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Related Concept Videos

Phosphorylation01:02

Phosphorylation

55.7K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Investigation of Macrophage Polarization Using Bone Marrow Derived Macrophages
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Selective phosphorylation during early macrophage differentiation.

Huoming Zhang1,2, Pei-Yuan Qian3, Timothy Ravasi1

  • 1Division of Biological and Environmental Sciences & Engineering, Division of Applied Mathematics and Computer Sciences, King Abdullah University of Science & Technology, Thuwal, Kingdom of Saudi Arabia.

Proteomics
|August 27, 2015
PubMed
Summary
This summary is machine-generated.

This study reveals key molecular changes during early macrophage differentiation using phosphoproteome profiling. It identifies potential targets for treating myeloid leukemias by understanding these dynamic cellular processes.

Keywords:
BiomedicineLeukemiaMonocyte-to-macrophage differentiationPhosphoproteome

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Area of Science:

  • Cellular Biology
  • Proteomics
  • Molecular Biology

Background:

  • Macrophage differentiation from monocytes is complex, with early stages poorly understood.
  • Existing studies lack detailed temporal insights into early differentiation mechanisms.

Purpose of the Study:

  • To comprehensively profile the phosphoproteome during early macrophage differentiation.
  • To identify key regulatory pathways and molecular players involved in this process.
  • To uncover potential therapeutic targets in leukemic cells.

Main Methods:

  • Utilized SILAC (Stable Isotope Labeling by Amino acids in Cell culture)-based quantitative proteomics.
  • Performed temporal phosphoproteome profiling to capture dynamic changes.
  • Analyzed phosphoprotein data to identify regulated pathways and regulators.

Main Results:

  • Identified a significant set of phosphoproteins regulated during early differentiation.
  • Revealed activation of transcriptional suppression, cytoskeletal reorganization, and cell adhesion pathways.
  • Highlighted key regulators including mTOR, MYB, STAT1, CTNNB, and E2F at different stages.

Conclusions:

  • Provides the first dynamic phosphoproteome map of myeloid cell differentiation.
  • Identifies critical regulators and pathways in early macrophage development.
  • Suggests potential molecular targets for therapeutic intervention in leukemia.