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Related Concept Videos

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.
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Phosphorylation01:02

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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.
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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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Catching protein polyphosphorylation in the act.

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  • 1Center for Tropical and Emerging Global Diseases and Department of Cellular Biology, University of Georgia, Athens, Georgia 30602.

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|February 9, 2020
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Summary
This summary is machine-generated.

Lysine polyphosphorylation (K-PPn) is a new protein modification. Researchers developed a yeast model to detect authentic K-PPn, overcoming issues with sample handling and polyphosphatases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Yeast Genetics

Background:

  • Lysine polyphosphorylation (K-PPn) is an emerging post-translational modification.
  • The full range of K-PPn targets and functional impacts remain largely uncharacterized.
  • Studying endogenous K-PPn in yeast is challenging due to its nonenzymatic nature and susceptibility to artifacts during sample preparation.

Purpose of the Study:

  • To investigate the stability of K-PPn during protein extraction and sample handling.
  • To elucidate the mechanism underlying K-PPn.
  • To develop a reliable yeast model for detecting authentic endogenous K-PPn.

Main Methods:

  • Analysis of K-PPn modifications under various sample handling conditions.
  • Development of a novel yeast strain lacking vacuolar polyphosphate (polyP) and polyphosphatases.
  • Detection and characterization of K-PPn in the engineered yeast model.

Main Results:

  • Confirmed that K-PPn levels can be altered during standard sample handling procedures.
  • Gained new insights into the biochemical mechanisms driving K-PPn.
  • Successfully established a yeast model enabling the detection of authentic endogenous K-PPn.

Conclusions:

  • Sample handling critically affects the accurate assessment of K-PPn.
  • The developed yeast model provides a robust platform for future K-PPn research.
  • This work facilitates a deeper understanding of K-PPn's role in cellular processes.