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The year 2014 marks the 50th anniversary of the discovery of protein acetylation. In this Timeline article, Verdin and Ott discuss the identification of this modification, of its regulatory enzymes and of the roles of acetylation in transcription and other cellular processes, and provide an outlook on the future of the field.
The subcellular localization of mRNAs enables the spatial regulation of protein translation and generates functional and structural asymmetries in cells. New imaging (and other) techniques for tracking single-mRNA dynamics have unravelled mechanisms of mRNA movements and localization patterns in various cell types.
Post-translational modification of proteins by NEDD8 has been mainly characterized in terms of the cullin–RING E3 ligase family. However, recent studies have indicated that there might be non-cullin neddylation targets that require further verification.
Intrinsically disordered proteins (IDPs) are key components of the cellular signalling machinery. Their flexible conformation enables them to interact with different partners and to participate in the assembly of signalling complexes and membrane-less organelles; this leads to different cellular outcomes. Post-translational modification of IDPs and alternative splicing add complexity to regulatory networks.
Five papers report extensive transcriptomic, epigenomic and proteomic analyses of reprogramming, revealing the existence of several reprogramming routes and multiple unique pluripotent cell states.
The signal recognition particle (SRP) interacts with nascent polypeptides and assists protein translocation across membranes. Pechmannet al. identified that downstream non-optimal codons in the mRNA attenuate translation and promote SRP binding.
Lys and Arg methylation on non-histone proteins regulates various signalling pathways, and its crosstalk with other post-translational modifications and with histone methylation affects cellular processes such as transcription and DNA damage repair. Advances in proteomics now allow us to decode the methylproteome and elucidate its functions.
Faithful chromosome segregation during mitosis depends on the bi-oriented attachment of chromosomes to spindle microtubules through their kinetochores. The precise regulation of kinetochore–microtubule attachment that ensures error-free mitosis may be explained by homeostatic principles involving receptors, a core control network, effectors and feedback control.
New insights into how iron–sulphur (Fe–S) clusters are incorporated into proteins, particularly the discovery of a role for Leu-Tyr-Arg motifs in Fe–S recipient proteins, are shedding light on the fundamental roles of Fe–S proteins in mammalian cells.
