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TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.

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Title: TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.
Authors: Jessica L Bell, Alena Malyukova, Jessica K Holien, Jessica Koach, Michael W Parker, Maria Kavallaris, Glenn M Marshall, Belamy B Cheung
Source: PLoS ONE, Vol 7, Iss 5, p e37470 (2012)
Publisher Information: Public Library of Science (PLoS), 2012.
Publication Year: 2012
Collection: LCC:Medicine
LCC:Science
Subject Terms: Medicine, Science
More Details: The TRIM family of proteins is distinguished by its tripartite motif (TRIM). Typically, TRIM proteins contain a RING finger domain, one or two B-box domains, a coiled-coil domain and the more variable C-terminal domains. TRIM16 does not have a RING domain but does harbour two B-box domains. Here we showed that TRIM16 homodimerized through its coiled-coil domain and heterodimerized with other TRIM family members; TRIM24, Promyelocytic leukaemia (PML) protein and Midline-1 (MID1). Although, TRIM16 has no classic RING domain, three-dimensional modelling of TRIM16 suggested that its B-box domains adopts RING-like folds leading to the hypothesis that TRIM16 acts as an ubiquitin ligase. Consistent with this hypothesis, we demonstrated that TRIM16, devoid of a classical RING domain had auto-polyubiquitination activity and acted as an E3 ubiquitin ligase in vivo and in vitro assays. Thus via its unique structure, TRIM16 possesses both heterodimerization function with other TRIM proteins and also has E3 ubiquitin ligase activity.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1932-6203
Relation: https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22629402/pdf/?tool=EBI; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0037470
Access URL: https://doaj.org/article/b159544ce93a4517aecfb916f003a6c6
Accession Number: edsdoj.b159544ce93a4517aecfb916f003a6c6
Database: Directory of Open Access Journals
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  Data: TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.
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  Data: <searchLink fieldCode="AR" term="%22Jessica+L+Bell%22">Jessica L Bell</searchLink><br /><searchLink fieldCode="AR" term="%22Alena+Malyukova%22">Alena Malyukova</searchLink><br /><searchLink fieldCode="AR" term="%22Jessica+K+Holien%22">Jessica K Holien</searchLink><br /><searchLink fieldCode="AR" term="%22Jessica+Koach%22">Jessica Koach</searchLink><br /><searchLink fieldCode="AR" term="%22Michael+W+Parker%22">Michael W Parker</searchLink><br /><searchLink fieldCode="AR" term="%22Maria+Kavallaris%22">Maria Kavallaris</searchLink><br /><searchLink fieldCode="AR" term="%22Glenn+M+Marshall%22">Glenn M Marshall</searchLink><br /><searchLink fieldCode="AR" term="%22Belamy+B+Cheung%22">Belamy B Cheung</searchLink>
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  Data: PLoS ONE, Vol 7, Iss 5, p e37470 (2012)
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  Data: The TRIM family of proteins is distinguished by its tripartite motif (TRIM). Typically, TRIM proteins contain a RING finger domain, one or two B-box domains, a coiled-coil domain and the more variable C-terminal domains. TRIM16 does not have a RING domain but does harbour two B-box domains. Here we showed that TRIM16 homodimerized through its coiled-coil domain and heterodimerized with other TRIM family members; TRIM24, Promyelocytic leukaemia (PML) protein and Midline-1 (MID1). Although, TRIM16 has no classic RING domain, three-dimensional modelling of TRIM16 suggested that its B-box domains adopts RING-like folds leading to the hypothesis that TRIM16 acts as an ubiquitin ligase. Consistent with this hypothesis, we demonstrated that TRIM16, devoid of a classical RING domain had auto-polyubiquitination activity and acted as an E3 ubiquitin ligase in vivo and in vitro assays. Thus via its unique structure, TRIM16 possesses both heterodimerization function with other TRIM proteins and also has E3 ubiquitin ligase activity.
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