My paper has been published in the current issue of the journal Proteomics. The paper also makes the cover of the issue, which is a special issue on the theme of Cancer Proteomics.

Proteomics cover, 2012, vol. 12 (no. 13) // Images by Adam Byron & Sue Craig // Reproduced with permission from Wiley-VCH Verlag GmbH & Co. KGaA

Proteomics cover, 2012, vol. 12 (no. 13)

Cancer is a multifactorial group of diseases, with various genetic and environmental factors contributing to disease. In terms of pathogenesis, cancer is driven by genetic mutations that change the way cells behave, resulting in uncontrolled and inappropriate cell growth. To understand the pathophysiology of cancer, it is important to attain an overall view of the mechanisms that cause or prevent disease. This concept is often referred to as systems biology, which is in contrast to reductionist approaches that examine the component molecules of a particular cell signalling pathway.

Proteomic approaches, utilising technologies such as mass spectrometry, can be used to analyse all proteins in a given system. This makes these methods well suited to the holistic study of biological systems. The current special issue of Proteomics focusses on how proteomics can be used to investigate cancer.

My paper uses mass spectrometry–based proteomics to analyse the proteins found in cell adhesion complexes. Many proteins interact to form these complexes, which serve to control how well cells adhere to each other and to the extracellular matrix that surrounds them. Adhesion complexes are associated with integrin adhesion receptors at the cell surface. Different integrins recruit distinct adhesion complexes to direct specific cell behaviour. The work in this paper details the differential recruitment of proteins and highlights patterns of enrichment of proteins to distinct adhesion complexes. Investigating how specific integrins recruit specific proteins to determine specific functional differences in cells will help us to understand how adhesion signalling is controlled and how cell adhesion events go wrong in disease states such as inflammation, fibrosis and cancer.

Many previously unreported components of adhesion complexes are identified in the proteomic datasets, and the cytoskeletal molecule myosin XVIIIA (MYO18A) is shown for the first time to localise to sites of active integrin in migrating cells. The paper demonstrates that the catalogues of adhesion complex proteomes can be effectively combined with bioinformatic data interrogation to identify new components of adhesion complexes with relevance to cell migration.

The paper is freely available as an OnlineOpen article, and the datasets are also available as a resource to aid further study of integrin receptor-specific adhesion signalling.

Funding: This work was supported by the Wellcome Trust, the Biotechnology and Biological Sciences Research Council and GlaxoSmithKline.

Citation: A Byron, JD Humphries, SE Craig, D Knight, MJ Humphries, Proteomic analysis of α4β1 integrin adhesion complexes reveals α-subunit-dependent protein recruitment. Proteomics 12, 2107-2114 (2012). DOI | PMID | Full text | Reprint

5 September 2012 //
Update: This post now includes an image of the cover of the special issue of Proteomics, which features data from the paper.

Citation: Cover Picture: Proteomics 12’13. Proteomics 12, NA (2012). DOI | PMID

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