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

@inproceedings{Bell2012TRIM16AA,
  title={TRIM16 Acts as an E3 Ubiquitin Ligase and Can Heterodimerize with Other TRIM Family Members},
  author={Jessica L. Bell and Alena Malyukova and Jessica K Holien and Jessica Koach and Michael W Parker and Maria Kavallaris and Glenn M. Marshall and Belamy B. Cheung},
  booktitle={PloS one},
  year={2012}
}
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… CONTINUE READING
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