Gerbracht, Jennifer V. ORCID: 0000-0002-3377-4649 and Gehring, Niels H. (2018). The exon junction complex: structural insights into a faithful companion of mammalian mRNPs. Biochem. Soc. Trans., 46. S. 153 - 162. LONDON: PORTLAND PRESS LTD. ISSN 1470-8752

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Abstract

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.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Gerbracht, Jennifer V.UNSPECIFIEDorcid.org/0000-0002-3377-4649UNSPECIFIED
Gehring, Niels H.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
URN: urn:nbn:de:hbz:38-195859
DOI: 10.1042/BST20170059
Journal or Publication Title: Biochem. Soc. Trans.
Volume: 46
Page Range: S. 153 - 162
Date: 2018
Publisher: PORTLAND PRESS LTD
Place of Publication: LONDON
ISSN: 1470-8752
Language: English
Faculty: Faculty of Mathematics and Natural Sciences
Divisions: Faculty of Mathematics and Natural Sciences > Department of Biology > Institute for Genetics
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
NONSENSE-MEDIATED DECAY; SPLICED MESSENGER-RNAS; CRYO-EM STRUCTURE; CORE COMPLEX; CRYSTAL-STRUCTURE; HELICASE ACTIVITY; EJC; REVEALS; TRANSLATION; EIF4AIIIMultiple languages
Biochemistry & Molecular BiologyMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/19585

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