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Molecular basis for the fold organization and sarcomeric targeting of the muscle atrogin MuRF1
Institute of Integrative Biology, University of Liverpool, Biosciences Building, Liverpool, UK.
Institut für Anästhesiologie und Operative Intensivmedizin, Universitätsklinikum Mannheim, Mannheim, Germany.
Instituto de Biología Molecular de Barcelona, Barcelona Science Park, Barcelona, Spain.
Center for Cellular Imaging and Nanoanalytics (C-CINA), Biozentrum, University of Basel, Basel, Switzerland.
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2014 (English)In: Open Biology, ISSN 2046-2441, E-ISSN 2046-2441, Vol. 4, article id 130172Article in journal (Refereed) Published
Abstract [en]

MuRF1 is an E3 ubiquitin ligase central to muscle catabolism. It belongs to the TRIM protein family characterized by a tripartite fold of RING, B-box and coiled-coil (CC) motifs, followed by variable C-terminal domains. The CC motif is hypothesized to be responsible for domain organization in the fold as well as for high-order assembly into functional entities. But data on CC from this family that can clarify the structural significance of this motif are scarce. We have characterized the helical region from MuRF1 and show that, contrary to expectations, its CC domain assembles unproductively, being the B2- and COS-boxes in the fold (respectively flanking the CC) that promote a native quaternary structure. In particular, the C-terminal COS-box seemingly forms an α-hairpin that packs against the CC, influencing its dimerization. This shows that a C-terminal variable domain can be tightly integrated within the conserved TRIM fold to modulate its structure and function. Furthermore, data from transfected muscle show that in MuRF1 the COS-box mediates the in vivo targeting of sarcoskeletal structures and points to the pharmacological relevance of the COS domain for treating MuRF1-mediated muscle atrophy.

Place, publisher, year, edition, pages
London, United Kingdom: The Royal Society Publishing , 2014. Vol. 4, article id 130172
Keyword [en]
COS-box, RBCC/TRIM fold, X-ray crystallography, ab initio modelling, coiled-coil, electron microscopy
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:liu:diva-143661DOI: 10.1098/rsob.130172ISI: 000333906500002PubMedID: 24671946Scopus ID: 2-s2.0-84900993019OAI: oai:DiVA.org:liu-143661DiVA, id: diva2:1165098
Available from: 2017-12-12 Created: 2017-12-12 Last updated: 2018-01-26Bibliographically approved

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