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Related Concept Videos

The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

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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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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.
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

ATP Driven Pumps III: V-type Pumps

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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: 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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The Proteasome Structure01:17

The Proteasome Structure

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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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Related Experiment Video

Updated: Mar 24, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
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Structure and function of the AAA+ ATPase p97/Cdc48p.

Di Xia1, Wai Kwan Tang1, Yihong Ye2

  • 1Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, United States.

Gene
|March 7, 2016
PubMed
Summary

p97 ATPase, also known as valosin-containing protein (VCP), is a conserved protein that disassembles cellular structures. It uses ATP hydrolysis to release proteins for degradation or recycling, acting as a key cellular chaperone.

Keywords:
AAA+ ATPaseChromatin-associated degradationER-associated degradationMembrane fusionMitochondria-associated degradationProteasomeProtein quality controlRibosome-associated degradationSegregaseUbiquitinUnfoldasep97/CDC48

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • p97/VCP/Cdc48p is an evolutionarily conserved ATPase found in eukaryotes and archaebacteria.
  • It functions as a molecular chaperone in conjunction with numerous cofactors and adaptors.
  • Its primary role involves modulating the stability of client proteins within the cell.

Purpose of the Study:

  • To review the current understanding of the structure and function of the p97 ATPase.
  • To highlight its role in protein homeostasis and cellular remodeling.
  • To provide insights into its mechanism of action in protein disaggregation.

Main Methods:

  • This review synthesizes existing research on p97/VCP/Cdc48p.
  • It integrates structural and functional data from various eukaryotic systems.
  • The review focuses on the mechanism of ATP-dependent protein disaggregation.

Main Results:

  • p97/VCP/Cdc48p utilizes ATP hydrolysis to segregate client proteins from cellular structures.
  • This process facilitates the degradation of ubiquitinated proteins via the proteasome.
  • It also enables the recycling of released polypeptides.

Conclusions:

  • p97/VCP/Cdc48p is an essential cellular machine for maintaining protein homeostasis.
  • Its ability to remodel protein complexes and organelles is critical for cell viability.
  • Further research into its structure-function relationship can reveal therapeutic targets.