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

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...

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Autores principales:	Jessica L Bell, Alena Malyukova, Jessica K Holien, Jessica Koach, Michael W Parker, Maria Kavallaris, Glenn M Marshall, Belamy B Cheung
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b159544ce93a4517aecfb916f003a6c6
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spelling	oai:doaj.org-article:b159544ce93a4517aecfb916f003a6c62021-11-18T07:17:55ZTRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.1932-620310.1371/journal.pone.0037470https://doaj.org/article/b159544ce93a4517aecfb916f003a6c62012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22629402/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The 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.Jessica L BellAlena MalyukovaJessica K HolienJessica KoachMichael W ParkerMaria KavallarisGlenn M MarshallBelamy B CheungPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 5, p e37470 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jessica L Bell Alena Malyukova Jessica K Holien Jessica Koach Michael W Parker Maria Kavallaris Glenn M Marshall Belamy B Cheung TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.
description	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.
format	article
author	Jessica L Bell Alena Malyukova Jessica K Holien Jessica Koach Michael W Parker Maria Kavallaris Glenn M Marshall Belamy B Cheung
author_facet	Jessica L Bell Alena Malyukova Jessica K Holien Jessica Koach Michael W Parker Maria Kavallaris Glenn M Marshall Belamy B Cheung
author_sort	Jessica L Bell
title	TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.
title_short	TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.
title_full	TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.
title_fullStr	TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.
title_full_unstemmed	TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.
title_sort	trim16 acts as an e3 ubiquitin ligase and can heterodimerize with other trim family members.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/b159544ce93a4517aecfb916f003a6c6
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TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.

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