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Related Concept Videos

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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Energy to Drive Translocation01:37

Energy to Drive Translocation

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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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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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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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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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Updated: May 5, 2026

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
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In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

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Tau binds ATP and induces its aggregation.

Mina Farid1, Christopher P Corbo, Alejandra Del C Alonso

  • 1Department of Biology and Center for Developmental Neuroscience, College of Staten Island and Graduate Center, The City University of New York, Staten Island, New York, 10314.

Microscopy Research and Technique
|November 22, 2013
PubMed
Summary
This summary is machine-generated.

Adenosine triphosphate (ATP) binding induces tau protein self-assembly into filaments, mimicking pathological structures found in Alzheimer's disease. This finding offers new insights into tauopathies and neurodegeneration mechanisms.

Keywords:
ATPfilamentsself-assemblytau

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Tau is a microtubule-associated protein crucial for neuronal structure and transport.
  • Tauopathies, neurodegenerative diseases, are linked to abnormal tau protein function.
  • Hyperphosphorylated tau aggregates are hallmarks of many tauopathies, but the exact toxicity mechanism is debated.

Purpose of the Study:

  • To investigate the role of ATP/GTP binding in tau protein behavior.
  • To determine if tau binds ATP or GTP and how this affects its self-assembly.
  • To explore the potential link between ATP-induced tau assembly and pathological filaments.

Main Methods:

  • Investigated tau protein's interaction with ATP and GTP using biochemical assays.
  • Analyzed tau self-assembly into filaments under varying ATP concentrations (1 mM and 10 mM).
  • Utilized non-hydrolyzable ATP analogs to assess the energy dependence of tau self-assembly.

Main Results:

  • Demonstrated that tau binds ATP, but not GTP.
  • Observed ATP-induced self-assembly of tau into filaments (4-7 nm width at 1 mM ATP).
  • Found that higher ATP concentrations (10 mM) promote filament bundling and twisting, resembling Paired Helical Filaments (PHF) seen in Alzheimer's disease brain. ATP-induced assembly was independent of ATP hydrolysis.

Conclusions:

  • Tau's N-terminal region binds ATP, initiating self-assembly into filaments.
  • ATP-induced tau filament formation recapitulates key structural features of pathological PHF.
  • This mechanism provides a novel perspective on tau's role in neurodegeneration and Alzheimer's disease pathogenesis.