Journal article

TRIM16 Acts as an E3 Ubiquitin Ligase and Can Heterodimerize with Other TRIM Family Members

Jessica L Bell, Alena Malyukova, Jessica K Holien, Jessica Koach, Michael W Parker, Maria Kavallaris, Glenn M Marshall, Belamy B Cheung

PLOS ONE | PUBLIC LIBRARY SCIENCE | Published : 2012

Abstract

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..

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Grants

Funding Acknowledgements

This work was supported by an Early Career Development Fellowship, Cancer Institute NSW (B. C.); National Health & Medical Research Council (NHMRC) and a Biomedical PhD Scholarship (J.B.). M. W. P. is an Australian Research Council Federation Fellow and an NHMRC Honorary Fellow and thanks the Victorian State Government Operational Infrastructure Support Program for support. M. K. is an NHMRC Senior Research Fellow. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.