Tripartite motif (TRIM) proteins constitute one of the largest subfamilies of Really Interesting New Gene (RING) E3 ubiquitin ligases and contribute to the regulation of numerous cellular activities, including innate immune responses. The conserved TRIM harbours a RING domain that imparts E3 ligase activity to TRIM family proteins, whilst a variable C-terminal region can mediate recognition of substrate proteins. The knowledge of the structure of these multidomain proteins and the functional interplay between their constituent domains is paramount to understanding their cellular roles. To date, available structural information on TRIM proteins is still largely restricted to subdomains of many TRIMs in isolation. Nevertheless, applying a combination of structural, biophysical and biochemical approaches has recently allowed important progress to be made towards providing a better understanding of the molecular features that underlie the function of TRIM family proteins and has uncovered an unexpected diversity in the link between self-association and catalytic activity.
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February 2017
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Cover Image
Cover Image
The surface of the catalytic subunit of protein phosphatase PP1 (central 3D-structure) has many binding sites for regulatory proteins that are embedded in regulatory networks (coloured circles linked by lines). Please see pp. 89–99 for more information. Image provided by Mathieu Bollen.
Review Article|
February 15 2017
Structural determinants of TRIM protein function
Diego Esposito;
Diego Esposito
1Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
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Marios G. Koliopoulos;
Marios G. Koliopoulos
1Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
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Katrin Rittinger
1Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
Correspondence: Katrin Rittinger (katrin.rittinger@crick.ac.uk)
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Publisher: Portland Press Ltd
Received:
September 15 2016
Revision Received:
October 14 2016
Accepted:
October 24 2016
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society
2017
Biochem Soc Trans (2017) 45 (1): 183–191.
Article history
Received:
September 15 2016
Revision Received:
October 14 2016
Accepted:
October 24 2016
Citation
Diego Esposito, Marios G. Koliopoulos, Katrin Rittinger; Structural determinants of TRIM protein function. Biochem Soc Trans 8 February 2017; 45 (1): 183–191. doi: https://doi.org/10.1042/BST20160325
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