TRIM16 Acts as an E3 Ubiquitin Ligase and Can Heterodimerize with Other TRIM Family Members
Autor: | Jessica Koach, Belamy B. Cheung, Jessica L. Bell, A Malyukova, Michael W. Parker, Jessica K. Holien, Maria Kavallaris, Glenn M. Marshall |
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Jazyk: | angličtina |
Rok vydání: | 2012 |
Předmět: |
Models
Molecular Protein Structure Science Ubiquitin-Protein Ligases Protein domain Biophysics Promyelocytic Leukemia Protein Transfection Biochemistry Protein Chemistry Cell Line Tripartite Motif Proteins Protein structure Ubiquitin Molecular Cell Biology Humans Protein Interactions Biology Cells Cultured Genetics Multidisciplinary biology Physics Tumor Suppressor Proteins Ubiquitination Proteins Computational Biology Nuclear Proteins Tripartite motif family Ubiquitin ligase Cell biology Protein Structure Tertiary RING finger domain DNA-Binding Proteins Oncology Computer Science biology.protein Microtubule Proteins Medicine TRIM Family Research Article Computer Modeling Transcription Factors |
Zdroj: | PLoS ONE PLoS ONE, Vol 7, Iss 5, p e37470 (2012) |
ISSN: | 1932-6203 |
Popis: | 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. |
Databáze: | OpenAIRE |
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