Protein interactions study through proximity-labeling |
| |
Authors: | Benoît Béganton Isabelle Solassol Alain Mangé |
| |
Affiliation: | 1. IRCM, INSERM, Univ Montpellier, ICM, Montpellier, France;2. Department of Pathology and onco-biology, CHU Montpellier, Montpellier, France;3. Translational Research Unit, Montpellier Cancer Institute, Montpellier, France |
| |
Abstract: | Introduction: The proteome is a dynamic system in which protein-protein interactions play a crucial part in shaping the cell phenotype. However, given the current limitations of available technologies to describe the dynamic nature of these interactions, the identification of protein-protein interactions has long been a major challenge in proteomics. In recent years, the development of BioID and APEX, two proximity-tagging technologies, have opened-up new perspectives and have already started to change our conception of protein-protein interactions, and more generally, of the proteome. With a broad range of application encompassing health, these new technologies are currently setting milestones crucial to understand fine cellular mechanisms. Area covered: In this article, we describe both the recent and the more conventional available tools to study protein-protein interactions, compare the advantages and the limitations of these techniques, and discuss the recent advancements led by the proximity tagging techniques to refine our conception of the proteome. Expert opinion: The recent development of proximity labeling techniques emphasizes the growing importance of such technologies to decipher cellular mechanism. Although several challenges still need to be addressed, many fields can benefit from these tools and notably the detection of new therapeutic targets for patient care |
| |
Keywords: | APEX BioID mass spectrometry protein-protein interactions proximal labeling proximal labeling by complementation |
|
|