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Related Concept Videos

Subcellular Fractionation01:32

Subcellular Fractionation

The homogenate obtained after cell lysis contains various membrane-bound organelles that can be further separated into pure fractions by subcellular fractionation. These isolates are used to study specific cellular components, analyze localized protein activity, and are even employed in diagnostics. Fractionation is typically achieved using centrifugation methods, the most common being density-gradient and differential centrifugation.
Differential Centrifugation
Differential centrifugation is...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

Updated: Jun 8, 2026

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
15:41

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 12, 2009

Subcellular phosphoproteomics.

Matthias Trost1, Gaëlle Bridon, Michel Desjardins

  • 1Institute for Research in Immunology and Cancer, Université de Montréal, P.O. Box 6128, Station Centre-ville, Montréal, Québec, Canada H3C 3J7.

Mass Spectrometry Reviews
|October 9, 2010
PubMed
Summary
This summary is machine-generated.

Subcellular phosphoproteomics combines cell fractionation and mass spectrometry to map protein phosphorylation sites within specific cellular compartments. This approach reveals the spatial regulation of phosphorylation, offering insights into protein function and cellular signaling pathways.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Proteomics

Background:

  • Protein phosphorylation is a key post-translational modification regulating protein function.
  • Sensitive detection methods and mass spectrometry have expanded the understanding of phosphoproteomes.
  • Phosphorylation is dynamically orchestrated by kinases and phosphatases within specific subcellular compartments.

Purpose of the Study:

  • To introduce the emerging field of subcellular phosphoproteomics.
  • To highlight the importance of spatial resolution in understanding phosphorylation regulation.
  • To review methods combining cell fractionation and mass spectrometry for phosphoproteomics.

Main Methods:

  • Subcellular fractionation techniques to isolate cellular compartments.
  • Enrichment methods for phosphopeptides.
  • Sensitive mass spectrometry for protein identification and quantification.

Main Results:

  • Identification of low-abundance phosphoproteins.
  • Unraveling the spatial distribution and regulation of protein phosphorylation.
  • Mapping phosphorylation dynamics across different subcellular locations.

Conclusions:

  • Subcellular phosphoproteomics provides critical spatio-temporal resolution for studying protein phosphorylation.
  • This approach is essential for understanding the intricate regulation of cellular signaling.
  • Future research will benefit from integrating subcellular fractionation with phosphoproteomic analyses.