Proteomic analyses, which often aim to catalogue – to ever-increasing depths – all the proteins present in a particular biological sample, generate vast sets of data. Of course, these datasets are only useful if they are interrogated to extract meaningful information, which is not a trivial task. Proteomic data are usually interpreted on the basis of current knowledge, which is important to gain understanding in the context of the experiment. Still, proteomic approaches such as mass spectrometry lend themselves to the discovery of new insights into proteins.
My letter in today’s issue of the Journal of Proteomics argues that the interpretation of proteomic data should be open to the possibility of identifying unexpected functions or subcellular locations of proteins.
Such approaches to the analysis of the ever-increasing volume of large-scale datasets will likely lead to many new discoveries.
The correspondence provides a perspective on the biological interpretation of proteomic data and highlights RCC2, a molecule known to be involved in the cell cycle. A recent paper by Grigera et al. used proteomics to implicate the actin-binding protein cortactin in mitosis, which they report may be through its interaction with RCC2, although no functional evidence was provided. We have previously shown that RCC2 is a coordinator of adhesion signalling pathways, which acts to support effective spreading and directional migration of cells, processes known to be regulated by cortactin. The intriguing overlap between binding partners and functions of RCC2 calls for further investigation of the role of RCC2 in modulating cell behaviour.
The Journal of Proteomics letter was originally published online on 9 May 2012.
Funding: This work was supported by the Wellcome Trust.
Citation: A Byron, JD Humphries, MJ Humphries, Alternative cellular roles for proteins identified using proteomics. J. Proteomics 75, 4184-4185 (2012). DOI | PMID
Adam Byron 