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ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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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.
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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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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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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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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
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Measuring In Vitro ATPase Activity for Enzymatic Characterization
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The AAA+ ATPase p97, a cellular multitool.

Lasse Stach1, Paul S Freemont2

  • 1Section of Structural Biology, Department of Medicine, Imperial College London, London, U.K.

The Biochemical Journal
|August 19, 2017
PubMed
Summary
This summary is machine-generated.

The AAA+ ATPase p97 protein is crucial for cellular functions and is regulated by ubiquitination. Its dysfunction causes disease, and inhibiting p97 shows promise for cancer therapy.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The AAA+ ATPase p97 (also known as valosin-containing protein) is a key regulator of diverse cellular processes, including protein degradation, membrane fusion, and immune signaling.
  • p97 functions downstream of ubiquitination, utilizing ATP hydrolysis to remodel protein complexes and extract substrates.
  • Numerous cofactors bind p97, mediating substrate recognition and facilitating its enzymatic activity.

Purpose of the Study:

  • To review the cellular functions regulated by p97.
  • To describe the mechanisms of p97 cofactor interactions with substrates.
  • To discuss the implications of p97 mutations in disease and the therapeutic potential of p97 inhibitors in cancer.

Main Methods:

  • Literature review of studies on p97 function, cofactors, and inhibitors.
  • Analysis of the role of p97 in various cellular pathways.
  • Examination of the therapeutic strategies targeting p97.

Main Results:

  • p97 is essential for endoplasmic reticulum-associated degradation, membrane fusion, NF-κB activation, and chromatin remodeling.
  • Bi-functional cofactors containing ubiquitin-interacting and p97-binding domains are critical for p97 substrate recruitment.
  • Mutations in p97 are linked to multisystem proteinopathies, and p97 inhibition is a promising anti-cancer strategy.

Conclusions:

  • p97 plays a vital role in maintaining cellular homeostasis and is implicated in human diseases.
  • Understanding p97 enzymology and cofactor interactions is crucial for developing targeted therapies.
  • p97 inhibitors represent a potential therapeutic avenue for treating certain cancers by inducing proteotoxic stress.