During splicing, the exon junction complex (EJC) is deposited upstream of exon-exon boundaries. The EJC and its peripheral bound proteins play an essential role in mediating mRNA export, translation and turnover. However, the exact sequence of EJC assembly and the involved factors during splicing remain elusive. Recently published structures of the human C* spliceosome clarified the position of the EJC at this phase of splicing and have given insight into previously unidentified interactions between the EJC and spliceosomal proteins. Here, these new observations are presented and the significance for EJC assembly is discussed. Furthermore, the vast landscape of EJC interacting proteins and their manifold functions are described. Finally, the factors involved in EJC disassembly and recycling are recapitulated. This review aims to integrate structural, biochemical and physiological data to obtain a comprehensive picture of EJC components during the lifetime of the EJC.
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February 2018
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Cover Image
Cover Image
In this issue of Biochemical Society Transactions, Elliott and Jones review some of the techniques used to prepare, measure and analyse the electron transfer properties of metalloproteins, concentrating on scanning tunnelling microscopy-based techniques and advances in attachment of proteins to electrodes. The cover image, taken from Figure 2 in the review, shows the direct attachment of a protein (cytochrome b562) to gold substrate through an engineered cysteine residue. For further information see pages 1–9.
Review Article|
January 19 2018
The exon junction complex: structural insights into a faithful companion of mammalian mRNPs
Biochem Soc Trans (2018) 46 (1): 153–161.
Article history
Received:
November 06 2017
Revision Received:
December 13 2017
Accepted:
December 18 2017
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