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ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
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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.
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The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
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Phosphoinositides and PIPs01:42

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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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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Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
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Pom1 gradient buffering through intermolecular auto-phosphorylation.

Micha Hersch1, Olivier Hachet2, Sascha Dalessi1

  • 1Department of Medical Genetics, University of Lausanne, Lausanne, Switzerland Swiss Institute of Bioinformatics, Lausanne, Switzerland.

Molecular Systems Biology
|July 8, 2015
PubMed
Summary
This summary is machine-generated.

Robust Pom1 gradients in fission yeast are achieved through intermolecular auto-phosphorylation, providing stability against fluctuations. This autocatalysis mechanism buffers biological activities and ensures accurate cell division timing and placement.

Keywords:
auto‐catalysiscell cycle controlfission yeast Schizosaccharomyces pombegradient formationrobustness

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Area of Science:

  • Cell biology
  • Biochemistry
  • Systems biology

Background:

  • Concentration gradients are crucial for spatial organization in tissues.
  • In Schizosaccharomyces pombe, Pom1 kinase gradients regulate cell division timing and placement.
  • Pom1 gradients are formed by dephosphorylation and subsequent auto-phosphorylation at cell poles.

Purpose of the Study:

  • To investigate the mechanism underlying the robustness of Pom1 gradients.
  • To demonstrate that intermolecular auto-phosphorylation confers gradient stability.
  • To explore the implications of this mechanism for biological feedback systems.

Main Methods:

  • In vitro and in vivo biochemical assays to study Pom1 auto-phosphorylation.
  • Quantitative imaging techniques to analyze Pom1 gradient properties.
  • Theoretical modeling to predict and validate gradient formation dynamics.

Main Results:

  • Pom1 auto-phosphorylation occurs intermolecularly, both in vitro and in vivo.
  • Pom1 gradient amplitude is inversely correlated with its decay length.
  • The gradient is buffered against variations in Tea4 phosphatase levels.
  • A theoretical model accurately predicts these robustness properties.

Conclusions:

  • Intermolecular auto-phosphorylation is a key mechanism for robust Pom1 gradient formation in fission yeast.
  • This autocatalysis provides a simple feedback loop to buffer biological activities.
  • The findings exemplify gradient robustness through super-linear decay, achieved via autocatalysis.