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Phosphorylation01:02

Phosphorylation

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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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Phosphorylation01:02

Phosphorylation

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ATP Energy Storage and Release01:31

ATP Energy Storage and Release

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ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
One example of energy coupling using ATP involves a...
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ATP Energy Storage and Release01:31

ATP Energy Storage and Release

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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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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Related Experiment Video

Updated: Mar 13, 2026

Chemical Triphosphorylation of Oligonucleotides
13:19

Chemical Triphosphorylation of Oligonucleotides

Published on: June 2, 2022

4.2K

Protein pyrophosphorylation: moving forward.

Adolfo Saiardi1

  • 1Medical Research Council Laboratory for Molecular Cell Biology, University College London, Gower Street, London WC1E 6BT, U.K.

The Biochemical Journal
|October 30, 2016
PubMed
Summary

Inositol pyrophosphates regulate cell transport by modifying the dynein motor protein. This post-translational modification, serine pyrophosphorylation, controls how dynein interacts with vesicles, impacting intracellular membrane trafficking.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Inositol pyrophosphates are crucial molecules in eukaryotic cells.
  • Previous studies established their importance but lacked detailed mechanistic insights into their regulatory roles.
  • Understanding the signaling pathways involving inositol pyrophosphates is essential for cell biology.

Purpose of the Study:

  • To investigate the role of inositol pyrophosphates in regulating intracellular vesicular movement.
  • To elucidate the mechanism by which inositol pyrophosphates control membrane trafficking.
  • To characterize the post-translational modification of dynein subunits.

Main Methods:

  • Integration of multiple experimental approaches, including cell biology and biochemistry.

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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Oligopeptide Competition Assay for Phosphorylation Site Determination

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Last Updated: Mar 13, 2026

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Screening for Thermotoga maritima Membrane-Bound Pyrophosphatase Inhibitors
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  • Analysis of serine pyrophosphorylation of dynein 1 intermediate chain 2.
  • Investigation of the interaction between dynein, dynactin, and vesicles.

    • Main Results:

    • Inositol pyrophosphates regulate intracellular vesicular transport along microtubules.
    • The motor protein complex dynein is involved in this regulated transport.
    • Serine pyrophosphorylation of dynein 1 intermediate chain 2, a process driven by inositol pyrophosphates, modulates its interaction with dynactin.
    • This interaction is critical for recruiting the dynein motor to vesicles, thereby controlling membrane trafficking.

    Conclusions:

    • Inositol pyrophosphates play a critical role in intracellular membrane trafficking by regulating the dynein motor complex.
    • Serine pyrophosphorylation of dynein subunits is a key mechanism through which inositol pyrophosphates exert their control.
    • This study highlights the significance of serine pyrophosphorylation as an underappreciated post-translational modification in cellular processes.