Related Experiment Video

Updated: Jan 6, 2026

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
07:35

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess

Published on: June 1, 2022

2.5K

Intramolecular regulation of the MT-severing enzyme Katanin prevents futile ATP hydrolysis

Nicolas Joly1, Lionel Pintard1

  • 1Université Paris Cité, CNRS, Institut Jacques Monod , Paris, France.

The Journal of Cell Biology
|November 19, 2025
PubMed

Insights

Microtubule-severing enzymes like Katanin are regulated by a key N-terminal domain on MEI-1. This domain controls ATP hydrolysis and interaction with microtubules, ensuring proper cellular function and preventing wasteful energy use.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Microtubule-severing enzymes are AAA-ATPases crucial for cellular processes.
  • The mechanism coupling microtubule binding to ATP hydrolysis in these enzymes is unclear.

Purpose of the Study:

  • To investigate the regulatory role of the N-terminal domain of MEI-1 in Caenorhabditis elegans Katanin.
  • To elucidate the mechanism of Katanin activation and its coupling to microtubule binding.

Main Methods:

  • Utilized Caenorhabditis elegans Katanin (MEI-1 and MEI-2 subunits).
  • Investigated the function of MEI-1's N-terminal domain through biochemical assays and mutational analysis.

Main Results:

  • The N-terminal domain of MEI-1 represses the AAA+ core, limiting ATP hydrolysis and tubulin interaction without MEI-2.
  • MEI-1 lacking its N terminus is constitutively active, revealing critical pore residues for sensing microtubule C-terminal tails.
  • Identified a mechanism coupling Katanin activation to microtubule binding, preventing futile ATP hydrolysis.

Conclusions:

  • Katanin regulation involves the N-terminal domain of MEI-1 acting in cis.
  • This regulation ensures Katanin activation is dependent on microtubule binding.
  • Findings provide a framework for Katanin regulation in other organisms and have implications for diseases like neurodegeneration and cancer.

More Related Videos

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins07:25

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

Published on: October 17, 2014

15.9K
Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography10:39

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

30.8K

Related Concept Videos

ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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...
16.5K
Destabilization of Microtubules01:45

Destabilization of Microtubules

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...
3.4K
ATP Synthase: Structure01:18

ATP Synthase: Structure

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...
14.9K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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...
6.4K
The Electron Transport Chain01:30

The Electron Transport Chain

The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
19.5K
Energy to Drive Translocation01:37

Energy to Drive Translocation

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...
2.6K