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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.
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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

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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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ATP Driven Pumps II: P-type Pumps01:34

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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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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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ATP Driven Pumps I: An Overview01:27

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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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Coordinated conformational changes in the V1 complex during V-ATPase reversible dissociation.

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Vacuolar-type ATPases (V-ATPases) regulate cell acidification. Subunit C

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Vacuolar-type ATPases (V-ATPases) are essential rotary enzymes for intracellular acidification in eukaryotes.
  • These enzymes comprise a cytoplasmic V1 domain (ATP hydrolysis) and a membrane-bound VO domain (proton transport).
  • V-ATPase activity is regulated by reversible dissociation of V1 and VO, leading to autoinhibition and subunit detachment.

Purpose of the Study:

  • To elucidate the structural mechanism of V-ATPase reassembly.
  • To investigate the role of subunit C in V-ATPase assembly and regulation.
  • To understand how the regulator of the ATPase of vacuoles and endosomes (RAVE) complex mediates V1-VO reassembly.

Main Methods:

  • Cryogenic-electron microscopy (cryo-EM) of yeast V-ATPase.
  • Structural determination of intact V-ATPase, dissociated V1 complex, and V1 complex lacking subunit C.

Main Results:

  • V1 undergoes significant conformational changes upon dissociation from VO, altering its rotational state for reassembly.
  • The absence of subunit C in the V1 complex enables it to adopt a rotational state compatible with VO reassembly.
  • These findings suggest a model where RAVE facilitates V1-VO reassembly by recruiting subunit C.

Conclusions:

  • Subunit C plays a critical role in regulating the rotational state of the V1 domain for proper V-ATPase assembly.
  • The structural rearrangements observed provide insights into the dynamic regulation of V-ATPase function.
  • This study proposes a mechanism for RAVE-mediated V-ATPase reassembly involving subunit C recruitment.