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Proximity labeling methods for proteomic analysis of membrane proteins

Zafra, Francisco, Piniella, Dolores·2022·Journal of Proteomics
DOI 10.1016/j.jprot.2022.104620
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Abstract

Membrane proteins constitute the filter that controls the cellular traffic of nutrients, ions and other essential molecules, as well as the transmission of signals across the membrane. These proteins interact with other proteins in the cytosol, cytoskeleton or the extracellular side of the membrane, giving rise to complex interactomes that are distributed throughout the various lipid microdomains of the membrane plane. In this manner, complex networks of protein-protein and protein-lipid interactions are formed which regulate the most diverse biological functions, and disturbance of these networks can lead to disease. Therefore, characterization of these interactomes is a priority for current biomedical sciences. Traditionally, such studies have largely depended on solubilization/dissociation of the essential components of multiprotein complexes with detergents of various strength. However, this technique may result in the loss of certain components of such complexes, especially those whose binding is weak or transient. Moreover, protein solubilization can lead to the formation of non-native spurious interactions. As an alternative, proximity labelling (PL) techniques have been developed in recent years that can identify interactors of the protein of interest in a native cellular environment, prior to solubilization. In this article, we review the recent advances in PL and explore the new possibilities they offer for the characterization of membrane interactomes. SIGNIFICANCE…

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Metadata

Authors
Zafra, F., & Piniella, D.
Venue
Journal of Proteomics
Publisher
Elsevier BV
Published
2022-07
Volume
264
Pages
104620
ISSN
1874-3919
DOI
10.1016/j.jprot.2022.104620
Cited by
22
References
8
Language
en
Licence
Funders
  • España Ministerio de Ciencia e Innovación (RTI2018-098712-B-100)
  • Ministerio de Ciencia e Innovación
  • Fundación Ramón Areces

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