Mass Spectrometry-Based Proteomics Technologies to Define Endogenous Protein-Protein Interactions and Their Applications to Cancer and Viral Infectious Diseases

An intricate network of protein assemblies and protein-protein interactions (PPIs) underlies nearly every biological process in living systems. The organization of these cellular networks is highly dynamic and intimately tied to the genomic and proteomic landscapes of a cell. Disruptions in normal P...

Full description

Saved in:
Bibliographic Details
Published inMass spectrometry reviews
Main Authors Yu, Clinton, Adavikolanu, Rithika, Kaake, Robyn M, Huang, Lan
Format Journal Article
LanguageEnglish
Published United States 09.02.2025
Subjects
Proximity Labeling Mass Spectrometry (PL‐MS)
protein‐protein interactions (PPIs)
virology
Co‐Fractionation Mass Spectrometry (CF‐MS)
Cross‐Linking Mass Spectrometry (XL‐MS)
protein footprinting
genome tagging
immunoprecipitation (IP)
Affinity Purification Mass Spectrometry (AP‐MS)
Cancer
Online AccessGet full text

Cover

More Information
Summary:An intricate network of protein assemblies and protein-protein interactions (PPIs) underlies nearly every biological process in living systems. The organization of these cellular networks is highly dynamic and intimately tied to the genomic and proteomic landscapes of a cell. Disruptions in normal PPIs can impair cellular functions and contribute to the development of human diseases. In recent years, targeting PPIs has emerged as an attractive strategy for drug discovery. Consequently, the identification and characterization of endogenous PPIs-those occurring naturally under physiological conditions-has become crucial for unraveling the molecular mechanisms driving human pathology and for laying the groundwork for novel diagnostics and therapeutics. Owing to numerous technological advancements, mass spectrometry (MS)-based proteomics has transformed the study of PPIs at the systems-level. This review focuses on proteomics approaches that enable the characterization of physiologically relevant endogenous interactions, spanning complex-centric to structure-centric analyses. Additionally, their applications to define native PPIs in the contexts of cancer and viral infectious diseases is highlighted.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
Clinton Yu; Affiliation: 1Department of Physiology & Biophysics, University of California, Irvine, Irvine, CA, 92697, USA.Rithika Adavikolanu; Affiliations: 2Department of Bioengineering, University of California, San Francisco, San Francisco, CA, 94158, USA. 3Quantitative Biosciences Institute (QBI), University of California, San Francisco, San Francisco, CA, 94158, USA. 3-J. David Gladstone Institutes, San Francisco, CA, 94158, USA.Robyn M. Kaake; Affiliations: 3Quantitative Biosciences Institute (QBI), University of California, San Francisco, San Francisco, CA, 94158, USA. 3-J. David Gladstone Institutes, San Francisco, CA, 94158, USA. 4Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA, 94158, USA.Lan Huang; Affiliation: 1Department of Physiology & Biophysics, University of California, Irvine, Irvine, CA, 92697, USA.
C.Y., R.M.K., and L.H. conceptualized the overall content. L.H. and R.M.K. directed the research. C.Y., R.A., and R.M.K. collected the references. C.Y. and R.M.K. generated the figures. C.Y. produced the table. All authors contributed to the writing and editing of the manuscript.
Author Contributions
Author Information
ISSN:1098-2787
0277-7037
1098-2787
DOI:10.1002/mas.21926