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Related Concept Videos

ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

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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.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
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ATP Driven Pumps III: V-type Pumps01:30

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V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
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ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

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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.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
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ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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ATP Synthase: Structure01:18

ATP Synthase: Structure

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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Measuring In Vitro ATPase Activity for Enzymatic Characterization
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P2C-Type ATPases and Their Regulation.

Rocío Retamales-Ortega1, Carlos P Vio1,2,3, Nibaldo C Inestrosa4,5,6,7,8

  • 1Centro de Envejecimiento y Regeneración (CARE), Departamento de Biología Celular y Molecular, Santiago, Chile.

Molecular Neurobiology
|January 30, 2015
PubMed
Summary

P2C-type ATPases, including Na(+)/K(+)-ATPase and H(+)/K(+)-ATPase, are vital for cellular homeostasis and potassium regulation. Their dysfunction is linked to neurological diseases, highlighting their therapeutic potential.

Keywords:
Alzheimer’s diseaseH+/K+-ATPaseHypertensionNa+/K+-ATPasePotassium

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • P2C-type ATPases, specifically Na(+)/K(+)-ATPase and H(+)/K(+)-ATPase, are crucial ion transporters.
  • Na(+)/K(+)-ATPase is widely distributed and linked to neurological disorders, while H(+)/K(+)-ATPase is primarily in the colon, stomach, and kidney.
  • These ATPases, composed of α and β subunits, with Na(+)/K(+)-ATPase also featuring the FXYD regulatory subunit, are essential for maintaining cellular gradients and homeostasis.

Purpose of the Study:

  • To elucidate the functions, isoforms, and tissue localization of P2C-type ATPases.
  • To explore modulators affecting P2C-type ATPase activity.
  • To discuss the implications of P2C-type ATPases in various diseases, particularly neurological disorders.

Main Methods:

  • Literature review and synthesis of existing research on P2C-type ATPases.
  • Analysis of the roles of Na(+)/K(+)-ATPase and H(+)/K(+)-ATPase in physiological and pathological conditions.
  • Examination of the impact of modulators like lithium and ouabain on ATPase activity.

Main Results:

  • Na(+)/K(+)-ATPase is implicated in numerous neurological conditions including bipolar disorder, depression, and Alzheimer's disease.
  • H(+)/K(+)-ATPase plays a key role in regulating acidosis and potassium deficiencies.
  • Lithium exhibits neuroprotective effects against ouabain but can negatively impact H(+)/K(+)-ATPase at high concentrations.

Conclusions:

  • P2C-type ATPases are critical for maintaining potassium homeostasis through renal and extrarenal mechanisms.
  • Dysregulation of these ATPases contributes to the pathophysiology of diverse diseases.
  • Further research into P2C-type ATPases and their modulators may offer novel therapeutic strategies.