Identification and Regulation of Multimeric Protein Complexes in Autophagy via SILAC-Based Mass Spectrometry Approaches

Methods Mol Biol. 2019:1880:341-357. doi: 10.1007/978-1-4939-8873-0_23.

Abstract

Mass spectrometry (MS)-based identification and characterization of protein complexes is becoming a prerequisite for in-depth biochemical analyses of intracellular processes. Here, we describe two state-of-the-art MS-based approaches to characterize protein-protein interactions and multi-protein complexes involved in autophagy in mammalian cells. The combination of affinity purification (AP)-MS, which identifies binary protein-protein interactions, with size-exclusion chromatography (SEC)-protein correlation profiling (PCP), which helps monitor protein complex assemblies, is a powerful tool to acquire a full overview of the interlinkage and regulation of novel multi-protein complexes that might play a role in autophagy.

Keywords: AP-MS; Autophagy; Macroautophagy; Mass spectrometry; Proteomics; SEC-PCP-SILAC; SILAC; Starvation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autophagy / drug effects
  • Autophagy / physiology*
  • Chromatography, Affinity / instrumentation
  • Chromatography, Affinity / methods
  • Chromatography, Gel / instrumentation
  • Chromatography, Gel / methods
  • Humans
  • MCF-7 Cells
  • Macrolides / pharmacology
  • Multiprotein Complexes / metabolism*
  • Protein Interaction Mapping / instrumentation
  • Protein Interaction Mapping / methods*
  • Protein Multimerization / physiology
  • Tandem Mass Spectrometry / instrumentation
  • Tandem Mass Spectrometry / methods*

Substances

  • Macrolides
  • Multiprotein Complexes
  • concanamycin A