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Biological Roles of Non-Histone Protein Lysine Methylation
Submission Deadline: Apr. 30, 2016
Lead Guest Editor
Byron Baron
Centre for Molecular Medicine and Biobanking, Faculty of Medicine and Surgery, University of Malta, Marsaskala, Malta
Guest Editor
  • Byron Baron
    Centre for Molecular Medicine and Biobanking, Faculty of Medicine and Surgery, University of Malta, Marsaskala, Malta
Guidelines for Submission
Manuscripts can be submitted until the expiry of the deadline. Submissions must be previously unpublished and may not be under consideration elsewhere.
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Published Papers
The special issue currently is open for paper submission. Potential authors are humbly requested to submit an electronic copy of their complete manuscript by clicking here.
Proteins can undergo a number of post-translational modifications (PTMs), depending of the type of residue, and one of the more interesting and multi-faceted PTM is lysine methylation. Lysine methylation can alter protein stability and degradation, sub-cellular localisation, functionality of protein domains, or interaction strength with DNA, proteins or substrates. Although the most well-characterised lysine methylations tend to be on histones, this area of protein PTM is quickly expanding among non-histone proteins, particularly transcription factors. This is accepted as a further level of transcription factor regulation and reports of such modulations have provided crucial information for understanding some of the roles of lysine methylation. Though still in its infancy, the study of changes in the properties of proteins brought about by lysine methylation particularly in cellular contexts related to carcinogenesis, are gaining increasing attention. What has become evident in recent years is that lysine methylation can trigger unique protein functions and signal recognition, as has been shown through the blocking of particular interactors from binding or alternatively the creation new interaction settings, leading to completely new signals. The enzymes involved in the addition (protein lysine methyltransferases - PKMTs) and removal (protein lysine demethylases - PKDMs) of methyl groups on lysine, have been shown to display great specificity for the position and degree of methylation even for residues very close to each other on particular proteins. Moreover, while most of these enzymes also act on histones, there is a small sub-set that is unique to non-histone proteins. This special issue aims to improve the knowledge regarding the biochemical contexts and functions of lysine methylation. Original research papers are solicited in any aspect of lysine methylation.

Aims and Scope:
1.Identification of new target non-histone proteins of PKMTs and PKDMs
2.Cross-talk between lysine methylation and other PTMs
3.Clinical consequences of lysine methylation dysregulation
4.Elucidation of mechanisms by which lysine methylation affects transcription factor activity
5.Processes of carcinogenesis which involve lysine methylation
6.Evolutionary significance of PKMTs and PKDMs
7.Development and activity of methyltransferase inhibitors for drug therapies
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