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Related Concept Videos

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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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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Microtubule Instability02:17

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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated...
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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.
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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Destabilization of Microtubules01:45

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The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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Mechanical Protein Functions

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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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Reconstitution of Msp1 Extraction Activity with Fully Purified Components
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Torsin ATPases: Harnessing Dynamic Instability for Function.

Anna R Chase1, Ethan Laudermilch1, Christian Schlieker1,2

  • 1Department of Molecular Biophysics and Biochemistry, Yale UniversityNew Haven, CT, USA.

Frontiers in Molecular Biosciences
|May 30, 2017
PubMed
Summary
This summary is machine-generated.

Torsins are vital AAA+ proteins involved in cellular functions. Their dynamic interaction with cofactors is crucial for nuclear transport and may explain DYT1 dystonia.

Keywords:
AAA+ proteinsDYT1 dystoniaTorsinAdystonic disordersnuclear membranenuclear pore complexprotein quality controlubiquitin

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Medicine

Background:

  • Torsins are essential AAA+ proteins located in the endoplasmic reticulum and perinuclear space.
  • They play roles in various cellular functions, with recent discoveries shedding light on their mechanisms.
  • Torsins are related to Clp/HSP100 proteins but have distinct features, including weaker ATPase activity regulated by cofactors.

Purpose of the Study:

  • To explore the structural and functional details of Torsins and their cofactors.
  • To understand the role of Torsin-cofactor interplay in cellular processes and disease.
  • To propose models for Torsin complex formation and function based on their dynamic nature.

Main Methods:

  • Comparative analysis of Torsin and Clp/HSP100 protein structures and functions.
  • Investigation of Torsin ATPase activity and its regulation by cofactors.
  • Hypothesizing Torsin function based on structural distinctions and cofactor interactions.

Main Results:

  • Torsins exhibit weak ATPase activity tightly controlled by accessory cofactors.
  • TorsinA, implicated in DYT1 dystonia, shows altered Torsin-cofactor interplay.
  • TorsinA lacks conserved aromatic pore loops found in Clp/HSP100 proteins.

Conclusions:

  • The dynamic assembly and disassembly of the Torsin/cofactor system are critical for Torsin function.
  • This dynamic system is likely essential for nuclear trafficking and nuclear pore complex homeostasis.
  • Further research into Torsin-cofactor interactions will enhance understanding of DYT1 dystonia.