Experimental and Molecular Medicine
Volume	47
Issue number	4
DOIs	https://doi.org/10.1038/EMM.2015.12
Publication status	Published - 2015 Apr

Bibliographical note

Funding Information:
This research was supported by the Global Research Laboratory Program of the National Research Foundation (NRF) funded by the Ministry of Science, ICT and Future Planning (MEST; K20705000006-12A0500-00610 to Y-JK), the Bio and Medical Technology Development Program of the National Research Foundation (NRF) funded by the Ministry of Science, ICT and Future Planning (MEST; 2012028272 to Y-JK), the Korea Health Technology R&D Project through the Korea Health Industry Development Institute (KHIDI), funded by the Ministry of Health and Welfare, Republic of Korea (grant number: HI13C08470200), the Introduced Innovative R&D Team Leadership of Guangdong Province, People’s Republic of China.

Publisher Copyright:
© 2015 KSBMB.

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Medicine
Molecular Biology
Clinical Biochemistry

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10.1038/EMM.2015.12

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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 Yung} and Choi, {Won Young} and Hur, {Ji Yeon} and Kim, {Young Joon}",

note = "Funding Information: This research was supported by the Global Research Laboratory Program of the National Research Foundation (NRF) funded by the Ministry of Science, ICT and Future Planning (MEST; K20705000006-12A0500-00610 to Y-JK), the Bio and Medical Technology Development Program of the National Research Foundation (NRF) funded by the Ministry of Science, ICT and Future Planning (MEST; 2012028272 to Y-JK), the Korea Health Technology R&D Project through the Korea Health Industry Development Institute (KHIDI), funded by the Ministry of Health and Welfare, Republic of Korea (grant number: HI13C08470200), the Introduced Innovative R&D Team Leadership of Guangdong Province, People{\textquoteright}s Republic of China. Publisher Copyright: {\textcopyright} 2015 KSBMB.",

year = "2015",

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doi = "10.1038/EMM.2015.12",

language = "English",

volume = "47",

journal = "Experimental and Molecular Medicine",

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AU - Choi, Un Yung

AU - Choi, Won Young

AU - Hur, Ji Yeon

AU - Kim, Young Joon

N1 - Funding Information: This research was supported by the Global Research Laboratory Program of the National Research Foundation (NRF) funded by the Ministry of Science, ICT and Future Planning (MEST; K20705000006-12A0500-00610 to Y-JK), the Bio and Medical Technology Development Program of the National Research Foundation (NRF) funded by the Ministry of Science, ICT and Future Planning (MEST; 2012028272 to Y-JK), the Korea Health Technology R&D Project through the Korea Health Industry Development Institute (KHIDI), funded by the Ministry of Health and Welfare, Republic of Korea (grant number: HI13C08470200), the Introduced Innovative R&D Team Leadership of Guangdong Province, People’s Republic of China. Publisher Copyright: © 2015 KSBMB.

PY - 2015/4

Y1 - 2015/4

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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Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies

Abstract

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