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Deregulated MYC activity is oncogenic and is deregulated in a large fraction of human cancers. Here the authors find that protein phosphatase 1 and its regulatory subunit PNUTS controls MYC stability and its interaction with chromatin.

BioID was performed using FlagBirA⁎ (the R118G biotin ligase mutant protein) and FlagBirA⁎-Myc in HEK293 T-REx cells maintained both under standard cell culture conditions and as mouse xenografts. The mass spectrometry dataset acquired in this study has been uploaded to the MassIVE repository with ID: MSV000078518, and consists of 28 ⁎.raw MS files acquired on an Orbitrap Velos instrument, collected in data-dependent mode. iProphet processed MS/MS search results are also included as a reference. This study has been published as “BioID identifies novel c-MYC interacting partners in cultured cells and xenograft tumors”, by Dingar et al. in the Journal of Proteomics, 2014 [1].

The c-MYC transcription factor is a master regulator of many cellular processes and deregulation of this oncogene has been linked to more than 50% of all cancers. This deregulation can take many forms, including altered post-translational regulation. Here, using immunoprecipitation combined with mass spectrometry, we identified a MYC SUMOylation site (K326). Abrogation of signaling through this residue by substitution with arginine (K326R) has no obvious effects on MYC half-life, intracellular localization, transcriptional targets, nor on the biological effects of MYC overexpression in two different cell systems assessed for soft agar colony formation, proliferation, and apoptosis. While we have definitively demonstrated that MYC SUMOylation can occur on K326, future work will be needed to elucidate the mechanisms and biological significance of MYC regulation by SUMOylation.

An advanced elective laboratory course is offered in order to help students leap the gap between undergraduate laboratory experience and the independent working environment in post graduate studies. The synthesis of room temperature ionic liquids and their application to Mannich reactions is a project-based experiment developed to be a part of advanced program which provides a opportunity for students to experience innovative ideas in chemical research.

The article describes the analysis of the enzymes implicated in the protein ubiquitination system in cells, with particular focus on deubiquitinating enzymes, or deubiquitinases (DUBs). Enzyme inhibitors were designed for DUBs such as ubiquitin-specific proteases (USPs), as well as ubiquitin-conjugating enzymes and ubiquitin ligases. Crystallography of the enzyme-inhibitors complexes indicated that enzyme activity was modulated by the use of different ubiquitin variants. The researchers also investigated ubiquitin-binding domain selectivity of various ubiquitin variants. It is suggested that the regulation of enzyme activity by ubiquitin variants would make them an effective genetic probe in drug discovery research.

The article discusses a study on the mannich reactions in room temperature ionic liquids (RTIL). The project which took 4 laboratory sessions to complete, involves several experimental works which includes the preparation of the RTIL 1-butyl-3-methyl-imidazolium tetrafluoroborate, [bmim][BF4]; the investigation of the effectiveness of [bmim][BF4] as a recyclable reaction medium for the Mannich reactions; and the spectroscopic characterization of the products of the reaction. This project offers students a great opportunity to work on a current research area and to experience research oriented work related to postgraduate studies.

An abstract of the article "Proteomic Profiling of the Human Cytomegalovirus UL35 Gene Products Reveals a Role for UL35 in the DNA Repair Response," by Jayme Salsman and colleagues is presented.