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Related Concept Videos

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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ATP Synthase: Mechanism01:48

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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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Allosteric Proteins-ATCase01:19

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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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Energy to Drive Translocation01:37

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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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.
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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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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Related Experiment Video

Updated: Jun 28, 2025

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Human V-ATPase function is positively and negatively regulated by TLDc proteins.

Rebecca A Oot1, Stephan Wilkens1

  • 1Department of Biochemistry & Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.

Structure (London, England : 1993)
|April 9, 2024
PubMed
Summary

Human TLDc proteins impact vacuolar ATPase (V-ATPase) activity. Some inhibit V-ATPase by causing disassembly, while one activates it, revealing new insights into V-ATPase regulation and TLDc protein function.

Keywords:
NCOA7OXR1TBC1D24TLDC2TLDc domainV(1)-ATPaseV(o) proton channelV-ATPasemEAK7reversible disassembly

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Proteins with the conserved TLDc domain are crucial for cellular protection against oxidative stress and are linked to neurological health and disease.
  • The precise mechanisms by which TLDc proteins function remain largely unknown.
  • Previous studies showed yeast Oxr1p inhibits vacuolar ATPase (V-ATPase) by promoting its disassembly.

Purpose of the Study:

  • To investigate the direct impact of five human TLDc proteins (TLDC2, NCOA7, OXR1, TBC1D24, and mEAK7) on the activity of the human V-ATPase.
  • To elucidate the role of TLDc proteins in the regulation of V-ATPase function in mammals.

Main Methods:

  • Assaying the activity of purified human V-ATPase in the presence of different human TLDc proteins.
  • Analyzing the effect of TLDc proteins on V-ATPase assembly and disassembly using biochemical techniques.
  • Comparing the functional outcomes of TLDc protein interactions with V-ATPase.

Main Results:

  • TLDC2, TBC1D24, and the TLDc domains of OXR1 and NCOA7 were found to inhibit human V-ATPase activity by inducing enzyme disassembly.
  • Conversely, mEAK7 was identified as an activator of human V-ATPase activity.
  • These findings demonstrate differential regulation of V-ATPase by various human TLDc proteins.

Conclusions:

  • Mammalian TLDc proteins exhibit diverse regulatory effects on V-ATPase activity, including both inhibition and activation.
  • The study provides novel insights into the mechanisms of V-ATPase regulation by the TLDc protein family.
  • Understanding these interactions is critical for elucidating the role of TLDc proteins in neurological health and disease.